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Glycerol-3-Phosphate Dehydrogenase

2010-04-01T07:09:51Z

Indu Toora:

{{STRUCTURE_2r4e| PDB=2r4e | SCENE=Sandbox_189/Mynewscene/1 }}
'''Glycerol 3-Phosphate Dehydrogenase'''

Glycerol 3-phosphate dehydrogenase (GlpD) is a membrane bound enzyme in prokaryotes and in eukaryotes. Glycerol 3-Phosphate Dehydrogenase (GlpD) is an oxidoreductase enzyme which catalyzes the reduction in [http://en.wikipedia.org/wiki/File:Dihydroxyacetone_phosphate_to_glycerol_3-phosphate_en.svg reaction] of Dihydroxyacetone Phosphate to Glycerol 3-Phosphate, with NADH as the reductant. GlpD is involved in many cellular functions such as phospholipids biosynthesis, respiration and metabolism. <ref name="cellfunction">PubMed:18296637</ref>The GlpD is a dimer consisting of two subunits which contain the catabolite activator protein (CAP)-Domain,the flavin adenine dinucleotide(FAD)-Domain and a ubiquinone analogue, MD.

===Structure===

[[Image:FINAL.png|thumb|Glycerol 3-Phosphate Dehydrogenase]]

GlpD is a dimer that consists of two subunits; α and β. The GlpD structure also contains seven ligands; 1,3-Dihydroxyacetonephosphate (13P), β-Octylglucoside (βOG), 1,2-Ethanediol (EDO), Flavin-Adenine Dinucleotide (FAD), Imidazole (IMD), PO4 (Phosphate Ion) and N-(Tris(Hydroxymethyl)methyl)-3-Aminopropanesulfonic Acid (T3A). The active sites on GlpD are the Cap-Domain, FAD- Domain and a ubiquinone substrate analogue, menadione (MD).

<scene name='Sandbox_189/Cap_domain/1'>Cap-Binding Domain</scene>

The C-terminal CAP-Domain consists of negatively charged residues that are opposite in orientation to the positively charged residues of the FAD-Domain in the phospholipid membrane. The CAP-domain is responsible in gene transcription and helical turns.

<scene name='Sandbox_189/Fad/2'>FAD Active Site</scene>

The N-terminal FAD-Domain exists in each monomer subunit of GlpD and is embedded into the phospholipid membrane bilayer.Substrate binding occurs at this domain which causes a conformational change to the structure of the GlpD enzyme. The FAD-domain plays a major role in metabolism and energy synthesis.

===Function===

GlpD functions in the intracellular membrane of E. coli and in the inner-mitochondrial membrane of eukaryotes. In E. Coli, GlpD catalyzes and reduces the reaction of dihydroxyacetone phosphate to glycerol 3-phosphate in the [http://www.pnas.org/content/105/9/3280/F1.large.jpg glycerol metabolism pathway]. The binding of the substrate analogues (glyceraldehydes 3-phosphate, glyceric acid 2-phosphate and phosphoenolpyruvate, dihydroxyacetone phosphate)or UQ substrate analogues (2-n-heptyl-4-hydroxyquinoline N-oxide and menadione). The conformational change of the structure and resiudes of GlpD catalyzes many different metabolic reactions.

===Metabolic Pathways===

====Phosphoplipid Biosynthesis====

GlpD reduces dihydroxyacetone phosphate to glycerol 3-phosphate. Then the glycerol 3-phosphate is catalyzed by acyl transferase to 1-acylglyverol-3-phosphate, and then another acyl transferase catalyzes that to a phosphatidic acid. head groups are added to the phosphatidic acid to synthesize phospholipids.

====Glyceroneogenesis====

GlpD is also involved in the glyceroneogenesis pathway. By gluconeogenesis, phosphoenolpyruvate converts to dihydroxyacetone phosphate which is reduced by GlpD to glycerol 3-phosphate which then forms a backbone for the synthesis of triacylglycerol.

====Respiration====

The FAD-domain in GlpD plays a major role in the transport of electrons into the repiratory pathway. Glycerol 3-phosphate is oxidized to dihydroxyacetone phosphate with simultaneous reduction of of FAD to FADH2 occuring, and the electrons are transported to Ubiquinone, which are further transported to oxygen or nitrogen and into the respiratory pathway.

===Diseases===

GlpD is involved in diseases such as alzeheimer`s, muscle dystrophy, hyaline membrane diseases and many more.

===References===
<references />

<table style="background-color:#ffffc0" cellpadding="8" width="95%" border="0"><tr><td>Please do NOT make changes to this Sandbox until after April 23, 2010. Sandboxes 151-200 are reserved until then for use by the Chemistry 307 class at UNBC taught by Prof. [[User:Andrea Gorrell|Andrea Gorrell]].</td></tr>

Glycerol-3-Phosphate Dehydrogenase

2010-04-01T07:07:23Z

Indu Toora:

Glycerol-3-Phosphate Dehydrogenase

2010-04-01T07:05:17Z

Indu Toora:

{{STRUCTURE_2r4e| PDB=2r4e | SCENE=Sandbox_189/Mynewscene/1 }}
'''Glycerol 3-Phosphate Dehydrogenase'''

Glycerol 3-phosphate dehydrogenase (GlpD) is a membrane bound enzyme in prokaryotes and in eukaryotes. Glycerol 3-Phosphate Dehydrogenase (GlpD) is an oxidoreductase enzyme which catalyzes the reduction in [http://en.wikipedia.org/wiki/File:Dihydroxyacetone_phosphate_to_glycerol_3-phosphate_en.svg reaction] of Dihydroxyacetone Phosphate to Glycerol 3-Phosphate, with NADH as the reductant. GlpD is involved in many cellular functions such as phospholipids biosynthesis, respiration and metabolism. <ref name=”placeholder”>PubMed:18296637</ref>. The GlpD is a dimer consisting of two subunits which contain the catabolite activator protein (CAP)-Domain,the flavin adenine dinucleotide(FAD)-Domain and a ubiquinone analogue, MD.

===Structure===

[[Image:FINAL.png|thumb|Glycerol 3-Phosphate Dehydrogenase]]

GlpD is a dimer that consists of two subunits; α and β. The GlpD structure also contains seven ligands; 1,3-Dihydroxyacetonephosphate (13P), β-Octylglucoside (βOG), 1,2-Ethanediol (EDO), Flavin-Adenine Dinucleotide (FAD), Imidazole (IMD), PO4 (Phosphate Ion) and N-(Tris(Hydroxymethyl)methyl)-3-Aminopropanesulfonic Acid (T3A). The active sites on GlpD are the Cap-Domain, FAD- Domain and a ubiquinone substrate analogue, menadione (MD).

<scene name='Sandbox_189/Cap_domain/1'>Cap-Binding Domain</scene>

The C-terminal CAP-Domain consists of negatively charged residues that are opposite in orientation to the positively charged residues of the FAD-Domain in the phospholipid membrane. The CAP-domain is responsible in gene transcription and helical turns.

<scene name='Sandbox_189/Fad/2'>FAD Active Site</scene>

The N-terminal FAD-Domain exists in each monomer subunit of GlpD and is embedded into the phospholipid membrane bilayer.Substrate binding occurs at this domain which causes a conformational change to the structure of the GlpD enzyme. The FAD-domain plays a major role in metabolism and energy synthesis.

===Function===

GlpD functions in the intracellular membrane of E. coli and in the inner-mitochondrial membrane of eukaryotes. In E. Coli, GlpD catalyzes and reduces the reaction of dihydroxyacetone phosphate to glycerol 3-phosphate in the [http://www.pnas.org/content/105/9/3280/F1.large.jpg glycerol metabolism pathway]. The binding of the substrate analogues (glyceraldehydes 3-phosphate, glyceric acid 2-phosphate and phosphoenolpyruvate, dihydroxyacetone phosphate)or UQ substrate analogues (2-n-heptyl-4-hydroxyquinoline N-oxide and menadione). The conformational change of the structure and resiudes of GlpD catalyzes many different metabolic reactions.

===Metabolic Pathways===

====Phosphoplipid Biosynthesis====

GlpD reduces dihydroxyacetone phosphate to glycerol 3-phosphate. Then the glycerol 3-phosphate is catalyzed by acyl transferase to 1-acylglyverol-3-phosphate, and then another acyl transferase catalyzes that to a phosphatidic acid. head groups are added to the phosphatidic acid to synthesize phospholipids.

====Glyceroneogenesis====

GlpD is also involved in the glyceroneogenesis pathway. By gluconeogenesis, phosphoenolpyruvate converts to dihydroxyacetone phosphate which is reduced by GlpD to glycerol 3-phosphate which then forms a backbone for the synthesis of triacylglycerol.

====Respiration====

The FAD-domain in GlpD plays a major role in the transport of electrons into the repiratory pathway. Glycerol 3-phosphate is oxidized to dihydroxyacetone phosphate with simultaneous reduction of of FAD to FADH2 occuring, and the electrons are transported to Ubiquinone, which are further transported to oxygen or nitrogen and into the respiratory pathway.

===Diseases===

GlpD is involved in diseases such as alzeheimer`s, muscle dystrophy, hyaline membrane diseases and many more.

===References===
<references />

<table style="background-color:#ffffc0" cellpadding="8" width="95%" border="0"><tr><td>Please do NOT make changes to this Sandbox until after April 23, 2010. Sandboxes 151-200 are reserved until then for use by the Chemistry 307 class at UNBC taught by Prof. [[User:Andrea Gorrell|Andrea Gorrell]].</td></tr>

Glycerol-3-Phosphate Dehydrogenase

2010-04-01T07:00:18Z

Indu Toora:

Glycerol-3-Phosphate Dehydrogenase

2010-04-01T06:59:15Z

Indu Toora:

{{STRUCTURE_2r4e| PDB=2r4e | SCENE=Sandbox_189/Mynewscene/1 }}
'''Glycerol 3-Phosphate Dehydrogenase'''

Glycerol 3-phosphate dehydrogenase (GlpD) is a membrane bound enzyme in prokaryotes and in eukaryotes. Glycerol 3-Phosphate Dehydrogenase (GlpD) is an oxidoreductase enzyme which catalyzes the reduction in [http://en.wikipedia.org/wiki/File:Dihydroxyacetone_phosphate_to_glycerol_3-phosphate_en.svg reaction] of Dihydroxyacetone Phosphate to Glycerol 3-Phosphate, with NADH as the reductant. GlpD is involved in many cellular functions such as phospholipids biosynthesis, respiration and metabolism. <ref name="cellfunction">PubMed:18296637</ref>The GlpD is a dimer consisting of two subunits which contain the catabolite activator protein (CAP)-Domain,the flavin adenine dinucleotide(FAD)-Domain and a ubiquinone analogue, MD.

===Structure===

GlpD is a dimer that consists of two subunits; α and β. The GlpD structure also contains seven ligands; 1,3-Dihydroxyacetonephosphate (13P), β-Octylglucoside (βOG), 1,2-Ethanediol (EDO), Flavin-Adenine Dinucleotide (FAD), Imidazole (IMD), PO4 (Phosphate Ion) and N-(Tris(Hydroxymethyl)methyl)-3-Aminopropanesulfonic Acid (T3A). The active sites on GlpD are the Cap-Domain, FAD- Domain and a ubiquinone substrate analogue, menadione (MD).

<scene name='Sandbox_189/Cap_domain/1'>Cap-Binding Domain</scene>

The C-terminal CAP-Domain consists of negatively charged residues that are opposite in orientation to the positively charged residues of the FAD-Domain in the phospholipid membrane. The CAP-domain is responsible in gene transcription and helical turns.

<scene name='Sandbox_189/Fad/2'>FAD Active Site</scene>

The N-terminal FAD-Domain exists in each monomer subunit of GlpD and is embedded into the phospholipid membrane bilayer.Substrate binding occurs at this domain which causes a conformational change to the structure of the GlpD enzyme. The FAD-domain plays a major role in metabolism and energy synthesis.

===Function===

GlpD functions in the intracellular membrane of E. coli and in the inner-mitochondrial membrane of eukaryotes. In E. Coli, GlpD catalyzes and reduces the reaction of dihydroxyacetone phosphate to glycerol 3-phosphate in the [http://www.pnas.org/content/105/9/3280/F1.large.jpg glycerol metabolism pathway]. The binding of the substrate analogues (glyceraldehydes 3-phosphate, glyceric acid 2-phosphate and phosphoenolpyruvate, dihydroxyacetone phosphate)or UQ substrate analogues (2-n-heptyl-4-hydroxyquinoline N-oxide and menadione). The conformational change of the structure and resiudes of GlpD catalyzes many different metabolic reactions.

===Metabolic Pathways===

====Phosphoplipid Biosynthesis====

GlpD reduces dihydroxyacetone phosphate to glycerol 3-phosphate. Then the glycerol 3-phosphate is catalyzed by acyl transferase to 1-acylglyverol-3-phosphate, and then another acyl transferase catalyzes that to a phosphatidic acid. head groups are added to the phosphatidic acid to synthesize phospholipids.

====Glyceroneogenesis====

GlpD is also involved in the glyceroneogenesis pathway. By gluconeogenesis, phosphoenolpyruvate converts to dihydroxyacetone phosphate which is reduced by GlpD to glycerol 3-phosphate which then forms a backbone for the synthesis of triacylglycerol.

====Respiration====

The FAD-domain in GlpD plays a major role in the transport of electrons into the repiratory pathway. Glycerol 3-phosphate is oxidized to dihydroxyacetone phosphate with simultaneous reduction of of FAD to FADH2 occuring, and the electrons are transported to Ubiquinone, which are further transported to oxygen or nitrogen and into the respiratory pathway.

===Diseases===

GlpD is involved in diseases such as alzeheimer`s, muscle dystrophy, hyaline membrane diseases and many more.

===References===
<references />

[[Image:FINAL.png|thumb|Glycerol 3-Phosphate Dehydrogenase]]

<table style="background-color:#ffffc0" cellpadding="8" width="95%" border="0"><tr><td>Please do NOT make changes to this Sandbox until after April 23, 2010. Sandboxes 151-200 are reserved until then for use by the Chemistry 307 class at UNBC taught by Prof. [[User:Andrea Gorrell|Andrea Gorrell]].</td></tr>

Glycerol-3-Phosphate Dehydrogenase

2010-04-01T06:55:50Z

Indu Toora:

{{STRUCTURE_2r4e| PDB=2r4e | SCENE=Sandbox_189/Mynewscene/1 }}
'''Glycerol 3-Phosphate Dehydrogenase'''

Glycerol 3-phosphate dehydrogenase (GlpD) is a membrane bound enzyme in prokaryotes and in eukaryotes. Glycerol 3-Phosphate Dehydrogenase (GlpD) is an oxidoreductase enzyme which catalyzes the reduction in [http://en.wikipedia.org/wiki/File:Dihydroxyacetone_phosphate_to_glycerol_3-phosphate_en.svg reaction] of Dihydroxyacetone Phosphate to Glycerol 3-Phosphate, with NADH as the reductant. GlpD is involved in many cellular functions such as phospholipids biosynthesis, respiration and metabolism. The GlpD is a dimer consisting of two subunits which contain the catabolite activator protein (CAP)-Domain,the flavin adenine dinucleotide(FAD)-Domain and a ubiquinone analogue, MD.

===Structure===

GlpD is a dimer that consists of two subunits; α and β. The GlpD structure also contains seven ligands; 1,3-Dihydroxyacetonephosphate (13P), β-Octylglucoside (βOG), 1,2-Ethanediol (EDO), Flavin-Adenine Dinucleotide (FAD), Imidazole (IMD), PO4 (Phosphate Ion) and N-(Tris(Hydroxymethyl)methyl)-3-Aminopropanesulfonic Acid (T3A). The active sites on GlpD are the Cap-Domain, FAD- Domain and a ubiquinone substrate analogue, menadione (MD).

<scene name='Sandbox_189/Cap_domain/1'>Cap-Binding Domain</scene>

The C-terminal CAP-Domain consists of negatively charged residues that are opposite in orientation to the positively charged residues of the FAD-Domain in the phospholipid membrane. The CAP-domain is responsible in gene transcription and helical turns.

<scene name='Sandbox_189/Fad/2'>FAD Active Site</scene>

The N-terminal FAD-Domain exists in each monomer subunit of GlpD and is embedded into the phospholipid membrane bilayer.Substrate binding occurs at this domain which causes a conformational change to the structure of the GlpD enzyme. The FAD-domain plays a major role in metabolism and energy synthesis.

===Function===

GlpD functions in the intracellular membrane of E. coli and in the inner-mitochondrial membrane of eukaryotes. In E. Coli, GlpD catalyzes and reduces the reaction of dihydroxyacetone phosphate to glycerol 3-phosphate in the [http://www.pnas.org/content/105/9/3280/F1.large.jpg glycerol metabolism pathway]. The binding of the substrate analogues (glyceraldehydes 3-phosphate, glyceric acid 2-phosphate and phosphoenolpyruvate, dihydroxyacetone phosphate)or UQ substrate analogues (2-n-heptyl-4-hydroxyquinoline N-oxide and menadione). The conformational change of the structure and resiudes of GlpD catalyzes many different metabolic reactions.

===Metabolic Pathways===

====Phosphoplipid Biosynthesis====

GlpD reduces dihydroxyacetone phosphate to glycerol 3-phosphate. Then the glycerol 3-phosphate is catalyzed by acyl transferase to 1-acylglyverol-3-phosphate, and then another acyl transferase catalyzes that to a phosphatidic acid. head groups are added to the phosphatidic acid to synthesize phospholipids.

====Glyceroneogenesis====

GlpD is also involved in the glyceroneogenesis pathway. By gluconeogenesis, phosphoenolpyruvate converts to dihydroxyacetone phosphate which is reduced by GlpD to glycerol 3-phosphate which then forms a backbone for the synthesis of triacylglycerol.

====Respiration====

The FAD-domain in GlpD plays a major role in the transport of electrons into the repiratory pathway. Glycerol 3-phosphate is oxidized to dihydroxyacetone phosphate with simultaneous reduction of of FAD to FADH2 occuring, and the electrons are transported to Ubiquinone, which are further transported to oxygen or nitrogen and into the respiratory pathway.

===Diseases===

GlpD is involved in diseases such as alzeheimer`s, muscle dystrophy, hyaline membrane diseases and many more.

===References===
<references />

[[Image:FINAL.png|thumb|Glycerol 3-Phosphate Dehydrogenase]]

<table style="background-color:#ffffc0" cellpadding="8" width="95%" border="0"><tr><td>Please do NOT make changes to this Sandbox until after April 23, 2010. Sandboxes 151-200 are reserved until then for use by the Chemistry 307 class at UNBC taught by Prof. [[User:Andrea Gorrell|Andrea Gorrell]].</td></tr>

Glycerol-3-Phosphate Dehydrogenase

2010-04-01T06:50:02Z

Indu Toora:

{{STRUCTURE_2r4e| PDB=2r4e | SCENE=Sandbox_189/Mynewscene/1 }}
'''Glycerol 3-Phosphate Dehydrogenase'''

Glycerol 3-phosphate dehydrogenase (GlpD) is a membrane bound enzyme in prokaryotes and in eukaryotes. Glycerol 3-Phosphate Dehydrogenase (GlpD) is an oxidoreductase enzyme which catalyzes the reduction (in [http://en.wikipedia.org/wiki/File:Dihydroxyacetone_phosphate_to_glycerol_3-phosphate_en.svg reaction] of Dihydroxyacetone Phosphate to Glycerol 3-Phosphate, with NADH as the reductant. GlpD is involved in many cellular functions such as phospholipids biosynthesis, respiration and metabolism. The GlpD is a dimer consisting of two subunits which contain the catabolite activator protein (CAP)-Domain,the flavin adenine dinucleotide(FAD)-Domain and a ubiquinone analogue, MD.

===Structure===

GlpD is a dimer that consists of two subunits; α and β. The GlpD structure also contains seven ligands; 1,3-Dihydroxyacetonephosphate (13P), β-Octylglucoside (βOG), 1,2-Ethanediol (EDO), Flavin-Adenine Dinucleotide (FAD), Imidazole (IMD), PO4 (Phosphate Ion) and N-(Tris(Hydroxymethyl)methyl)-3-Aminopropanesulfonic Acid (T3A). The active sites on GlpD are the Cap-Domain, FAD- Domain and a ubiquinone substrate analogue, menadione (MD).

<scene name='Sandbox_189/Cap_domain/1'>Cap-Binding Domain</scene>

The C-terminal CAP-Domain consists of negatively charged residues that are opposite in orientation to the positively charged residues of the FAD-Domain in the phospholipid membrane. The CAP-domain is responsible in gene transcription and helical turns.

<scene name='Sandbox_189/Fad/2'>FAD Active Site</scene>

The N-terminal FAD-Domain exists in each monomer subunit of GlpD and is embedded into the phospholipid membrane bilayer.Substrate binding occurs at this domain which causes a conformational change to the structure of the GlpD enzyme. The FAD-domain plays a major role in metabolism and energy synthesis.

===Function===

GlpD functions in the intracellular membrane of E. coli and in the inner-mitochondrial membrane of eukaryotes. In E. Coli, GlpD catalyzes and reduces the reaction of dihydroxyacetone phosphate to glycerol 3-phosphate in the [http://www.pnas.org/content/105/9/3280/F1.large.jpg glycerol metabolism pathway]. The binding of the substrate analogues (glyceraldehydes 3-phosphate, glyceric acid 2-phosphate and phosphoenolpyruvate, dihydroxyacetone phosphate)or UQ substrate analogues (2-n-heptyl-4-hydroxyquinoline N-oxide and menadione). The conformational change of the structure and resiudes of GlpD catalyzes many different metabolic reactions.

===Metabolic Pathways===

====Phosphoplipid Biosynthesis====

GlpD reduces dihydroxyacetone phosphate to glycerol 3-phosphate. Then the glycerol 3-phosphate is catalyzed by acyl transferase to 1-acylglyverol-3-phosphate, and then another acyl transferase catalyzes that to a phosphatidic acid. head groups are added to the phosphatidic acid to synthesize phospholipids.

====Glyceroneogenesis====

GlpD is also involved in the glyceroneogenesis pathway. By gluconeogenesis, phosphoenolpyruvate converts to dihydroxyacetone phosphate which is reduced by GlpD to glycerol 3-phosphate which then forms a backbone for the synthesis of triacylglycerol.

====Respiration====

The FAD-domain in GlpD plays a major role in the transport of electrons into the repiratory pathway. Glycerol 3-phosphate is oxidized to dihydroxyacetone phosphate with simultaneous reduction of of FAD to FADH2 occuring, and the electrons are transported to Ubiquinone, which are further transported to oxygen or nitrogen and into the respiratory pathway.

===Diseases===

===References===
<references />

[[Image:FINAL.png|thumb|Glycerol 3-Phosphate Dehydrogenase]]

<table style="background-color:#ffffc0" cellpadding="8" width="95%" border="0"><tr><td>Please do NOT make changes to this Sandbox until after April 23, 2010. Sandboxes 151-200 are reserved until then for use by the Chemistry 307 class at UNBC taught by Prof. [[User:Andrea Gorrell|Andrea Gorrell]].</td></tr>

Glycerol-3-Phosphate Dehydrogenase

2010-04-01T06:49:12Z

Indu Toora:

{{STRUCTURE_2r4e| PDB=2r4e | SCENE=Sandbox_189/Mynewscene/1 }}
'''Glycerol 3-Phosphate Dehydrogenase'''

Glycerol 3-phosphate dehydrogenase (GlpD) is a membrane bound enzyme in prokaryotes and in eukaryotes. Glycerol 3-Phosphate Dehydrogenase (GlpD) is an oxidoreductase enzyme which catalyzes the reduction (in [http://en.wikipedia.org/wiki/File:Dihydroxyacetone_phosphate_to_glycerol_3-phosphate_en.svg reaction] of Dihydroxyacetone Phosphate to Glycerol 3-Phosphate, with NADH as the reductant. GlpD is involved in many cellular functions such as phospholipids biosynthesis, respiration and metabolism. The GlpD is a dimer consisting of two subunits which contain the catabolite activator protein (CAP)-Domain,the flavin adenine dinucleotide(FAD)-Domain and a ubiquinone analogue, MD.

===Structure===

GlpD is a dimer that consists of two subunits; α and β. The GlpD structure also contains seven ligands; 1,3-Dihydroxyacetonephosphate (13P), β-Octylglucoside (βOG), 1,2-Ethanediol (EDO), Flavin-Adenine Dinucleotide (FAD), Imidazole (IMD), PO4 (Phosphate Ion) and N-(Tris(Hydroxymethyl)methyl)-3-Aminopropanesulfonic Acid (T3A). The active sites on GlpD are the Cap-Domain, FAD- Domain and a ubiquinone substrate analogue, menadione (MD).

<scene name='Sandbox_189/Cap_domain/1'>Cap-Binding Domain</scene>

The C-terminal CAP-Domain consists of negatively charged residues that are opposite in orientation to the positively charged residues of the FAD-Domain in the phospholipid membrane. The CAP-domain is responsible in gene transcription and helical turns.

<scene name='Sandbox_189/Fad/2'>FAD Active Site</scene>

The N-terminal FAD-Domain exists in each monomer subunit of GlpD and is embedded into the phospholipid membrane bilayer.Substrate binding occurs at this domain which causes a conformational change to the structure of the GlpD enzyme. The FAD-domain plays a major role in metabolism and energy synthesis.

===Function===

GlpD functions in the intracellular membrane of E. coli and in the inner-mitochondrial membrane of eukaryotes. In E. Coli, GlpD catalyzes and reduces the reaction of dihydroxyacetone phosphate to glycerol 3-phosphate in the [http://www.pnas.org/content/105/9/3280/F1.large.jpg glycerol metabolism pathway]. The binding of the substrate analogues (glyceraldehydes 3-phosphate, glyceric acid 2-phosphate and phosphoenolpyruvate, dihydroxyacetone phosphate)or UQ substrate analogues (2-n-heptyl-4-hydroxyquinoline N-oxide and menadione). The conformational change of the structure and resiudes of GlpD catalyzes many different metabolic reactions.

====Phosphoplipid Biosynthesis====

GlpD reduces dihydroxyacetone phosphate to glycerol 3-phosphate. Then the glycerol 3-phosphate is catalyzed by acyl transferase to 1-acylglyverol-3-phosphate, and then another acyl transferase catalyzes that to a phosphatidic acid. head groups are added to the phosphatidic acid to synthesize phospholipids.

====Glyceroneogenesis====

GlpD is also involved in the glyceroneogenesis pathway. By gluconeogenesis, phosphoenolpyruvate converts to dihydroxyacetone phosphate which is reduced by GlpD to glycerol 3-phosphate which then forms a backbone for the synthesis of triacylglycerol.

====Respiration===

The FAD-domain in GlpD plays a major role in the transport of electrons into the repiratory pathway. Glycerol 3-phosphate is oxidized to dihydroxyacetone phosphate with simultaneous reduction of of FAD to FADH2 occuring, and the electrons are transported to Ubiquinone, which are further transported to oxygen or nitrogen and into the respiratory pathway.

===Diseases===

===References===
<references />

[[Image:FINAL.png|thumb|Glycerol 3-Phosphate Dehydrogenase]]

<table style="background-color:#ffffc0" cellpadding="8" width="95%" border="0"><tr><td>Please do NOT make changes to this Sandbox until after April 23, 2010. Sandboxes 151-200 are reserved until then for use by the Chemistry 307 class at UNBC taught by Prof. [[User:Andrea Gorrell|Andrea Gorrell]].</td></tr>

Glycerol-3-Phosphate Dehydrogenase

2010-04-01T06:24:37Z

Indu Toora:

{{STRUCTURE_2r4e| PDB=2r4e | SCENE=Sandbox_189/Mynewscene/1 }}
'''Glycerol 3-Phosphate Dehydrogenase'''

Glycerol 3-phosphate dehydrogenase (GlpD) is a membrane bound enzyme in prokaryotes and in eukaryotes. Glycerol 3-Phosphate Dehydrogenase (GlpD) is an oxidoreductase enzyme which catalyzes the reduction (in [http://en.wikipedia.org/wiki/File:Dihydroxyacetone_phosphate_to_glycerol_3-phosphate_en.svg reaction] of Dihydroxyacetone Phosphate to Glycerol 3-Phosphate, with NADH as the reductant. GlpD is involved in many cellular functions such as phospholipids biosynthesis, respiration and metabolism. The GlpD is a dimer consisting of two subunits which contain the catabolite activator protein (CAP)-Domain,the flavin adenine dinucleotide(FAD)-Domain and a ubiquinone analogue, MD.

===Structure===

GlpD is a dimer that consists of two subunits; α and β. The GlpD structure also contains seven ligands; 1,3-Dihydroxyacetonephosphate (13P), β-Octylglucoside (βOG), 1,2-Ethanediol (EDO), Flavin-Adenine Dinucleotide (FAD), Imidazole (IMD), PO4 (Phosphate Ion) and N-(Tris(Hydroxymethyl)methyl)-3-Aminopropanesulfonic Acid (T3A). The active sites on GlpD are the Cap-Domain, FAD- Domain and a ubiquinone substrate analogue, menadione (MD).

<scene name='Sandbox_189/Cap_domain/1'>Cap-Binding Domain</scene>

The C-terminal CAP-Domain consists of negatively charged residues that are opposite in orientation to the positively charged residues of the FAD-Domain in the phospholipid membrane. The CAP-domain is responsible in gene transcription and helical turns.

<scene name='Sandbox_189/Fad/2'>FAD Active Site</scene>

The N-terminal FAD-Domain exists in each monomer subunit of GlpD and is embedded into the phospholipid membrane bilayer.Substrate binding occurs at this domain which causes a conformational change to the structure of the GlpD enzyme. The FAD-domain plays a major role in metabolism and energy synthesis.

===Function===

GlpD functions in the intracellular membrane of E. coli and in the inner-mitochondrial membrane of eukaryotes. In E. Coli, GlpD catalyzes and reduces the reaction of dihydroxyacetone phosphate to glycerol 3-phosphate in the [http://www.pnas.org/content/105/9/3280/F1.large.jpg glycerol metabolism pathway]. The binding of the substrate analogues (glyceraldehydes 3-phosphate, glyceric acid 2-phosphate and phosphoenolpyruvate, dihydroxyacetone phosphate)or UQ substrate analogues (2-n-heptyl-4-hydroxyquinoline N-oxide and menadione). The conformational change of the structure and resiudes of GlpD catalyzes many different metabolic reactions.

====Phosphoplipid Biosynthesis====

GlpD reduces dihydroxyacetone phosphate to glycerol 3-phosphate. Then the glycerol 3-phosphate is catalyzed by acyl transferase to 1-acylglyverol-3-phosphate, and then another acyl transferase catalyzes that to a phosphatidic acid. head groups are added to the phosphatidic acid to synthesize phospholipids.

====Glycerol Metabolic Pathway====

====Glyceride Phosphate Shuttle===

Glycerol
===Diseases===
===References===
<references />

[[Image:FINAL.png|thumb|Glycerol 3-Phosphate Dehydrogenase]]

<table style="background-color:#ffffc0" cellpadding="8" width="95%" border="0"><tr><td>Please do NOT make changes to this Sandbox until after April 23, 2010. Sandboxes 151-200 are reserved until then for use by the Chemistry 307 class at UNBC taught by Prof. [[User:Andrea Gorrell|Andrea Gorrell]].</td></tr>

Glycerol-3-Phosphate Dehydrogenase

2010-04-01T06:13:39Z

Indu Toora:

{{STRUCTURE_2r4e| PDB=2r4e | SCENE=Sandbox_189/Mynewscene/1 }}
'''Glycerol 3-Phosphate Dehydrogenase'''

Glycerol 3-phosphate dehydrogenase (GlpD) is a membrane bound enzyme in prokaryotes and in eukaryotes. Glycerol 3-Phosphate Dehydrogenase (GlpD) is an oxidoreductase enzyme which catalyzes the reduction (in [http://en.wikipedia.org/wiki/File:Dihydroxyacetone_phosphate_to_glycerol_3-phosphate_en.svg reaction] of Dihydroxyacetone Phosphate to Glycerol 3-Phosphate. GlpD is involved in many cellular functions such as phospholipids biosynthesis, respiration and metabolism. The GlpD is a dimer consisting of two subunits which contain the catabolite activator protein (CAP)-Domain,the flavin adenine dinucleotide(FAD)-Domain and a ubiquinone analogue, MD.

===Structure===

GlpD is a dimer that consists of two subunits; α and β. The GlpD structure also contains seven ligands; 1,3-Dihydroxyacetonephosphate (13P), β-Octylglucoside (βOG), 1,2-Ethanediol (EDO), Flavin-Adenine Dinucleotide (FAD), Imidazole (IMD), PO4 (Phosphate Ion) and N-(Tris(Hydroxymethyl)methyl)-3-Aminopropanesulfonic Acid (T3A). The active sites on GlpD are the Cap-Domain, FAD- Domain and a ubiquinone substrate analogue, menadione (MD).

<scene name='Sandbox_189/Cap_domain/1'>Cap-Binding Domain</scene>

The C-terminal CAP-Domain consists of negatively charged residues that are opposite in orientation to the positively charged residues of the FAD-Domain in the phospholipid membrane. The CAP-domain is responsible in gene transcription and helical turns.

<scene name='Sandbox_189/Fad/2'>FAD Active Site</scene>

The N-terminal FAD-Domain exists in each monomer subunit of GlpD and is embedded into the phospholipid membrane bilayer.Substrate binding occurs at this domain which causes a conformational change to the structure of the GlpD enzyme. The FAD-domain plays a major role in metabolism and energy synthesis.

===Function===

GlpD functions in the intracellular membrane of E. coli and in the inner-mitochondrial membrane of eukaryotes. In E. Coli, GlpD catalyzes and reduces the reaction of dihydroxyacetone phosphate to glycerol 3-phosphate in the [http://www.pnas.org/content/105/9/3280/F1.large.jpg glycerol metabolism pathway]. The binding of the substrate analogues (glyceraldehydes 3-phosphate, glyceric acid 2-phosphate and phosphoenolpyruvate, dihydroxyacetone phosphate)or UQ substrate analogues (2-n-heptyl-4-hydroxyquinoline N-oxide and menadione). The conformational change of the structure and resiudes of GlpD catalyzes many different metabolic reactions.

====Glycerol Metabolic Pathway====

====Glyceride Phosphate Shuttle===

Glycerol
===Diseases===
===References===
<references />

[[Image:FINAL.png|thumb|Glycerol 3-Phosphate Dehydrogenase]]

<table style="background-color:#ffffc0" cellpadding="8" width="95%" border="0"><tr><td>Please do NOT make changes to this Sandbox until after April 23, 2010. Sandboxes 151-200 are reserved until then for use by the Chemistry 307 class at UNBC taught by Prof. [[User:Andrea Gorrell|Andrea Gorrell]].</td></tr>

Glycerol-3-Phosphate Dehydrogenase

2010-04-01T06:02:52Z

Indu Toora:

{{STRUCTURE_2r4e| PDB=2r4e | SCENE=Sandbox_189/Mynewscene/1 }}
'''Glycerol 3-Phosphate Dehydrogenase'''

Glycerol 3-phosphate dehydrogenase (GlpD) is a membrane bound enzyme in prokaryotes and in eukaryotes. Glycerol 3-Phosphate Dehydrogenase (GlpD) is an oxidoreductase enzyme which catalyzes the reduction in [http://en.wikipedia.org/wiki/File:Dihydroxyacetone_phosphate_to_glycerol_3-phosphate_en.svg reaction] of Dihydroxyacetone Phosphate to Glycerol 3-Phosphate. GlpD is involved in many cellular functions such as phospholipids biosynthesis, respiration and metabolism. The GlpD is a dimer consisting of two subunits which contain the catabolite activator protein (CAP)-Domain,the flavin adenine dinucleotide(FAD)-Domain and a ubiquinone analogue, MD.

===Structure===

GlpD is a dimer that consists of two subunits; α and β. The GlpD structure also contains seven ligands; 1,3-Dihydroxyacetonephosphate (13P), β-Octylglucoside (βOG), 1,2-Ethanediol (EDO), Flavin-Adenine Dinucleotide (FAD), Imidazole (IMD), PO4 (Phosphate Ion) and N-(Tris(Hydroxymethyl)methyl)-3-Aminopropanesulfonic Acid (T3A). The active sites on GlpD are the Cap-Domain, FAD- Domain and a ubiquinone substrate analogue, menadione (MD).

<scene name='Sandbox_189/Cap_domain/1'>Cap-Binding Domain</scene>

The C-terminal CAP-Domain consists of negatively charged residues that are opposite in orientation to the positively charged residues of the FAD-Domain in the phospholipid membrane. The CAP-domain is responsible in gene transcription and helical turns.

<scene name='Sandbox_189/Fad/2'>FAD Active Site</scene>

The N-terminal FAD-Domain exists in each monomer subunit of GlpD and is embedded into the phospholipid membrane bilayer.Substrate binding occurs at this domain which causes a conformational change to the structure of the GlpD enzyme. The FAD-domain plays a major role in metabolism and energy synthesis.

===Function===

GlpD functions in the intracellular membrane of E. coli and in the inner-mitochondrial membrane of eukaryotes. In E. Coli, GlpD catalyzes and reduces the reaction of dihydroxyacetone phosphate to glycerol 3-phosphate in the [http://www.pnas.org/content/105/9/3280/F1.large.jpg glycerol metabolism pathway]. The binding of the substrate analogues (glyceraldehydes 3-phosphate, glyceric acid 2-phosphate and phosphoenolpyruvate, dihydroxyacetone phosphate)or UQ substrate analogues (2-n-heptyl-4-hydroxyquinoline N-oxide and menadione). The conformational change of the structure and resiudes of GlpD catalyzes many different metabolic reactions.

====Glycerol Metabolic Pathway====

===Diseases===
===References===
<references />

[[Image:FINAL.png|thumb|Glycerol 3-Phosphate Dehydrogenase]]

<table style="background-color:#ffffc0" cellpadding="8" width="95%" border="0"><tr><td>Please do NOT make changes to this Sandbox until after April 23, 2010. Sandboxes 151-200 are reserved until then for use by the Chemistry 307 class at UNBC taught by Prof. [[User:Andrea Gorrell|Andrea Gorrell]].</td></tr>

Glycerol-3-Phosphate Dehydrogenase

2010-04-01T05:34:42Z

Indu Toora:

{{STRUCTURE_2r4e| PDB=2r4e | SCENE=Sandbox_189/Mynewscene/1 }}
'''Glycerol 3-Phosphate Dehydrogenase'''

Glycerol 3-phosphate dehydrogenase (GlpD) is a membrane bound enzyme in prokaryotes and in eukaryotes. Glycerol 3-Phosphate Dehydrogenase (GlpD) is an oxidoreductase enzyme which catalyzes the reduction in [http://en.wikipedia.org/wiki/File:Dihydroxyacetone_phosphate_to_glycerol_3-phosphate_en.svg reaction] of Dihydroxyacetone Phosphate to Glycerol 3-Phosphate. GlpD is involved in many cellular functions such as phospholipids biosynthesis, respiration and metabolism. The GlpD is a dimer consisting of two subunits which contain the Cap-Domain,the flavin adenine dinucleotide(FAD)-Domain and a ubiquinone analogue, MD.

===Structure===

GlpD is a dimer that consists of two subunits; α and β. The GlpD structure also contains seven ligands; 1,3-Dihydroxyacetonephosphate (13P), β-Octylglucoside (βOG), 1,2-Ethanediol (EDO), Flavin-Adenine Dinucleotide (FAD), Imidazole (IMD), PO4 (Phosphate Ion) and N-(Tris(Hydroxymethyl)methyl)-3-Aminopropanesulfonic Acid (T3A). The active sites on GlpD are the Cap-Domain, FAD- Domain and a ubiquinone substrate analogue, menadione (MD).

<scene name='Sandbox_189/Cap_domain/1'>Cap-Binding Domain</scene>

The C-terminal consists of negatively charged residues that are opposite in orientation to the positively charged residues of the FAD-Domain in the phospholipid membrane.

<scene name='Sandbox_189/Fad/2'>FAD Active Site</scene>

The N-terminal FAD-Domain exists in each monomer subunit of GlpD and is embedded into the phospholipid membrane bilayer. Substrate binding occurs at this domain which causes a conformational change to the structure of the GlpD enzyme. The base of the enzyme has positivly charged regions capable of association with the negatively charged heads of the phospholipid membrane.

===Function===

GlpD functions in the intracellular membrane of E. coli and in the inner-mitochondrial membrane of eukaryotes. In E. Coli, GlpD catalyzes and reduces the reaction of dihydroxyacetone phosphate to glycerol 3-phosphate in the [http://www.pnas.org/content/105/9/3280/F1.large.jpg glycerol metabolism pathway]. The binding of the substrate analogues and GlpD, a conformational change of the structure of the GlpD occurs.

Upon the oxidation of glycerol 3-phosphate, flavin adenine dinucleotide (FAD) reduces to FADH2, passing on electrons to Ubiquinone(UQ). UQ then reduces to UQH2 which allows for the transport of electrons into the respiratory pathway.

Glycerol 3-phosphate dehydrogenase (GlpD) is a membrane bound enzyme in prokaryotes and in eukaryotes. GlpD is involved in many cellular functions, some of which are phospholipids biosynthesis, respiration and metabolism. The authors believed that GlpD undergoes a conformational change upon complexing with analogue substrates, which are thought to catalyze glycerol 3-phosphate (G3P) dehydrogenation in two possible ways. The authors further researched and discovered more GlpD structures that are bound to Ubiquonone (Ub) analogues in order to link catalytic dehydrogenation to respiration and to gain insight on the mechanism involved in the transport of electrons into the respiratory pathway. It is also thought by the authors that the prokaryotic enzyme structural results can be applied to eukaryotic GlpD enzyme structural results, due to the conservation of greater than 45% of consensus protein sequences in almost all organisms.

====Metabolism====
===Diseases===
===References===
<references />

[[Image:FINAL.png|thumb|Glycerol 3-Phosphate Dehydrogenase]]

<table style="background-color:#ffffc0" cellpadding="8" width="95%" border="0"><tr><td>Please do NOT make changes to this Sandbox until after April 23, 2010. Sandboxes 151-200 are reserved until then for use by the Chemistry 307 class at UNBC taught by Prof. [[User:Andrea Gorrell|Andrea Gorrell]].</td></tr>

Glycerol-3-Phosphate Dehydrogenase

2010-04-01T05:33:49Z

Indu Toora:

{{STRUCTURE_2r4e| PDB=2r4e | SCENE=Sandbox_189/Mynewscene/1 }}
'''Glycerol 3-Phosphate Dehydrogenase'''

Glycerol 3-phosphate dehydrogenase (GlpD) is a membrane bound enzyme in prokaryotes and in eukaryotes. Glycerol 3-Phosphate Dehydrogenase (GlpD) is an oxidoreductase enzyme which catalyzes the reduction in [http://en.wikipedia.org/wiki/File:Dihydroxyacetone_phosphate_to_glycerol_3-phosphate_en.svg reaction] of Dihydroxyacetone Phosphate to Glycerol 3-Phosphate. GlpD is involved in many cellular functions such as phospholipids biosynthesis, respiration and metabolism. The GlpD is a dimer consisting of two subunits which contain the Cap-Domain,the flavin adenine dinucleotide(FAD)-Domain and a ubiquinone analogue, MD.

===Structure===
GlpD is a dimer that consists of two subunits; α and β. The GlpD structure also contains seven ligands; 1,3-Dihydroxyacetonephosphate (13P), β-Octylglucoside (βOG), 1,2-Ethanediol (EDO), Flavin-Adenine Dinucleotide (FAD), Imidazole (IMD), PO4 (Phosphate Ion) and N-(Tris(Hydroxymethyl)methyl)-3-Aminopropanesulfonic Acid (T3A). The active sites on GlpD are the Cap-Domain, FAD- Domain and a ubiquinone substrate analogue, menadione (MD).

<scene name='Sandbox_189/Cap_domain/1'>Cap-Binding Domain</scene>

The C-terminal consists of negatively charged residues that are opposite in orientation to the positively charged residues of the FAD-Domain in the phospholipid membrane.

<scene name='Sandbox_189/Fad/2'>FAD Active Site</scene>

The N-terminal FAD-Domain exists in each monomer subunit of GlpD and is embedded into the phospholipid membrane bilayer. Substrate binding occurs at this domain which causes a conformational change to the structure of the GlpD enzyme. The base of the enzyme has positivly charged regions capable of association with the negatively charged heads of the phospholipid membran<ref>PubMed:18296637</ref2>

===Function===

GlpD functions in the intracellular membrane of E. coli and in the inner-mitochondrial membrane of eukaryotes. In E. Coli, GlpD catalyzes and reduces the reaction of dihydroxyacetone phosphate to glycerol 3-phosphate in the [http://www.pnas.org/content/105/9/3280/F1.large.jpg glycerol metabolism pathway]. The binding of the substrate analogues and GlpD, a conformational change of the structure of the GlpD occurs.

Upon the oxidation of glycerol 3-phosphate, flavin adenine dinucleotide (FAD) reduces to FADH2, passing on electrons to Ubiquinone(UQ). UQ then reduces to UQH2 which allows for the transport of electrons into the respiratory pathway.

Glycerol 3-phosphate dehydrogenase (GlpD) is a membrane bound enzyme in prokaryotes and in eukaryotes. GlpD is involved in many cellular functions, some of which are phospholipids biosynthesis, respiration and metabolism. The authors believed that GlpD undergoes a conformational change upon complexing with analogue substrates, which are thought to catalyze glycerol 3-phosphate (G3P) dehydrogenation in two possible ways. The authors further researched and discovered more GlpD structures that are bound to Ubiquonone (Ub) analogues in order to link catalytic dehydrogenation to respiration and to gain insight on the mechanism involved in the transport of electrons into the respiratory pathway. It is also thought by the authors that the prokaryotic enzyme structural results can be applied to eukaryotic GlpD enzyme structural results, due to the conservation of greater than 45% of consensus protein sequences in almost all organisms.

====Metabolism====
===Diseases===
===References===
<references />

[[Image:FINAL.png|thumb|Glycerol 3-Phosphate Dehydrogenase]]

<table style="background-color:#ffffc0" cellpadding="8" width="95%" border="0"><tr><td>Please do NOT make changes to this Sandbox until after April 23, 2010. Sandboxes 151-200 are reserved until then for use by the Chemistry 307 class at UNBC taught by Prof. [[User:Andrea Gorrell|Andrea Gorrell]].</td></tr>

Glycerol-3-Phosphate Dehydrogenase

2010-04-01T05:33:12Z

Indu Toora:

{{STRUCTURE_2r4e| PDB=2r4e | SCENE=Sandbox_189/Mynewscene/1 }}
'''Glycerol 3-Phosphate Dehydrogenase'''

Glycerol 3-phosphate dehydrogenase (GlpD) is a membrane bound enzyme in prokaryotes and in eukaryotes. Glycerol 3-Phosphate Dehydrogenase (GlpD) is an oxidoreductase enzyme which catalyzes the reduction in [http://en.wikipedia.org/wiki/File:Dihydroxyacetone_phosphate_to_glycerol_3-phosphate_en.svg reaction] of Dihydroxyacetone Phosphate to Glycerol 3-Phosphate. GlpD is involved in many cellular functions such as phospholipids biosynthesis, respiration and metabolism. The GlpD is a dimer consisting of two subunits which contain the Cap-Domain,the flavin adenine dinucleotide(FAD)-Domain and a ubiquinone analogue, MD. <ref>PubMed:18296637</ref1>

===Structure===
GlpD is a dimer that consists of two subunits; α and β. The GlpD structure also contains seven ligands; 1,3-Dihydroxyacetonephosphate (13P), β-Octylglucoside (βOG), 1,2-Ethanediol (EDO), Flavin-Adenine Dinucleotide (FAD), Imidazole (IMD), PO4 (Phosphate Ion) and N-(Tris(Hydroxymethyl)methyl)-3-Aminopropanesulfonic Acid (T3A). The active sites on GlpD are the Cap-Domain, FAD- Domain and a ubiquinone substrate analogue, menadione (MD).

<scene name='Sandbox_189/Cap_domain/1'>Cap-Binding Domain</scene>

The C-terminal consists of negatively charged residues that are opposite in orientation to the positively charged residues of the FAD-Domain in the phospholipid membrane.

<scene name='Sandbox_189/Fad/2'>FAD Active Site</scene>

The N-terminal FAD-Domain exists in each monomer subunit of GlpD and is embedded into the phospholipid membrane bilayer. Substrate binding occurs at this domain which causes a conformational change to the structure of the GlpD enzyme. The base of the enzyme has positivly charged regions capable of association with the negatively charged heads of the phospholipid membran<ref>PubMed:18296637</ref2>

===Function===

GlpD functions in the intracellular membrane of E. coli and in the inner-mitochondrial membrane of eukaryotes. In E. Coli, GlpD catalyzes and reduces the reaction of dihydroxyacetone phosphate to glycerol 3-phosphate in the [http://www.pnas.org/content/105/9/3280/F1.large.jpg glycerol metabolism pathway]. The binding of the substrate analogues and GlpD, a conformational change of the structure of the GlpD occurs.

Upon the oxidation of glycerol 3-phosphate, flavin adenine dinucleotide (FAD) reduces to FADH2, passing on electrons to Ubiquinone(UQ). UQ then reduces to UQH2 which allows for the transport of electrons into the respiratory pathway.

Glycerol 3-phosphate dehydrogenase (GlpD) is a membrane bound enzyme in prokaryotes and in eukaryotes. GlpD is involved in many cellular functions, some of which are phospholipids biosynthesis, respiration and metabolism. The authors believed that GlpD undergoes a conformational change upon complexing with analogue substrates, which are thought to catalyze glycerol 3-phosphate (G3P) dehydrogenation in two possible ways. The authors further researched and discovered more GlpD structures that are bound to Ubiquonone (Ub) analogues in order to link catalytic dehydrogenation to respiration and to gain insight on the mechanism involved in the transport of electrons into the respiratory pathway. It is also thought by the authors that the prokaryotic enzyme structural results can be applied to eukaryotic GlpD enzyme structural results, due to the conservation of greater than 45% of consensus protein sequences in almost all organisms.

====Metabolism====
===Diseases===
===References===
<references />

[[Image:FINAL.png|thumb|Glycerol 3-Phosphate Dehydrogenase]]

<table style="background-color:#ffffc0" cellpadding="8" width="95%" border="0"><tr><td>Please do NOT make changes to this Sandbox until after April 23, 2010. Sandboxes 151-200 are reserved until then for use by the Chemistry 307 class at UNBC taught by Prof. [[User:Andrea Gorrell|Andrea Gorrell]].</td></tr>

Glycerol-3-Phosphate Dehydrogenase

2010-04-01T05:32:50Z

Indu Toora:

{{STRUCTURE_2r4e| PDB=2r4e | SCENE=Sandbox_189/Mynewscene/1 }}
'''Glycerol 3-Phosphate Dehydrogenase'''

Glycerol 3-phosphate dehydrogenase (GlpD) is a membrane bound enzyme in prokaryotes and in eukaryotes. Glycerol 3-Phosphate Dehydrogenase (GlpD) is an oxidoreductase enzyme which catalyzes the reduction in [http://en.wikipedia.org/wiki/File:Dihydroxyacetone_phosphate_to_glycerol_3-phosphate_en.svg reaction] of Dihydroxyacetone Phosphate to Glycerol 3-Phosphate. GlpD is involved in many cellular functions such as phospholipids biosynthesis, respiration and metabolism. The GlpD is a dimer consisting of two subunits which contain the Cap-Domain,the flavin adenine dinucleotide(FAD)-Domain and a ubiquinone analogue, MD<ref>PubMed:18296637</ref1>.

===Structure===
GlpD is a dimer that consists of two subunits; α and β. The GlpD structure also contains seven ligands; 1,3-Dihydroxyacetonephosphate (13P), β-Octylglucoside (βOG), 1,2-Ethanediol (EDO), Flavin-Adenine Dinucleotide (FAD), Imidazole (IMD), PO4 (Phosphate Ion) and N-(Tris(Hydroxymethyl)methyl)-3-Aminopropanesulfonic Acid (T3A). The active sites on GlpD are the Cap-Domain, FAD- Domain and a ubiquinone substrate analogue, menadione (MD).

<scene name='Sandbox_189/Cap_domain/1'>Cap-Binding Domain</scene>

The C-terminal consists of negatively charged residues that are opposite in orientation to the positively charged residues of the FAD-Domain in the phospholipid membrane.

<scene name='Sandbox_189/Fad/2'>FAD Active Site</scene>

The N-terminal FAD-Domain exists in each monomer subunit of GlpD and is embedded into the phospholipid membrane bilayer. Substrate binding occurs at this domain which causes a conformational change to the structure of the GlpD enzyme. The base of the enzyme has positivly charged regions capable of association with the negatively charged heads of the phospholipid membran<ref>PubMed:18296637</ref2>

===Function===

GlpD functions in the intracellular membrane of E. coli and in the inner-mitochondrial membrane of eukaryotes. In E. Coli, GlpD catalyzes and reduces the reaction of dihydroxyacetone phosphate to glycerol 3-phosphate in the [http://www.pnas.org/content/105/9/3280/F1.large.jpg glycerol metabolism pathway]. The binding of the substrate analogues and GlpD, a conformational change of the structure of the GlpD occurs.

Upon the oxidation of glycerol 3-phosphate, flavin adenine dinucleotide (FAD) reduces to FADH2, passing on electrons to Ubiquinone(UQ). UQ then reduces to UQH2 which allows for the transport of electrons into the respiratory pathway.

Glycerol 3-phosphate dehydrogenase (GlpD) is a membrane bound enzyme in prokaryotes and in eukaryotes. GlpD is involved in many cellular functions, some of which are phospholipids biosynthesis, respiration and metabolism. The authors believed that GlpD undergoes a conformational change upon complexing with analogue substrates, which are thought to catalyze glycerol 3-phosphate (G3P) dehydrogenation in two possible ways. The authors further researched and discovered more GlpD structures that are bound to Ubiquonone (Ub) analogues in order to link catalytic dehydrogenation to respiration and to gain insight on the mechanism involved in the transport of electrons into the respiratory pathway. It is also thought by the authors that the prokaryotic enzyme structural results can be applied to eukaryotic GlpD enzyme structural results, due to the conservation of greater than 45% of consensus protein sequences in almost all organisms.

====Metabolism====
===Diseases===
===References===
<references />

[[Image:FINAL.png|thumb|Glycerol 3-Phosphate Dehydrogenase]]

<table style="background-color:#ffffc0" cellpadding="8" width="95%" border="0"><tr><td>Please do NOT make changes to this Sandbox until after April 23, 2010. Sandboxes 151-200 are reserved until then for use by the Chemistry 307 class at UNBC taught by Prof. [[User:Andrea Gorrell|Andrea Gorrell]].</td></tr>

Glycerol-3-Phosphate Dehydrogenase

2010-04-01T05:32:30Z

Indu Toora:

{{STRUCTURE_2r4e| PDB=2r4e | SCENE=Sandbox_189/Mynewscene/1 }}
'''Glycerol 3-Phosphate Dehydrogenase'''

Glycerol 3-phosphate dehydrogenase (GlpD) is a membrane bound enzyme in prokaryotes and in eukaryotes. Glycerol 3-Phosphate Dehydrogenase (GlpD) is an oxidoreductase enzyme which catalyzes the reduction in [http://en.wikipedia.org/wiki/File:Dihydroxyacetone_phosphate_to_glycerol_3-phosphate_en.svg reaction] of Dihydroxyacetone Phosphate to Glycerol 3-Phosphate. GlpD is involved in many cellular functions such as phospholipids biosynthesis, respiration and metabolism. The GlpD is a dimer consisting of two subunits which contain the Cap-Domain,the flavin adenine dinucleotide(FAD)-Domain and a ubiquinone analogue, MD<ref>PubMed:18296637</ref1>

===Structure===
GlpD is a dimer that consists of two subunits; α and β. The GlpD structure also contains seven ligands; 1,3-Dihydroxyacetonephosphate (13P), β-Octylglucoside (βOG), 1,2-Ethanediol (EDO), Flavin-Adenine Dinucleotide (FAD), Imidazole (IMD), PO4 (Phosphate Ion) and N-(Tris(Hydroxymethyl)methyl)-3-Aminopropanesulfonic Acid (T3A). The active sites on GlpD are the Cap-Domain, FAD- Domain and a ubiquinone substrate analogue, menadione (MD).

<scene name='Sandbox_189/Cap_domain/1'>Cap-Binding Domain</scene>

The C-terminal consists of negatively charged residues that are opposite in orientation to the positively charged residues of the FAD-Domain in the phospholipid membrane.

<scene name='Sandbox_189/Fad/2'>FAD Active Site</scene>

The N-terminal FAD-Domain exists in each monomer subunit of GlpD and is embedded into the phospholipid membrane bilayer. Substrate binding occurs at this domain which causes a conformational change to the structure of the GlpD enzyme. The base of the enzyme has positivly charged regions capable of association with the negatively charged heads of the phospholipid membran<ref>PubMed:18296637</ref2>

===Function===

GlpD functions in the intracellular membrane of E. coli and in the inner-mitochondrial membrane of eukaryotes. In E. Coli, GlpD catalyzes and reduces the reaction of dihydroxyacetone phosphate to glycerol 3-phosphate in the [http://www.pnas.org/content/105/9/3280/F1.large.jpg glycerol metabolism pathway]. The binding of the substrate analogues and GlpD, a conformational change of the structure of the GlpD occurs.

Upon the oxidation of glycerol 3-phosphate, flavin adenine dinucleotide (FAD) reduces to FADH2, passing on electrons to Ubiquinone(UQ). UQ then reduces to UQH2 which allows for the transport of electrons into the respiratory pathway.

Glycerol 3-phosphate dehydrogenase (GlpD) is a membrane bound enzyme in prokaryotes and in eukaryotes. GlpD is involved in many cellular functions, some of which are phospholipids biosynthesis, respiration and metabolism. The authors believed that GlpD undergoes a conformational change upon complexing with analogue substrates, which are thought to catalyze glycerol 3-phosphate (G3P) dehydrogenation in two possible ways. The authors further researched and discovered more GlpD structures that are bound to Ubiquonone (Ub) analogues in order to link catalytic dehydrogenation to respiration and to gain insight on the mechanism involved in the transport of electrons into the respiratory pathway. It is also thought by the authors that the prokaryotic enzyme structural results can be applied to eukaryotic GlpD enzyme structural results, due to the conservation of greater than 45% of consensus protein sequences in almost all organisms.

====Metabolism====
===Diseases===
===References===
<references />

[[Image:FINAL.png|thumb|Glycerol 3-Phosphate Dehydrogenase]]

<table style="background-color:#ffffc0" cellpadding="8" width="95%" border="0"><tr><td>Please do NOT make changes to this Sandbox until after April 23, 2010. Sandboxes 151-200 are reserved until then for use by the Chemistry 307 class at UNBC taught by Prof. [[User:Andrea Gorrell|Andrea Gorrell]].</td></tr>

Glycerol-3-Phosphate Dehydrogenase

2010-04-01T05:31:35Z

Indu Toora:

{{STRUCTURE_2r4e| PDB=2r4e | SCENE=Sandbox_189/Mynewscene/1 }}
'''Glycerol 3-Phosphate Dehydrogenase'''

Glycerol 3-phosphate dehydrogenase (GlpD) is a membrane bound enzyme in prokaryotes and in eukaryotes. Glycerol 3-Phosphate Dehydrogenase (GlpD) is an oxidoreductase enzyme which catalyzes the reduction in [http://en.wikipedia.org/wiki/File:Dihydroxyacetone_phosphate_to_glycerol_3-phosphate_en.svg reaction] of Dihydroxyacetone Phosphate to Glycerol 3-Phosphate. GlpD is involved in many cellular functions such as phospholipids biosynthesis, respiration and metabolism. The GlpD is a dimer consisting of two subunits which contain the Cap-Domain,the flavin adenine dinucleotide(FAD)-Domain and a ubiquinone analogue, MD<ref>PubMed:18296637</ref1>.

===Structure===
GlpD is a dimer that consists of two subunits; α and β. The GlpD structure also contains seven ligands; 1,3-Dihydroxyacetonephosphate (13P), β-Octylglucoside (βOG), 1,2-Ethanediol (EDO), Flavin-Adenine Dinucleotide (FAD), Imidazole (IMD), PO4 (Phosphate Ion) and N-(Tris(Hydroxymethyl)methyl)-3-Aminopropanesulfonic Acid (T3A). The active sites on GlpD are the Cap-Domain, FAD- Domain and a ubiquinone substrate analogue, menadione (MD).

<scene name='Sandbox_189/Cap_domain/1'>Cap-Binding Domain</scene>

The C-terminal consists of negatively charged residues that are opposite in orientation to the positively charged residues of the FAD-Domain in the phospholipid membrane.

<scene name='Sandbox_189/Fad/2'>FAD Active Site</scene>

The N-terminal FAD-Domain exists in each monomer subunit of GlpD and is embedded into the phospholipid membrane bilayer. Substrate binding occurs at this domain which causes a conformational change to the structure of the GlpD enzyme. The base of the enzyme has positivly charged regions capable of association with the negatively charged heads of the phospholipid membran<ref>PubMed:18296637</ref2>.

===Function===

GlpD functions in the intracellular membrane of E. coli and in the inner-mitochondrial membrane of eukaryotes. In E. Coli, GlpD catalyzes and reduces the reaction of dihydroxyacetone phosphate to glycerol 3-phosphate in the [http://www.pnas.org/content/105/9/3280/F1.large.jpg glycerol metabolism pathway]. The binding of the substrate analogues and GlpD, a conformational change of the structure of the GlpD occurs.

Upon the oxidation of glycerol 3-phosphate, flavin adenine dinucleotide (FAD) reduces to FADH2, passing on electrons to Ubiquinone(UQ). UQ then reduces to UQH2 which allows for the transport of electrons into the respiratory pathway.

Glycerol 3-phosphate dehydrogenase (GlpD) is a membrane bound enzyme in prokaryotes and in eukaryotes. GlpD is involved in many cellular functions, some of which are phospholipids biosynthesis, respiration and metabolism. The authors believed that GlpD undergoes a conformational change upon complexing with analogue substrates, which are thought to catalyze glycerol 3-phosphate (G3P) dehydrogenation in two possible ways. The authors further researched and discovered more GlpD structures that are bound to Ubiquonone (Ub) analogues in order to link catalytic dehydrogenation to respiration and to gain insight on the mechanism involved in the transport of electrons into the respiratory pathway. It is also thought by the authors that the prokaryotic enzyme structural results can be applied to eukaryotic GlpD enzyme structural results, due to the conservation of greater than 45% of consensus protein sequences in almost all organisms.

====Metabolism====
===Diseases===
===References===
<references />

[[Image:FINAL.png|thumb|Glycerol 3-Phosphate Dehydrogenase]]

<table style="background-color:#ffffc0" cellpadding="8" width="95%" border="0"><tr><td>Please do NOT make changes to this Sandbox until after April 23, 2010. Sandboxes 151-200 are reserved until then for use by the Chemistry 307 class at UNBC taught by Prof. [[User:Andrea Gorrell|Andrea Gorrell]].</td></tr>

Glycerol-3-Phosphate Dehydrogenase

2010-04-01T05:30:50Z

Indu Toora:

{{STRUCTURE_2r4e| PDB=2r4e | SCENE=Sandbox_189/Mynewscene/1 }}
'''Glycerol 3-Phosphate Dehydrogenase'''

Glycerol 3-phosphate dehydrogenase (GlpD) is a membrane bound enzyme in prokaryotes and in eukaryotes. Glycerol 3-Phosphate Dehydrogenase (GlpD) is an oxidoreductase enzyme which catalyzes the reduction in [http://en.wikipedia.org/wiki/File:Dihydroxyacetone_phosphate_to_glycerol_3-phosphate_en.svg reaction] of Dihydroxyacetone Phosphate to Glycerol 3-Phosphate. GlpD is involved in many cellular functions such as phospholipids biosynthesis, respiration and metabolism. The GlpD is a dimer consisting of two subunits which contain the Cap-Domain,the flavin adenine dinucleotide(FAD)-Domain and a ubiquinone analogue, MD.
===Structure===
GlpD is a dimer that consists of two subunits; α and β. The GlpD structure also contains seven ligands; 1,3-Dihydroxyacetonephosphate (13P), β-Octylglucoside (βOG), 1,2-Ethanediol (EDO), Flavin-Adenine Dinucleotide (FAD), Imidazole (IMD), PO4 (Phosphate Ion) and N-(Tris(Hydroxymethyl)methyl)-3-Aminopropanesulfonic Acid (T3A). The active sites on GlpD are the Cap-Domain, FAD- Domain and a ubiquinone substrate analogue, menadione (MD).

<scene name='Sandbox_189/Cap_domain/1'>Cap-Binding Domain</scene>

The C-terminal consists of negatively charged residues that are opposite in orientation to the positively charged residues of the FAD-Domain in the phospholipid membrane.

<scene name='Sandbox_189/Fad/2'>FAD Active Site</scene>

The N-terminal FAD-Domain exists in each monomer subunit of GlpD and is embedded into the phospholipid membrane bilayer. Substrate binding occurs at this domain which causes a conformational change to the structure of the GlpD enzyme. The base of the enzyme has positivly charged regions capable of association with the negatively charged heads of the phospholipid membrane. <ref>PubMed:18296637</ref2>

===Function===

GlpD functions in the intracellular membrane of E. coli and in the inner-mitochondrial membrane of eukaryotes. In E. Coli, GlpD catalyzes and reduces the reaction of dihydroxyacetone phosphate to glycerol 3-phosphate in the [http://www.pnas.org/content/105/9/3280/F1.large.jpg glycerol metabolism pathway]. The binding of the substrate analogues and GlpD, a conformational change of the structure of the GlpD occurs.

Upon the oxidation of glycerol 3-phosphate, flavin adenine dinucleotide (FAD) reduces to FADH2, passing on electrons to Ubiquinone(UQ). UQ then reduces to UQH2 which allows for the transport of electrons into the respiratory pathway.

Glycerol 3-phosphate dehydrogenase (GlpD) is a membrane bound enzyme in prokaryotes and in eukaryotes. GlpD is involved in many cellular functions, some of which are phospholipids biosynthesis, respiration and metabolism. The authors believed that GlpD undergoes a conformational change upon complexing with analogue substrates, which are thought to catalyze glycerol 3-phosphate (G3P) dehydrogenation in two possible ways. The authors further researched and discovered more GlpD structures that are bound to Ubiquonone (Ub) analogues in order to link catalytic dehydrogenation to respiration and to gain insight on the mechanism involved in the transport of electrons into the respiratory pathway. It is also thought by the authors that the prokaryotic enzyme structural results can be applied to eukaryotic GlpD enzyme structural results, due to the conservation of greater than 45% of consensus protein sequences in almost all organisms.

====Metabolism====
===Diseases===
===References===
<references />

[[Image:FINAL.png|thumb|Glycerol 3-Phosphate Dehydrogenase]]

<table style="background-color:#ffffc0" cellpadding="8" width="95%" border="0"><tr><td>Please do NOT make changes to this Sandbox until after April 23, 2010. Sandboxes 151-200 are reserved until then for use by the Chemistry 307 class at UNBC taught by Prof. [[User:Andrea Gorrell|Andrea Gorrell]].</td></tr>

Glycerol-3-Phosphate Dehydrogenase

2010-04-01T05:28:42Z

Indu Toora:

{{STRUCTURE_2r4e| PDB=2r4e | SCENE=Sandbox_189/Mynewscene/1 }}
'''Glycerol 3-Phosphate Dehydrogenase'''

Glycerol 3-phosphate dehydrogenase (GlpD) is a membrane bound enzyme in prokaryotes and in eukaryotes. Glycerol 3-Phosphate Dehydrogenase (GlpD) is an oxidoreductase enzyme which catalyzes the reduction in [http://en.wikipedia.org/wiki/File:Dihydroxyacetone_phosphate_to_glycerol_3-phosphate_en.svg reaction] of Dihydroxyacetone Phosphate to Glycerol 3-Phosphate. GlpD is involved in many cellular functions such as phospholipids biosynthesis, respiration and metabolism. The GlpD is a dimer consisting of two subunits which contain the Cap-Domain,the flavin adenine dinucleotide(FAD)-Domain and a ubiquinone analogue, MD. <ref>PubMed:18296637</ref1>.

===Structure===
GlpD is a dimer that consists of two subunits; α and β. The GlpD structure also consists of of seven ligands; 1,3-Dihydroxyacetonephosphate (13P), β-Octylglucoside (βOG), 1,2-Ethanediol (EDO), Flavin-Adenine Dinucleotide (FAD), Imidazole (IMD), PO4 (Phosphate Ion) and N-(Tris(Hydroxymethyl)methyl)-3-Aminopropanesulfonic Acid (T3A). The active sites on GlpD are the Cap-Domain, FAD- Domain and a ubiquinone substrate analogue, menadione (MD).

<scene name='Sandbox_189/Cap_domain/1'>Cap-Binding Domain</scene>

The C-terminal Cap-Domain consists of residues 389-501. This domain consists of negatively charged residues that are opposite in orientation to the positively charged residues of the FAD-Domain in the phospholipid membrane.

<scene name='Sandbox_189/Fad/2'>FAD Active Site</scene>

The N-terminal FAD-Binding Domain (also known as FAD-Domain) consists of residues 1 to 388. The FAD-Domain exists in each monomer subunit of GlpD and is embedded into the phospholipid membrane bilayer. Substrate binding occurs at this domain which causes a conformational change to the structure of the GlpD enzyme. The base of the enzyme has positivly charged regions capable of association with the negatively charged heads of the phospholipid membrane. <ref>PubMed:18296637</ref2>

===Function===

GlpD functions in the intracellular membrane of E. coli and in the inner-mitochondrial membrane of eukaryotes. In E. Coli, GlpD catalyzes and reduces the reaction of dihydroxyacetone phosphate to glycerol 3-phosphate in the [http://www.pnas.org/content/105/9/3280/F1.large.jpg glycerol metabolism pathway]. The binding of the substrate analogues and GlpD, a conformational change of the structure of the GlpD occurs.

Upon the oxidation of glycerol 3-phosphate, flavin adenine dinucleotide (FAD) reduces to FADH2, passing on electrons to Ubiquinone(UQ). UQ then reduces to UQH2 which allows for the transport of electrons into the respiratory pathway.

Glycerol 3-phosphate dehydrogenase (GlpD) is a membrane bound enzyme in prokaryotes and in eukaryotes. GlpD is involved in many cellular functions, some of which are phospholipids biosynthesis, respiration and metabolism. The authors believed that GlpD undergoes a conformational change upon complexing with analogue substrates, which are thought to catalyze glycerol 3-phosphate (G3P) dehydrogenation in two possible ways. The authors further researched and discovered more GlpD structures that are bound to Ubiquonone (Ub) analogues in order to link catalytic dehydrogenation to respiration and to gain insight on the mechanism involved in the transport of electrons into the respiratory pathway. It is also thought by the authors that the prokaryotic enzyme structural results can be applied to eukaryotic GlpD enzyme structural results, due to the conservation of greater than 45% of consensus protein sequences in almost all organisms.

====Metabolism====
===Diseases===
===References===
<references />

[[Image:FINAL.png|thumb|Glycerol 3-Phosphate Dehydrogenase]]

<table style="background-color:#ffffc0" cellpadding="8" width="95%" border="0"><tr><td>Please do NOT make changes to this Sandbox until after April 23, 2010. Sandboxes 151-200 are reserved until then for use by the Chemistry 307 class at UNBC taught by Prof. [[User:Andrea Gorrell|Andrea Gorrell]].</td></tr>

Glycerol-3-Phosphate Dehydrogenase

2010-04-01T05:27:09Z

Indu Toora:

{{STRUCTURE_2r4e| PDB=2r4e | SCENE=Sandbox_189/Mynewscene/1 }}
'''Glycerol 3-Phosphate Dehydrogenase'''

Glycerol 3-phosphate dehydrogenase (GlpD) is a membrane bound enzyme in prokaryotes and in eukaryotes. Glycerol 3-Phosphate Dehydrogenase (GlpD) is an oxidoreductase enzyme which catalyzes the reduction in [http://en.wikipedia.org/wiki/File:Dihydroxyacetone_phosphate_to_glycerol_3-phosphate_en.svg reaction] of Dihydroxyacetone Phosphate to Glycerol 3-Phosphate. GlpD is involved in many cellular functions such as phospholipids biosynthesis, respiration and metabolism. The GlpD is a dimer consisting of two subunits which contain the Cap-Domain,the flavin adenine dinucleotide (FAD)-Domain and a ubiquinone analogue, MD. <ref>PubMed:18296637</ref1>.

===Structure===
GlpD is a dimer that consists of two subunits; α and β. The GlpD structure also consists of of seven ligands; 1,3-Dihydroxyacetonephosphate (13P), β-Octylglucoside (βOG), 1,2-Ethanediol (EDO), Flavin-Adenine Dinucleotide (FAD), Imidazole (IMD), PO4 (Phosphate Ion) and N-(Tris(Hydroxymethyl)methyl)-3-Aminopropanesulfonic Acid (T3A). The active sites on GlpD are the Cap-Domain, FAD- Domain and a ubiquinone substrate analogue, menadione (MD).

<scene name='Sandbox_189/Cap_domain/1'>Cap-Binding Domain</scene>

The C-terminal Cap-Domain consists of residues 389-501. This domain consists of negatively charged residues that are opposite in orientation to the positively charged residues of the FAD-Domain in the phospholipid membrane.

<scene name='Sandbox_189/Fad/2'>FAD Active Site</scene>

The N-terminal FAD-Binding Domain (also known as FAD-Domain) consists of residues 1 to 388. The FAD-Domain exists in each monomer subunit of GlpD and is embedded into the phospholipid membrane bilayer. Substrate binding occurs at this domain which causes a conformational change to the structure of the GlpD enzyme. The base of the enzyme has positivly charged regions capable of association with the negatively charged heads of the phospholipid membrane. <ref>PubMed:18296637</ref2>

===Function===

GlpD functions in the intracellular membrane of E. coli and in the inner-mitochondrial membrane of eukaryotes. In E. Coli, GlpD catalyzes and reduces the reaction of dihydroxyacetone phosphate to glycerol 3-phosphate in the [http://www.pnas.org/content/105/9/3280/F1.large.jpg glycerol metabolism pathway]. The binding of the substrate analogues and GlpD, a conformational change of the structure of the GlpD occurs.

Upon the oxidation of glycerol 3-phosphate, flavin adenine dinucleotide (FAD) reduces to FADH2, passing on electrons to Ubiquinone(UQ). UQ then reduces to UQH2 which allows for the transport of electrons into the respiratory pathway.

Glycerol 3-phosphate dehydrogenase (GlpD) is a membrane bound enzyme in prokaryotes and in eukaryotes. GlpD is involved in many cellular functions, some of which are phospholipids biosynthesis, respiration and metabolism. The authors believed that GlpD undergoes a conformational change upon complexing with analogue substrates, which are thought to catalyze glycerol 3-phosphate (G3P) dehydrogenation in two possible ways. The authors further researched and discovered more GlpD structures that are bound to Ubiquonone (Ub) analogues in order to link catalytic dehydrogenation to respiration and to gain insight on the mechanism involved in the transport of electrons into the respiratory pathway. It is also thought by the authors that the prokaryotic enzyme structural results can be applied to eukaryotic GlpD enzyme structural results, due to the conservation of greater than 45% of consensus protein sequences in almost all organisms.

====Metabolism====
===Diseases===
===References===
<references />

[[Image:FINAL.png|thumb|Glycerol 3-Phosphate Dehydrogenase]]

<table style="background-color:#ffffc0" cellpadding="8" width="95%" border="0"><tr><td>Please do NOT make changes to this Sandbox until after April 23, 2010. Sandboxes 151-200 are reserved until then for use by the Chemistry 307 class at UNBC taught by Prof. [[User:Andrea Gorrell|Andrea Gorrell]].</td></tr>

Glycerol-3-Phosphate Dehydrogenase

2010-04-01T05:21:51Z

Indu Toora:

{{STRUCTURE_2r4e| PDB=2r4e | SCENE=Sandbox_189/Mynewscene/1 }}
'''Glycerol 3-Phosphate Dehydrogenase'''

Glycerol 3-phosphate dehydrogenase (GlpD) is a membrane bound enzyme in prokaryotes and in eukaryotes. Glycerol 3-Phosphate Dehydrogenase (GlpD) is an oxidoreductase enzyme which catalyzes the reduction in [http://en.wikipedia.org/wiki/File:Dihydroxyacetone_phosphate_to_glycerol_3-phosphate_en.svg reaction] of Dihydroxyacetone Phosphate to Glycerol 3-Phosphate. GlpD is involved in many cellular functions such as phospholipids biosynthesis, respiration and metabolism. The GlpD is a dimer consisting of two subunits which contain the Cap-Domain,the flavin adenine dinucleotide (FAD)-Domain and a ubiquinone analogue, MD. <ref>PubMed:18296637</ref1>

===Structure===
GlpD is a dimer that consists of two subunits; α and β. The GlpD structure also consists of of seven ligands; 1,3-Dihydroxyacetonephosphate (13P), β-Octylglucoside (βOG), 1,2-Ethanediol (EDO), Flavin-Adenine Dinucleotide (FAD), Imidazole (IMD), PO4 (Phosphate Ion) and N-(Tris(Hydroxymethyl)methyl)-3-Aminopropanesulfonic Acid (T3A). The active sites on GlpD are the Cap-Domain, FAD- Domain and a ubiquinone substrate analogue, menadione (MD).

<scene name='Sandbox_189/Cap_domain/1'>Cap-Binding Domain</scene>

The C-terminal Cap-Domain consists of residues 389-501. This domain consists of negatively charged residues that are opposite in orientation to the positively charged residues of the FAD-Domain in the phospholipid membrane.

<scene name='Sandbox_189/Fad/2'>FAD Active Site</scene>

The N-terminal FAD-Binding Domain (also known as FAD-Domain) consists of residues 1 to 388. The FAD-Domain exists in each monomer subunit of GlpD and is embedded into the phospholipid membrane bilayer. Substrate binding occurs at this domain which causes a conformational change to the structure of the GlpD enzyme. The base of the enzyme has positivly charged regions capable of association with the negatively charged heads of the phospholipid membrane. <ref>PubMed:18296637</ref2>

===Function===

GlpD functions in the intracellular membrane of E. coli and in the inner-mitochondrial membrane of eukaryotes. In E. Coli, GlpD catalyzes and reduces the reaction of dihydroxyacetone phosphate to glycerol 3-phosphate in the [http://www.pnas.org/content/105/9/3280/F1.large.jpg glycerol metabolism pathway]. The binding of the substrate analogues and GlpD, a conformational change of the structure of the GlpD occurs.

Upon the oxidation of glycerol 3-phosphate, flavin adenine dinucleotide (FAD) reduces to FADH2, passing on electrons to Ubiquinone(UQ). UQ then reduces to UQH2 which allows for the transport of electrons into the respiratory pathway.

Glycerol 3-phosphate dehydrogenase (GlpD) is a membrane bound enzyme in prokaryotes and in eukaryotes. GlpD is involved in many cellular functions, some of which are phospholipids biosynthesis, respiration and metabolism. The authors believed that GlpD undergoes a conformational change upon complexing with analogue substrates, which are thought to catalyze glycerol 3-phosphate (G3P) dehydrogenation in two possible ways. The authors further researched and discovered more GlpD structures that are bound to Ubiquonone (Ub) analogues in order to link catalytic dehydrogenation to respiration and to gain insight on the mechanism involved in the transport of electrons into the respiratory pathway. It is also thought by the authors that the prokaryotic enzyme structural results can be applied to eukaryotic GlpD enzyme structural results, due to the conservation of greater than 45% of consensus protein sequences in almost all organisms.

====Metabolism====
===Diseases===
===References===
<references />

[[Image:FINAL.png|thumb|Glycerol 3-Phosphate Dehydrogenase]]

<table style="background-color:#ffffc0" cellpadding="8" width="95%" border="0"><tr><td>Please do NOT make changes to this Sandbox until after April 23, 2010. Sandboxes 151-200 are reserved until then for use by the Chemistry 307 class at UNBC taught by Prof. [[User:Andrea Gorrell|Andrea Gorrell]].</td></tr>

Glycerol-3-Phosphate Dehydrogenase

2010-04-01T04:59:40Z

Indu Toora:

{{STRUCTURE_2r4e| PDB=2r4e | SCENE=Sandbox_189/Mynewscene/1 }}
'''Glycerol 3-Phosphate Dehydrogenase'''

Glycerol 3-phosphate dehydrogenase (GlpD) is a membrane bound enzyme in prokaryotes and in eukaryotes. Glycerol 3-Phosphate Dehydrogenase (GlpD) is an oxidoreductase enzyme which catalyzes the reduction in [http://en.wikipedia.org/wiki/File:Dihydroxyacetone_phosphate_to_glycerol_3-phosphate_en.svg reaction] of Dihydroxyacetone Phosphate to Glycerol 3-Phosphate. GlpD is involved in many cellular functions such as phospholipids biosynthesis, respiration and metabolism. The GlpD is a dimer consisting of two subunits which contain the Cap-Domain,the flavin adenine dinucleotide (FAD)-Domain and a ubiquinone analogue, MD. <ref>PubMed:18296637</ref1>

===Structure===
GlpD is a dimer that consists of two subunits; α and β. The GlpD structure also consists the Cap-Domain, FAD- Domain and a ubiquinone substrate analogue, menadione (MD)binding sites.

<scene name='Sandbox_189/Cap_domain/1'>Cap-Binding Domain</scene>

The C-terminal Cap-Domain consists of residues 389-501. This domain consists of negatively charged residues that are opposite in orientation to the positively charged residues of the FAD-Domain in the phospholipid membrane.

<scene name='Sandbox_189/Fad/2'>FAD Active Site</scene>

The N-terminal FAD-Binding Domain (also known as FAD-Domain) consists of residues 1 to 388. The FAD-Domain exists in each monomer subunit of GlpD and is embedded into the phospholipid membrane bilayer. Substrate binding occurs at this domain which causes a conformational change to the structure of the GlpD enzyme. The base of the enzyme has positivly charged regions capable of association with the negatively charged heads of the phospholipid membrane. <ref>PubMed:18296637</ref2>

===Function===

GlpD functions in the intracellular membrane of E. coli and in the inner-mitochondrial membrane of eukaryotes. In E. Coli, GlpD catalyzes and reduces the reaction of dihydroxyacetone phosphate to glycerol 3-phosphate in the [http://www.pnas.org/content/105/9/3280/F1.large.jpg glycerol metabolism pathway]. The binding of the substrate analogues and GlpD, a conformational change of the structure of the GlpD occurs.

Upon the oxidation of glycerol 3-phosphate, flavin adenine dinucleotide (FAD) reduces to FADH2, passing on electrons to Ubiquinone(UQ). UQ then reduces to UQH2 which allows for the transport of electrons into the respiratory pathway.

Glycerol 3-phosphate dehydrogenase (GlpD) is a membrane bound enzyme in prokaryotes and in eukaryotes. GlpD is involved in many cellular functions, some of which are phospholipids biosynthesis, respiration and metabolism. The authors believed that GlpD undergoes a conformational change upon complexing with analogue substrates, which are thought to catalyze glycerol 3-phosphate (G3P) dehydrogenation in two possible ways. The authors further researched and discovered more GlpD structures that are bound to Ubiquonone (Ub) analogues in order to link catalytic dehydrogenation to respiration and to gain insight on the mechanism involved in the transport of electrons into the respiratory pathway. It is also thought by the authors that the prokaryotic enzyme structural results can be applied to eukaryotic GlpD enzyme structural results, due to the conservation of greater than 45% of consensus protein sequences in almost all organisms.

====Metabolism====
===Diseases===
===References===
<references />

[[Image:FINAL.png|thumb|Glycerol 3-Phosphate Dehydrogenase]]

<table style="background-color:#ffffc0" cellpadding="8" width="95%" border="0"><tr><td>Please do NOT make changes to this Sandbox until after April 23, 2010. Sandboxes 151-200 are reserved until then for use by the Chemistry 307 class at UNBC taught by Prof. [[User:Andrea Gorrell|Andrea Gorrell]].</td></tr>

Glycerol-3-Phosphate Dehydrogenase

2010-04-01T04:58:29Z

Indu Toora:

{{STRUCTURE_2r4e| PDB=2r4e | SCENE=Sandbox_189/Mynewscene/1 }}
'''Glycerol 3-Phosphate Dehydrogenase'''

Glycerol 3-phosphate dehydrogenase (GlpD) is a membrane bound enzyme in prokaryotes and in eukaryotes. Glycerol 3-Phosphate Dehydrogenase (GlpD) is an oxidoreductase enzyme which catalyzes the reduction in [http://en.wikipedia.org/wiki/File:Dihydroxyacetone_phosphate_to_glycerol_3-phosphate_en.svg reaction] of Dihydroxyacetone Phosphate to Glycerol 3-Phosphate. GlpD is involved in many cellular functions such as phospholipids biosynthesis, respiration and metabolism. The GlpD is a dimer consisting of two subunits which contain the Cap-Domain,the flavin adenine dinucleotide (FAD)-Domain and a ubiquinone analogue, MD. <ref>PubMed:18296637</ref1>

===Structure===
GlpD is a dimer that consists of two subunits; α and β. The GlpD structure also consists the Cap-Domain, FAD- Domain and a ubiquinone substrate analogue, menadione (MD)binding sites.

<scene name='Sandbox_189/Cap_domain/1'>Cap-Binding Domain</scene>

The C-terminal Cap-Domain consists of residues 389-501. This domain consists of negatively charged residues that are opposite in orientation to the positively charged residues of the FAD-Domain in the phospholipid membrane.

<scene name='Sandbox_189/Fad/2'>FAD Active Site</scene>

The N-terminal FAD-Binding Domain (also known as FAD-Domain) consists of residues 1 to 388. The FAD-Domain exists in each monomer subunit of GlpD and is embedded into the phospholipid membrane bilayer. Substrate binding occurs at this domain which causes a conformational change to the structure of the GlpD enzyme. The base of the enzyme has positivly charged regions capable of association with the negatively charged heads of the phospholipid membrane. <ref>PubMed:18296637</ref2>

===Function===

GlpD functions in the intracellular membrane of E. coli and in the inner-mitochondrial membrane of eukaryotes. In E. Coli, GlpD catalyzes and reduces the reaction of dihydroxyacetone phosphate to glycerol 3-phosphate in the . The binding of the substrate analogues and GlpD, a conformational change of the structure of the GlpD occurs.

Upon the oxidation of glycerol 3-phosphate, flavin adenine dinucleotide (FAD) reduces to FADH2, passing on electrons to Ubiquinone(UQ). UQ then reduces to UQH2 which allows for the transport of electrons into the respiratory pathway.

Glycerol 3-phosphate dehydrogenase (GlpD) is a membrane bound enzyme in prokaryotes and in eukaryotes. GlpD is involved in many cellular functions, some of which are phospholipids biosynthesis, respiration and metabolism. The authors believed that GlpD undergoes a conformational change upon complexing with analogue substrates, which are thought to catalyze glycerol 3-phosphate (G3P) dehydrogenation in two possible ways. The authors further researched and discovered more GlpD structures that are bound to Ubiquonone (Ub) analogues in order to link catalytic dehydrogenation to respiration and to gain insight on the mechanism involved in the transport of electrons into the respiratory pathway. It is also thought by the authors that the prokaryotic enzyme structural results can be applied to eukaryotic GlpD enzyme structural results, due to the conservation of greater than 45% of consensus protein sequences in almost all organisms.

====Metabolism====
===Diseases===
===References===
<references />

[[Image:FINAL.png|thumb|Glycerol 3-Phosphate Dehydrogenase]]

<table style="background-color:#ffffc0" cellpadding="8" width="95%" border="0"><tr><td>Please do NOT make changes to this Sandbox until after April 23, 2010. Sandboxes 151-200 are reserved until then for use by the Chemistry 307 class at UNBC taught by Prof. [[User:Andrea Gorrell|Andrea Gorrell]].</td></tr>

Glycerol-3-Phosphate Dehydrogenase

2010-04-01T04:55:23Z

Indu Toora:

{{STRUCTURE_2r4e| PDB=2r4e | SCENE=Sandbox_189/Mynewscene/1 }}
'''Glycerol 3-Phosphate Dehydrogenase'''

Glycerol 3-phosphate dehydrogenase (GlpD) is a membrane bound enzyme in prokaryotes and in eukaryotes. Glycerol 3-Phosphate Dehydrogenase (GlpD) is an oxidoreductase enzyme which catalyzes the reduction of Dihydroxyacetone Phosphate to Glycerol 3-Phosphate. GlpD is involved in many cellular functions such as phospholipids biosynthesis, respiration and metabolism. The GlpD is a dimer consisting of two subunits which contain the Cap-Domain,the flavin adenine dinucleotide (FAD)-Domain and a ubiquinone analogue, MD. <ref>PubMed:18296637</ref1>

===Structure===
GlpD is a dimer that consists of two subunits; α and β. The GlpD structure also consists the Cap-Domain, FAD- Domain and a ubiquinone substrate analogue, menadione (MD)binding sites.

<scene name='Sandbox_189/Cap_domain/1'>Cap-Binding Domain</scene>

The C-terminal Cap-Domain consists of residues 389-501. This domain consists of negatively charged residues that are opposite in orientation to the positively charged residues of the FAD-Domain in the phospholipid membrane.

<scene name='Sandbox_189/Fad/2'>FAD Active Site</scene>

The N-terminal FAD-Binding Domain (also known as FAD-Domain) consists of residues 1 to 388. The FAD-Domain exists in each monomer subunit of GlpD and is embedded into the phospholipid membrane bilayer. Substrate binding occurs at this domain which causes a conformational change to the structure of the GlpD enzyme. The base of the enzyme has positivly charged regions capable of association with the negatively charged heads of the phospholipid membrane. <ref>PubMed:18296637</ref2>

===Function===

GlpD functions in the intracellular membrane of E. coli and in the inner-mitochondrial membrane of eukaryotes. In E. Coli, GlpD catalyzes and reduces the reaction of dihydroxyacetone phosphate to glycerol 3-phosphate in the . The binding of the substrate analogues and GlpD, a conformational change of the structure of the GlpD occurs.

Upon the oxidation of glycerol 3-phosphate, flavin adenine dinucleotide (FAD) reduces to FADH2, passing on electrons to Ubiquinone(UQ). UQ then reduces to UQH2 which allows for the transport of electrons into the respiratory pathway.

Glycerol 3-phosphate dehydrogenase (GlpD) is a membrane bound enzyme in prokaryotes and in eukaryotes. GlpD is involved in many cellular functions, some of which are phospholipids biosynthesis, respiration and metabolism. The authors believed that GlpD undergoes a conformational change upon complexing with analogue substrates, which are thought to catalyze glycerol 3-phosphate (G3P) dehydrogenation in two possible ways. The authors further researched and discovered more GlpD structures that are bound to Ubiquonone (Ub) analogues in order to link catalytic dehydrogenation to respiration and to gain insight on the mechanism involved in the transport of electrons into the respiratory pathway. It is also thought by the authors that the prokaryotic enzyme structural results can be applied to eukaryotic GlpD enzyme structural results, due to the conservation of greater than 45% of consensus protein sequences in almost all organisms.

====Metabolism====
===Diseases===
===References===
<references />

[[Image:FINAL.png|thumb|Glycerol 3-Phosphate Dehydrogenase]]

<table style="background-color:#ffffc0" cellpadding="8" width="95%" border="0"><tr><td>Please do NOT make changes to this Sandbox until after April 23, 2010. Sandboxes 151-200 are reserved until then for use by the Chemistry 307 class at UNBC taught by Prof. [[User:Andrea Gorrell|Andrea Gorrell]].</td></tr>

Glycerol-3-Phosphate Dehydrogenase

2010-04-01T04:42:29Z

Indu Toora:

Glycerol-3-Phosphate Dehydrogenase

2010-04-01T04:34:24Z

Indu Toora:

Glycerol-3-Phosphate Dehydrogenase

2010-04-01T04:32:35Z

Indu Toora:

Glycerol-3-Phosphate Dehydrogenase

2010-04-01T04:22:04Z

Indu Toora:

{{STRUCTURE_2r4e| PDB=2r4e | SCENE=Sandbox_189/Mynewscene/1 }}
'''Glycerol 3-Phosphate Dehydrogenase'''

Glycerol 3-phosphate dehydrogenase (GlpD) is a membrane bound enzyme in prokaryotes and in eukaryotes. Glycerol 3-Phosphate Dehydrogenase (GlpD) is an oxidoreductase enzyme which catalyzes the reduction [http://en.wikipedia.org/wiki/File:Dihydroxyacetone_phosphate_to_glycerol_3-phosphate_en.svg reaction]of Dihydroxyacetone Phosphate to Glycerol 3-Phosphate. GlpD is involved in many cellular functions such as phospholipids biosynthesis, respiration and metabolism. In E. coli, many newly discovered structures of GlpD seem to play a role in the transfer of electrons into the respiratory pathway by catalytic dehyrogenation of GlpD. a The GlpD enzyme is a dimer consisting of two subunits which contain the flavin adenine dinucleotide (FAD) active site. <ref>PubMed:18296637</ref1>

===Structure===
GlpD is a dimer that consists of two subunits; α and β. The GlpD structure also consists of a Cap Domain Site, FAD-Binding Domain and a ubiquinone substrate analogue, menadione (MD).

<scene name='Sandbox_189/Cap_domain/1'>Cap-Binding Domain</scene>

The C-terminal Cap-Binding Domain (also known as Cap-Domain) consists of residues 389-501. This domain consists of negatively charged residues that are opposite in orientation to the positively charged residues of the FAD-Domain.

<scene name='Sandbox_189/Fad/2'>FAD Active Site</scene>

The N-terminal FAD-Binding Domain (also known as FAD-Domain) consists of residues 1 to 388. The FAD-Domain exists in each monomer subunit of GlpD and is embedded into the phospholipid membrane bilayer. Substrate binding occurs at this domain which causes a conformational change to the structure of the GlpD enzyme. The base of the enzyme has positivly charged regions capable of association with the negatively charged heads of the phospholipid membrane. <ref>PubMed:18296637</ref2>

===Function===

GlpD is associated in the intracellular membrane of E. coli and in the inner-mitochondrial membrane of eukaryotes.
GlpD in E. Coli catalyzes and oxidizes the reaction of glycerol 3-phosphate to dihydroxyacetone phosphate in the glycerol metabolic pathway. The binding of the substrate analogues and GlpD, a conformational change of the structure of the GlpD occurs.

Upon the oxidation of glycerol 3-phosphate, flavin adenine dinucleotide (FAD) reduces to FADH2, passing on electrons to Ubiquinone(UQ). UQ then reduces to UQH2 which allows for the transport of electrons into the respiratory pathway.

====Metabolism====
===Diseases===
===References===
<references />

[[Image:FINAL.png|thumb|Glycerol 3-Phosphate Dehydrogenase]]

<table style="background-color:#ffffc0" cellpadding="8" width="95%" border="0"><tr><td>Please do NOT make changes to this Sandbox until after April 23, 2010. Sandboxes 151-200 are reserved until then for use by the Chemistry 307 class at UNBC taught by Prof. [[User:Andrea Gorrell|Andrea Gorrell]].</td></tr>

Glycerol-3-Phosphate Dehydrogenase

2010-04-01T04:15:20Z

Indu Toora:

{{STRUCTURE_2r4e| PDB=2r4e | SCENE=Sandbox_189/Mynewscene/1 }}
'''Glycerol 3-Phosphate Dehydrogenase'''

Glycerol 3-phosphate dehydrogenase (GlpD) is a membrane bound enzyme in prokaryotes and in eukaryotes. Glycerol 3-Phosphate Dehydrogenase (GlpD) is an oxidoreductase enzyme which catalyzes the reduction [http://en.wikipedia.org/wiki/File:Dihydroxyacetone_phosphate_to_glycerol_3-phosphate_en.svg reaction]of Dihydroxyacetone Phosphate to Glycerol 3-Phosphate. GlpD is involved in many cellular functions, where it uses the carbons from Glycerol 3-Phosphate for phospholipids biosynthesis, respiration and further metabolism. In E. coli, many newly discovered structures of GlpD seem to play a role in the transfer of electrons into the respiratory pathway by catalytic dehyrogenation of GlpD. a The GlpD enzyme is a dimer consisting of two subunits which contain the flavin adenine dinucleotide (FAD) active site. <ref>PubMed:18296637</ref1>

===Structure===
GlpD is a dimer that consists of two subunits; α and β. The GlpD structure also consists of a Cap Domain Site, FAD-Binding Domain and a ubiquinone substrate analogue, menadione (MD).

<scene name='Sandbox_189/Cap_domain/1'>Cap-Binding Domain</scene>

The C-terminal Cap-Binding Domain (also known as Cap-Domain) consists of residues 389-501. This domain consists of negatively charged residues that are opposite in orientation to the positively charged residues of the FAD-Domain.

<scene name='Sandbox_189/Fad/2'>FAD Active Site</scene>

The N-terminal FAD-Binding Domain (also known as FAD-Domain) consists of residues 1 to 388. The FAD-Domain exists in each monomer subunit of GlpD and is embedded into the phospholipid membrane bilayer. Substrate binding occurs at this domain which causes a conformational change to the structure of the GlpD enzyme. The base of the enzyme has positivly charged regions capable of association with the negatively charged heads of the phospholipid membrane. <ref>PubMed:18296637</ref2>

===Function===

GlpD is associated in the intracellular membrane of E. coli and in the inner-mitochondrial membrane of eukaryotes.
GlpD in E. Coli catalyzes and oxidizes the reaction of glycerol 3-phosphate to dihydroxyacetone phosphate in the glycerol metabolic pathway. The binding of the substrate analogues and GlpD, a conformational change of the structure of the GlpD occurs.

Upon the oxidation of glycerol 3-phosphate, flavin adenine dinucleotide (FAD) reduces to FADH2, passing on electrons to Ubiquinone(UQ). UQ then reduces to UQH2 which allows for the transport of electrons into the respiratory pathway.

====Metabolism====
===Diseases===
===References===
<references />

[[Image:FINAL.png|thumb|Glycerol 3-Phosphate Dehydrogenase]]

<table style="background-color:#ffffc0" cellpadding="8" width="95%" border="0"><tr><td>Please do NOT make changes to this Sandbox until after April 23, 2010. Sandboxes 151-200 are reserved until then for use by the Chemistry 307 class at UNBC taught by Prof. [[User:Andrea Gorrell|Andrea Gorrell]].</td></tr>

Glycerol-3-Phosphate Dehydrogenase

2010-04-01T04:06:50Z

Indu Toora:

{{STRUCTURE_2r4e| PDB=2r4e | SCENE=Sandbox_189/Mynewscene/1 }}
'''Glycerol 3-Phosphate Dehydrogenase'''

===Introduction===

Glycerol 3-phosphate dehydrogenase (GlpD) is a membrane bound enzyme in prokaryotes and in eukaryotes. Glycerol 3-Phosphate Dehydrogenase (GlpD) is an oxidoreductase enzyme which catalyzes the reduction [http://en.wikipedia.org/wiki/File:Dihydroxyacetone_phosphate_to_glycerol_3-phosphate_en.svg reaction]of Dihydroxyacetone Phosphate to Glycerol 3-Phosphate. GlpD is involved in many cellular functions, where it uses the carbons from Glycerol 3-Phosphate for phospholipids biosynthesis, respiration and further metabolism. In E. coli, many newly discovered structures of GlpD seem to play a role in the transfer of electrons into the respiratory pathway by catalytic dehyrogenation of GlpD. a The GlpD enzyme is a dimer consisting of two subunits which contain the flavin adenine dinucleotide (FAD) active site. <ref>PubMed:18296637</ref1>

===Structure===
GlpD is a dimer that consists of two subunits; α and β. The GlpD structure also consists of a Cap Domain Site, FAD-Binding Domain and a ubiquinone substrate analogue, menadione (MD).

<scene name='Sandbox_189/Cap_domain/1'>Cap-Binding Domain</scene>

The C-terminal Cap-Binding Domain (also known as Cap-Domain) consists of residues 389-501. This domain consists of negatively charged residues that are opposite in orientation to the positively charged residues of the FAD-Domain.

<scene name='Sandbox_189/Fad/2'>FAD Active Site</scene>

The N-terminal FAD-Binding Domain (also known as FAD-Domain) consists of residues 1 to 388. The FAD-Domain exists in each monomer subunit of GlpD and is embedded into the phospholipid membrane bilayer. Substrate binding occurs at this domain which causes a conformational change to the structure of the GlpD enzyme. The base of the enzyme has positivly charged regions capable of association with the negatively charged heads of the phospholipid membrane. <ref>PubMed:18296637</ref2>

===Function===

GlpD is associated in the intracellular membrane of E. coli and in the inner-mitochondrial membrane of eukaryotes.
GlpD in E. Coli catalyzes and oxidizes the reaction of glycerol 3-phosphate to dihydroxyacetone phosphate in the glycerol metabolic pathway. The binding of the substrate analogues and GlpD, a conformational change of the structure of the GlpD occurs.

Upon the oxidation of glycerol 3-phosphate, flavin adenine dinucleotide (FAD) reduces to FADH2, passing on electrons to Ubiquinone(UQ). UQ then reduces to UQH2 which allows for the transport of electrons into the respiratory pathway.

====Metabolism====
===Diseases===
===References===
<references />

[[Image:FINAL.png|thumb|Glycerol 3-Phosphate Dehydrogenase]]

<table style="background-color:#ffffc0" cellpadding="8" width="95%" border="0"><tr><td>Please do NOT make changes to this Sandbox until after April 23, 2010. Sandboxes 151-200 are reserved until then for use by the Chemistry 307 class at UNBC taught by Prof. [[User:Andrea Gorrell|Andrea Gorrell]].</td></tr>

Glycerol-3-Phosphate Dehydrogenase

2010-04-01T04:02:26Z

Indu Toora:

{{STRUCTURE_2r4e| PDB=2r4e | SCENE=Sandbox_189/Mynewscene/1 }}
'''Glycerol 3-Phosphate Dehydrogenase'''

===Introduction===

Glycerol 3-phosphate dehydrogenase (GlpD) is a membrane bound enzyme in prokaryotes and in eukaryotes. Glycerol 3-Phosphate Dehydrogenase (GlpD) is an oxidoreductase enzyme which catalyzes the reduction [http://en.wikipedia.org/wiki/File:Dihydroxyacetone_phosphate_to_glycerol_3-phosphate_en.svg reaction]of Dihydroxyacetone Phosphate to Glycerol 3-Phosphate. GlpD is involved in many cellular functions, where it uses the carbons from Glycerol 3-Phosphate for phospholipids biosynthesis, respiration and further metabolism. In E. coli, many newly discovered structures of GlpD seem to play a role in the transfer of electrons into the respiratory pathway by catalytic dehyrogenation of GlpD. a The GlpD enzyme is a dimer consisting of two subunits which contain the flavin adenine dinucleotide (FAD) active site. <ref>PubMed:18296637</ref1>
===Structure===
GlpD is a dimer that consists of two subunits; α and β. The GlpD structure also consists of a Cap Domain Site, FAD-Binding Domain and a ubiquinone substrate analogue, menadione (MD).

<scene name='Sandbox_189/Cap_domain/1'>Cap-Binding Domain</scene>

The C-terminal Cap-Binding Domain (also known as Cap-Domain) consists of residues 389-501. This domain consists of negatively charged residues that are opposite in orientation to the positively charged residues of the FAD-Domain.

<scene name='Sandbox_189/Fad/2'>FAD Active Site</scene>

The N-terminal FAD-Binding Domain (also known as FAD-Domain) consists of residues 1 to 388. The FAD-Domain exists in each monomer subunit of GlpD and is embedded into the phospholipid membrane bilayer. Substrate binding occurs at this domain which causes a conformational change to the structure of the GlpD enzyme. The base of the enzyme has positivly charged regions capable of association with the negatively charged heads of the phospholipid membrane. <ref>PubMed:18296637</ref2>

===Function===

GlpD is associated in the intracellular membrane of E. coli and in the inner-mitochondrial membrane of eukaryotes.
GlpD in E. Coli catalyzes and oxidizes the reaction of glycerol 3-phosphate to dihydroxyacetone phosphate in the glycerol metabolic pathway. The binding of the substrate analogues and GlpD, a conformational change of the structure of the GlpD occurs.

Upon the oxidation of glycerol 3-phosphate, flavin adenine dinucleotide (FAD) reduces to FADH2, passing on electrons to Ubiquinone(UQ). UQ then reduces to UQH2 which allows for the transport of electrons into the respiratory pathway.

====Metabolism====
===Diseases===
===References===

[[Image:FINAL.png|thumb|Glycerol 3-Phosphate Dehydrogenase]]

<table style="background-color:#ffffc0" cellpadding="8" width="95%" border="0"><tr><td>Please do NOT make changes to this Sandbox until after April 23, 2010. Sandboxes 151-200 are reserved until then for use by the Chemistry 307 class at UNBC taught by Prof. [[User:Andrea Gorrell|Andrea Gorrell]].</td></tr>

Glycerol-3-Phosphate Dehydrogenase

2010-04-01T04:02:04Z

Indu Toora:

{{STRUCTURE_2r4e| PDB=2r4e | SCENE=Sandbox_189/Mynewscene/1 }}
'''Glycerol 3-Phosphate Dehydrogenase'''

===Introduction===

Glycerol 3-phosphate dehydrogenase (GlpD) is a membrane bound enzyme in prokaryotes and in eukaryotes. Glycerol 3-Phosphate Dehydrogenase (GlpD) is an oxidoreductase enzyme which catalyzes the reduction [http://en.wikipedia.org/wiki/File:Dihydroxyacetone_phosphate_to_glycerol_3-phosphate_en.svg reaction]of Dihydroxyacetone Phosphate to Glycerol 3-Phosphate. GlpD is involved in many cellular functions, where it uses the carbons from Glycerol 3-Phosphate for phospholipids biosynthesis, respiration and further metabolism. In E. coli, many newly discovered structures of GlpD seem to play a role in the transfer of electrons into the respiratory pathway by catalytic dehyrogenation of GlpD. a The GlpD enzyme is a dimer consisting of two subunits which contain the flavin adenine dinucleotide (FAD) active site. <ref>PubMed:18296637</ref1>

===Structure===

GlpD is a dimer that consists of two subunits; α and β. The GlpD structure also consists of a Cap Domain Site, FAD-Binding Domain and a ubiquinone substrate analogue, menadione (MD).

<scene name='Sandbox_189/Cap_domain/1'>Cap-Binding Domain</scene>

The C-terminal Cap-Binding Domain (also known as Cap-Domain) consists of residues 389-501. This domain consists of negatively charged residues that are opposite in orientation to the positively charged residues of the FAD-Domain.

<scene name='Sandbox_189/Fad/2'>FAD Active Site</scene>

The N-terminal FAD-Binding Domain (also known as FAD-Domain) consists of residues 1 to 388. The FAD-Domain exists in each monomer subunit of GlpD and is embedded into the phospholipid membrane bilayer. Substrate binding occurs at this domain which causes a conformational change to the structure of the GlpD enzyme. The base of the enzyme has positivly charged regions capable of association with the negatively charged heads of the phospholipid membrane. <ref>PubMed:18296637</ref2>

===Function===

GlpD is associated in the intracellular membrane of E. coli and in the inner-mitochondrial membrane of eukaryotes.
GlpD in E. Coli catalyzes and oxidizes the reaction of glycerol 3-phosphate to dihydroxyacetone phosphate in the glycerol metabolic pathway. The binding of the substrate analogues and GlpD, a conformational change of the structure of the GlpD occurs.

Upon the oxidation of glycerol 3-phosphate, flavin adenine dinucleotide (FAD) reduces to FADH2, passing on electrons to Ubiquinone(UQ). UQ then reduces to UQH2 which allows for the transport of electrons into the respiratory pathway.

====Metabolism====
===Diseases===
===References===

[[Image:FINAL.png|thumb|Glycerol 3-Phosphate Dehydrogenase]]

<table style="background-color:#ffffc0" cellpadding="8" width="95%" border="0"><tr><td>Please do NOT make changes to this Sandbox until after April 23, 2010. Sandboxes 151-200 are reserved until then for use by the Chemistry 307 class at UNBC taught by Prof. [[User:Andrea Gorrell|Andrea Gorrell]].</td></tr>

Glycerol-3-Phosphate Dehydrogenase

2010-04-01T04:01:16Z

Indu Toora:

{{STRUCTURE_2r4e| PDB=2r4e | SCENE=Sandbox_189/Mynewscene/1 }}
'''Glycerol 3-Phosphate Dehydrogenase'''

===Introduction===

Glycerol 3-phosphate dehydrogenase (GlpD) is a membrane bound enzyme in prokaryotes and in eukaryotes. Glycerol 3-Phosphate Dehydrogenase (GlpD) is an oxidoreductase enzyme which catalyzes the reduction [website http://en.wikipedia.org/wiki/File:Dihydroxyacetone_phosphate_to_glycerol_3-phosphate_en.svg reaction]of Dihydroxyacetone Phosphate to Glycerol 3-Phosphate. GlpD is involved in many cellular functions, where it uses the carbons from Glycerol 3-Phosphate for phospholipids biosynthesis, respiration and further metabolism. In E. coli, many newly discovered structures of GlpD seem to play a role in the transfer of electrons into the respiratory pathway by catalytic dehyrogenation of GlpD. a The GlpD enzyme is a dimer consisting of two subunits which contain the flavin adenine dinucleotide (FAD) active site. <ref>PubMed:18296637</ref1>

===Structure===

GlpD is a dimer that consists of two subunits; α and β. The GlpD structure also consists of a Cap Domain Site, FAD-Binding Domain and a ubiquinone substrate analogue, menadione (MD).

<scene name='Sandbox_189/Cap_domain/1'>Cap-Binding Domain</scene>

The C-terminal Cap-Binding Domain (also known as Cap-Domain) consists of residues 389-501. This domain consists of negatively charged residues that are opposite in orientation to the positively charged residues of the FAD-Domain.

<scene name='Sandbox_189/Fad/2'>FAD Active Site</scene>

The N-terminal FAD-Binding Domain (also known as FAD-Domain) consists of residues 1 to 388. The FAD-Domain exists in each monomer subunit of GlpD and is embedded into the phospholipid membrane bilayer. Substrate binding occurs at this domain which causes a conformational change to the structure of the GlpD enzyme. The base of the enzyme has positivly charged regions capable of association with the negatively charged heads of the phospholipid membrane. <ref>PubMed:18296637</ref2>

===Function===

GlpD is associated in the intracellular membrane of E. coli and in the inner-mitochondrial membrane of eukaryotes.
GlpD in E. Coli catalyzes and oxidizes the reaction of glycerol 3-phosphate to dihydroxyacetone phosphate in the glycerol metabolic pathway. The binding of the substrate analogues and GlpD, a conformational change of the structure of the GlpD occurs.

Upon the oxidation of glycerol 3-phosphate, flavin adenine dinucleotide (FAD) reduces to FADH2, passing on electrons to Ubiquinone(UQ). UQ then reduces to UQH2 which allows for the transport of electrons into the respiratory pathway.

====Metabolism====
===Diseases===
===References===

[[Image:FINAL.png|thumb|Glycerol 3-Phosphate Dehydrogenase]]

<table style="background-color:#ffffc0" cellpadding="8" width="95%" border="0"><tr><td>Please do NOT make changes to this Sandbox until after April 23, 2010. Sandboxes 151-200 are reserved until then for use by the Chemistry 307 class at UNBC taught by Prof. [[User:Andrea Gorrell|Andrea Gorrell]].</td></tr>

Glycerol-3-Phosphate Dehydrogenase

2010-04-01T03:38:23Z

Indu Toora:

{{STRUCTURE_2r4e| PDB=2r4e | SCENE=Sandbox_189/Mynewscene/1 }}
'''Glycerol 3-Phosphate Dehydrogenase'''

===Introduction===

Glycerol 3-Phosphate Dehydrogenase (GlpD) is an oxidoreductase enzyme which catalyzes the reaction of transfer of electrons between molecules. GlpD is a membrane associated enzyme that is involved in glycerol metabolism, ubiquinone, glyceroneogenesis and respiratrion in E. coli. In Ecoli, many newly discovered structures of GlpD are being used to aid in transfer of electrons into the respiratory pathway and also for the metabolism of glycerol into its precursors for other pathways. The GlpD enzyme contains a flavin adenine dinucleotide (FAD active site which plays a major role in the respiratory electron transport chain and in synthesis of cellular components. <ref>PubMed:18296637</ref1>

===Structure===

GlpD is a dimer that consists of two subunits; α and β. The GlpD structure also consists of a Cap Domain Site, FAD-Binding Domain and a ubiquinone substrate analogue, menadione (MD).

<scene name='Sandbox_189/Cap_domain/1'>Cap-Binding Domain</scene>

The C-terminal Cap-Binding Domain (also known as Cap-Domain) consists of residues 389-501. This domain consists of negatively charged residues that are opposite in orientation to the positively charged residues of the FAD-Domain.

<scene name='Sandbox_189/Fad/2'>FAD Active Site</scene>

The N-terminal FAD-Binding Domain (also known as FAD-Domain) consists of residues 1 to 388. The FAD-Domain exists in each monomer subunit of GlpD and is embedded into the phospholipid membrane bilayer. Substrate binding occurs at this domain which causes a conformational change to the structure of the GlpD enzyme. The base of the enzyme has positivly charged regions capable of association with the negatively charged heads of the phospholipid membrane. <ref>PubMed:18296637</ref2>

===Function===

GlpD is associated in the intracellular membrane of E. coli and in the inner-mitochondrial membrane of eukaryotes.
GlpD in E. Coli catalyzes and oxidizes the reaction of glycerol 3-phosphate to dihydroxyacetone phosphate in the glycerol metabolic pathway. The binding of the substrate analogues and GlpD, a conformational change of the structure of the GlpD occurs.

Upon the oxidation of glycerol 3-phosphate, flavin adenine dinucleotide (FAD) reduces to FADH2, passing on electrons to Ubiquinone(UQ). UQ then reduces to UQH2 which allows for the transport of electrons into the respiratory pathway.

====Metabolism====
===Diseases===
===References===

[[Image:FINAL.png|thumb|Glycerol 3-Phosphate Dehydrogenase]]

<table style="background-color:#ffffc0" cellpadding="8" width="95%" border="0"><tr><td>Please do NOT make changes to this Sandbox until after April 23, 2010. Sandboxes 151-200 are reserved until then for use by the Chemistry 307 class at UNBC taught by Prof. [[User:Andrea Gorrell|Andrea Gorrell]].</td></tr>

Glycerol-3-Phosphate Dehydrogenase

2010-04-01T03:19:34Z

Indu Toora:

{{STRUCTURE_2r4e| PDB=2r4e | SCENE=Sandbox_189/Mynewscene/1 }}
'''Glycerol 3-Phosphate Dehydrogenase'''

===Introduction===

Glycerol 3-Phosphate Dehydrogenase (GlpD) is an oxidoreductase enzyme which catalyzes the reaction of transfer of electrons between molecules. GlpD is a membrane associated enzyme that is involved in glycerol metabolism, ubiquinone, glyceroneogenesis and respiratrion in E. coli. In Ecoli, many newly discovered structures of GlpD are being used to aid in transfer of electrons into the respiratory pathway and also for the metabolism of glycerol into its precursors for other pathways. The GlpD enzyme contains a flavin adenine dinucleotide (FAD active site which plays a major role in the respiratory electron transport chain and in synthesis of cellular components. <ref>PubMed:18296637</ref1>

===Structure===
GlpD is a dimer that consists of two subunits; α and β. The GlpD structure also consists of a Cap Domain Site, FAD-Binding Domain and a ubiquinone substrate analogue, menadione (MD).

<scene name='Sandbox_189/Cap_domain/1'>TextToBeDisplayed</scene>

The C-terminal Cap-Binding Domain (also known as Cap-Domain) consists of residues 389-501. This domain consists of negatively charged residues that are opposite in orientation to the positively charged residues of the FAD-Domain.

<scene name='Sandbox_189/Fad/2'>FAD Active Site</scene>

The N-terminal FAD-Binding Domain (also known as FAD-Domain) consists of residues 1 to 388. The FAD-Domain exists in each monomer subunit of GlpD and is embedded into the phospholipid membrane bilayer. Substrate binding occurs at this domain which causes a conformational change to the structure of the GlpD enzyme. The base of the enzyme has positivly charged regions capable of association with the negatively charged heads of the phospholipid membrane. <ref>PubMed:18296637</ref2>

===Function===
GlpD is associated in the intracellular membrane of E. coli and in the inner-mitochondrial membrane of eukaryotes.
GlpD in E. Coli catalyzes the reaction and oxidizes glycerol 3-phosphate to dihydroxyacetone phosphate in the glycerol metabolic pathway. Upon the oxidation of glycerol 3-phosphate, flavin adenine dinucleotide (FAD) reduces to FADH2, passing on electrons to Ubiquinone(UQ). UQ then reduces to UQH2 which allows for the transport of electrons into the respiratory pathway.

====Metabolism====
===Diseases===
===References===

[[Image:FINAL.png|thumb|Glycerol 3-Phosphate Dehydrogenase]]

<table style="background-color:#ffffc0" cellpadding="8" width="95%" border="0"><tr><td>Please do NOT make changes to this Sandbox until after April 23, 2010. Sandboxes 151-200 are reserved until then for use by the Chemistry 307 class at UNBC taught by Prof. [[User:Andrea Gorrell|Andrea Gorrell]].</td></tr>

Glycerol-3-Phosphate Dehydrogenase

2010-04-01T03:18:32Z

Indu Toora:

{{STRUCTURE_2r4e| PDB=2r4e | SCENE=Sandbox_172/Mynewscene/1 }}
'''Glycerol 3-Phosphate Dehydrogenase'''

===Introduction===

Glycerol 3-Phosphate Dehydrogenase (GlpD) is an oxidoreductase enzyme which catalyzes the reaction of transfer of electrons between molecules. GlpD is a membrane associated enzyme that is involved in glycerol metabolism, ubiquinone, glyceroneogenesis and respiratrion in E. coli. In Ecoli, many newly discovered structures of GlpD are being used to aid in transfer of electrons into the respiratory pathway and also for the metabolism of glycerol into its precursors for other pathways. The GlpD enzyme contains a flavin adenine dinucleotide (FAD active site which plays a major role in the respiratory electron transport chain and in synthesis of cellular components. <ref>PubMed:18296637</ref1>

===Structure===
GlpD is a dimer that consists of two subunits; α and β. The GlpD structure also consists of a Cap Domain Site, FAD-Binding Domain and a ubiquinone substrate analogue, menadione (MD).

<scene name='Sandbox_189/Cap_domain/1'>TextToBeDisplayed</scene>

The C-terminal Cap-Binding Domain (also known as Cap-Domain) consists of residues 389-501. This domain consists of negatively charged residues that are opposite in orientation to the positively charged residues of the FAD-Domain.

<scene name='Sandbox_189/Fad/2'>FAD Active Site</scene>

The N-terminal FAD-Binding Domain (also known as FAD-Domain) consists of residues 1 to 388. The FAD-Domain exists in each monomer subunit of GlpD and is embedded into the phospholipid membrane bilayer. Substrate binding occurs at this domain which causes a conformational change to the structure of the GlpD enzyme. The base of the enzyme has positivly charged regions capable of association with the negatively charged heads of the phospholipid membrane. <ref>PubMed:18296637</ref2>

===Function===
GlpD is associated in the intracellular membrane of E. coli and in the inner-mitochondrial membrane of eukaryotes.
GlpD in E. Coli catalyzes the reaction and oxidizes glycerol 3-phosphate to dihydroxyacetone phosphate in the glycerol metabolic pathway. Upon the oxidation of glycerol 3-phosphate, flavin adenine dinucleotide (FAD) reduces to FADH2, passing on electrons to Ubiquinone(UQ). UQ then reduces to UQH2 which allows for the transport of electrons into the respiratory pathway.

====Metabolism====
===Diseases===
===References===

[[Image:FINAL.png|thumb|Glycerol 3-Phosphate Dehydrogenase]]

<table style="background-color:#ffffc0" cellpadding="8" width="95%" border="0"><tr><td>Please do NOT make changes to this Sandbox until after April 23, 2010. Sandboxes 151-200 are reserved until then for use by the Chemistry 307 class at UNBC taught by Prof. [[User:Andrea Gorrell|Andrea Gorrell]].</td></tr>

Glycerol-3-Phosphate Dehydrogenase

2010-04-01T02:01:35Z

Indu Toora:

'''Glycerol 3-Phosphate Dehydrogenase'''

{{STRUCTURE_2r4e| PDB=2r4e | SCENE=Sandbox_172/Mynewscene/1 }}

===Introduction===

Glycerol 3-Phosphate Dehydrogenase (GlpD) is an oxidoreductase enzyme which catalyzes the reaction of transfer of electrons between molecules. GlpD is a membrane associated enzyme that is involved in glycerol metabolism, ubiquinone, glyceroneogenesis and respiratrion in E. coli. In Ecoli, many newly discovered structures of GlpD are being used to aid in transfer of electrons into the respiratory pathway and also for the metabolism of glycerol into its precursors for other pathways. The GlpD enzyme contains a flavin adenine dinucleotide (FAD active site which plays a major role in the respiratory electron transport chain and in synthesis of cellular components. <ref>PubMed:18296637</ref1>

===Structure===
GlpD is a dimer that consists of two subunits; α and β. The GlpD structure also consists of a Cap Domain Site, FAD-Binding Domain and a ubiquinone substrate analogue, menadione (MD).

<scene name='Sandbox_189/Cap_domain/1'>TextToBeDisplayed</scene>

The C-terminal Cap-Binding Domain (also known as Cap-Domain) consists of residues 389-501. This domain consists of negatively charged residues that are opposite in orientation to the positively charged residues of the FAD-Domain.

<scene name='Sandbox_189/Fad/2'>FAD Active Site</scene>

The N-terminal FAD-Binding Domain (also known as FAD-Domain) consists of residues 1 to 388. The FAD-Domain exists in each monomer subunit of GlpD and is embedded into the phospholipid membrane bilayer. Substrate binding occurs at this domain which causes a conformational change to the structure of the GlpD enzyme. The base of the enzyme has positivly charged regions capable of association with the negatively charged heads of the phospholipid membrane. <ref>PubMed:18296637</ref2>

===Function===
GlpD is associated in the intracellular membrane of E. coli and in the inner-mitochondrial membrane of eukaryotes.
GlpD in E. Coli catalyzes the reaction and oxidizes glycerol 3-phosphate to dihydroxyacetone phosphate in the glycerol metabolic pathway. Upon the oxidation of glycerol 3-phosphate, flavin adenine dinucleotide (FAD) reduces to FADH2, passing on electrons to Ubiquinone(UQ). UQ then reduces to UQH2 which allows for the transport of electrons into the respiratory pathway.

====Metabolism====
===Diseases===
===References===

[[Image:FINAL.png|thumb|Glycerol 3-Phosphate Dehydrogenase]]

<table style="background-color:#ffffc0" cellpadding="8" width="95%" border="0"><tr><td>Please do NOT make changes to this Sandbox until after April 23, 2010. Sandboxes 151-200 are reserved until then for use by the Chemistry 307 class at UNBC taught by Prof. [[User:Andrea Gorrell|Andrea Gorrell]].</td></tr>

Glycerol-3-Phosphate Dehydrogenase

2010-04-01T01:30:11Z

Indu Toora:

'''Glycerol 3-Phosphate Dehydrogenase'''

{{STRUCTURE_2r4e| PDB=2r4e | SCENE=Sandbox_172/Mynewscene/1 }}

===Introduction===

Glycerol 3-Phosphate Dehydrogenase (GlpD) is an oxidoreductase enzyme which catalyzes the reaction of transfer of electrons between molecules. GlpD is a membrane associated enzyme that is involved in glycerol metabolism, ubiquinone, glyceroneogenesis and respiratrion in E. coli. In Ecoli, many newly discovered structures of GlpD are being used to aid in transfer of electrons into the respiratory pathway and also for the metabolism of glycerol into its precursors for other pathways. The GlpD enzyme contains a flavin adenine dinucleotide (FAD active site which plays a major role in the respiratory electron transport chain and in synthesis of cellular components. <ref>PubMed:18296637</ref1>

===Structure===
GlpD is a dimer that consists of two subunits; α and β. The GlpD structure also consists of a Cap Domain Site, FAD-Binding Domain and a ubiquinone substrate analogue, menadione (MD).

<scene name='Sandbox_189/Cap_domain/1'>TextToBeDisplayed</scene>

The C-terminal Cap-Binding Domain (also known as Cap-Domain) consists of residues 389-501. This domain consists of negatively charged residues that are opposite in orientation to the positively charged residues of the FAD-Domain.

<scene name='Sandbox_189/Fad/2'>FAD Active Site</scene>

The N-terminal FAD-Binding Domain (also known as FAD-Domain) consists of residues 1 to 388. The FAD-Domain exists in each monomer subunit of GlpD and is embedded into the phospholipid membrane bilayer. Substrate binding occurs at this domain which causes a conformational change to the structure of the GlpD enzyme. The base of the enzyme has positivly charged regions capable of association with the negatively charged heads of the phospholipid membrane. <ref>PubMed:18296637</ref2>

===Function===
GlpD is associated in the intracellular membrane of E. coli and in the inner-mitochondrial membrane of eukaryotes.
GlpD in E. Coli catalyzes the reaction and oxidizes glycerol 3-phosphate to dihydroxyacetone phosphate in the glycerol metabolic pathway. Upon the oxidation of glycerol 3-phosphate, flavin adenine dinucleotide (FAD) reduces to FADH2, passing on electrons to Ubiquinone(UQ). UQ then reduces to UQH2 which allows for electrons to pass to nitrate or oxygen.
====Metabolism====
===Diseases===
===References===

[[Image:FINAL.png|thumb|Glycerol 3-Phosphate Dehydrogenase]]

<table style="background-color:#ffffc0" cellpadding="8" width="95%" border="0"><tr><td>Please do NOT make changes to this Sandbox until after April 23, 2010. Sandboxes 151-200 are reserved until then for use by the Chemistry 307 class at UNBC taught by Prof. [[User:Andrea Gorrell|Andrea Gorrell]].</td></tr>

Glycerol-3-Phosphate Dehydrogenase

2010-04-01T01:29:38Z

Indu Toora:

'''Glycerol 3-Phosphate Dehydrogenase'''

{{STRUCTURE_2r4e| PDB=2r4e | SCENE=Sandbox_172/Mynewscene/1 }}

===Introduction ==

Glycerol 3-Phosphate Dehydrogenase (GlpD) is an oxidoreductase enzyme which catalyzes the reaction of transfer of electrons between molecules. GlpD is a membrane associated enzyme that is involved in glycerol metabolism, ubiquinone, glyceroneogenesis and respiratrion in E. coli. In Ecoli, many newly discovered structures of GlpD are being used to aid in transfer of electrons into the respiratory pathway and also for the metabolism of glycerol into its precursors for other pathways. The GlpD enzyme contains a flavin adenine dinucleotide (FAD active site which plays a major role in the respiratory electron transport chain and in synthesis of cellular components. <ref>PubMed:18296637</ref1>

===Structure===
GlpD is a dimer that consists of two subunits; α and β. The GlpD structure also consists of a Cap Domain Site, FAD-Binding Domain and a ubiquinone substrate analogue, menadione (MD).

<scene name='Sandbox_189/Cap_domain/1'>TextToBeDisplayed</scene>

The C-terminal Cap-Binding Domain (also known as Cap-Domain) consists of residues 389-501. This domain consists of negatively charged residues that are opposite in orientation to the positively charged residues of the FAD-Domain.

<scene name='Sandbox_189/Fad/2'>FAD Active Site</scene>

The N-terminal FAD-Binding Domain (also known as FAD-Domain) consists of residues 1 to 388. The FAD-Domain exists in each monomer subunit of GlpD and is embedded into the phospholipid membrane bilayer. Substrate binding occurs at this domain which causes a conformational change to the structure of the GlpD enzyme. The base of the enzyme has positivly charged regions capable of association with the negatively charged heads of the phospholipid membrane. <ref>PubMed:18296637</ref2>

===Function===
GlpD is associated in the intracellular membrane of E. coli and in the inner-mitochondrial membrane of eukaryotes.
GlpD in E. Coli catalyzes the reaction and oxidizes glycerol 3-phosphate to dihydroxyacetone phosphate in the glycerol metabolic pathway. Upon the oxidation of glycerol 3-phosphate, flavin adenine dinucleotide (FAD) reduces to FADH2, passing on electrons to Ubiquinone(UQ). UQ then reduces to UQH2 which allows for electrons to pass to nitrate or oxygen.
====Metabolism====
===Diseases===
===References===

[[Image:FINAL.png|thumb|Glycerol 3-Phosphate Dehydrogenase]]

<table style="background-color:#ffffc0" cellpadding="8" width="95%" border="0"><tr><td>Please do NOT make changes to this Sandbox until after April 23, 2010. Sandboxes 151-200 are reserved until then for use by the Chemistry 307 class at UNBC taught by Prof. [[User:Andrea Gorrell|Andrea Gorrell]].</td></tr>

Glycerol-3-Phosphate Dehydrogenase

2010-04-01T01:27:19Z

Indu Toora:

'''Glycerol 3-Phosphate Dehydrogenase'''

{{STRUCTURE_2r4e| PDB=2r4e | SCENE=Sandbox_172/Mynewscene/1 }}

== Introduction ==

Glycerol 3-Phosphate Dehydrogenase (GlpD) is an oxidoreductase enzyme which catalyzes the reaction of transfer of electrons between molecules. GlpD is a membrane associated enzyme that is involved in glycerol metabolism, ubiquinone, glyceroneogenesis and respiratrion in E. coli. In Ecoli, many newly discovered structures of GlpD are being used to aid in transfer of electrons into the respiratory pathway and also for the metabolism of glycerol into its precursors for other pathways. The GlpD enzyme contains a flavin adenine dinucleotide (FAD active site which plays a major role in the respiratory electron transport chain and in synthesis of cellular components. <ref>PubMed:18296637</ref1>

===Structure===
GlpD is a dimer that consists of two subunits; α and β. The GlpD structure also consists of a Cap Domain Site, FAD-Binding Domain and a ubiquinone substrate analogue, menadione (MD).

<scene name='Sandbox_189/Cap_domain/1'>TextToBeDisplayed</scene>

The C-terminal Cap-Binding Domain (also known as Cap-Domain) consists of residues 389-501. This domain consists of negatively charged residues that are opposite in orientation to the positively charged residues of the FAD-Domain.

<scene name='Sandbox_189/Fad/2'>FAD Active Site</scene>

The N-terminal FAD-Binding Domain (also known as FAD-Domain) consists of residues 1 to 388. The FAD-Domain exists in each monomer subunit of GlpD and is embedded into the phospholipid membrane bilayer. Substrate binding occurs at this domain which causes a conformational change to the structure of the GlpD enzyme. The base of the enzyme has positivly charged regions capable of association with the negatively charged heads of the phospholipid membrane. <ref>PubMed:18296637</ref2>

===Function===
GlpD is associated in the intracellular membrane of E. coli and in the inner-mitochondrial membrane of eukaryotes.
GlpD in E. Coli catalyzes the reaction and oxidizes glycerol 3-phosphate to dihydroxyacetone phosphate in the glycerol metabolic pathway. Upon the oxidation of glycerol 3-phosphate, flavin adenine dinucleotide (FAD) reduces to FADH2, passing on electrons to Ubiquinone(UQ). UQ then reduces to UQH2 which allows for electrons to pass to nitrate or oxygen.
====Metabolism====
===Diseases===
===References===

[[Image:FINAL.png|thumb|Glycerol 3-Phosphate Dehydrogenase]]

<table style="background-color:#ffffc0" cellpadding="8" width="95%" border="0"><tr><td>Please do NOT make changes to this Sandbox until after April 23, 2010. Sandboxes 151-200 are reserved until then for use by the Chemistry 307 class at UNBC taught by Prof. [[User:Andrea Gorrell|Andrea Gorrell]].</td></tr>

Glycerol-3-Phosphate Dehydrogenase

2010-04-01T00:37:28Z

Indu Toora:

'''Glycerol 3-Phosphate Dehydrogenase'''

{{STRUCTURE_2r4e| PDB=2r4e | SCENE=Sandbox_172/Mynewscene/1 }}

== Introduction ==

Glycerol 3-Phosphate Dehydrogenase (GlpD) is an oxidoreductase enzyme which catalyzes the reaction of transfer of electrons between molecules. GlpD is a membrane associated enzyme that is involved in glycerol metabolism, ubiquinone, glyceroneogenesis and respiratrion in E. coli. In Ecoli, many newly discovered structures of GlpD are being used to aid in transfer of electrons into the respiratory pathway and also for the metabolism of glycerol into its precursors for other pathways. The GlpD enzyme contains a flavin adenine dinucleotide (FAD active site which plays a major role in the respiratory electron transport chain and in synthesis of cellular components. <ref>PubMed:18296637</ref1>

===Structure===
GlpD is a dimer that consists of two chains; α and β. The GlpD structure also consists of a Cap Domain Site, FAD-Binding Domain and a ubiquinone substrate analogue, menadione (MD).

<scene name='Sandbox_189/Fad/2'>FAD Active Site</scene>

The N-terminal FAD-Binding Domain (also known as FAD-Domain) consists of residues 1 to 388. The FAD-Domain of GlpD is embedded into the phospholipid membrane bilayer.

===Function===
GlpD is associated in the intracellular membrane of E. coli and in the inner-mitochondrial membrane of eukaryotes.
GlpD in E. Coli catalyzes the reaction and oxidizes glycerol 3-phosphate to dihydroxyacetone phosphate in the glycerol metabolic pathway. Upon the oxidation of glycerol 3-phosphate, flavin adenine dinucleotide (FAD) reduces to FADH2, passing on electrons to Ubiquinone(UQ). UQ then reduces to UQH2 which allows for electrons to pass to nitrate or oxygen.
====Metabolism====
===Diseases===
===References===

[[Image:FINAL.png|thumb|Glycerol 3-Phosphate Dehydrogenase]]

<table style="background-color:#ffffc0" cellpadding="8" width="95%" border="0"><tr><td>Please do NOT make changes to this Sandbox until after April 23, 2010. Sandboxes 151-200 are reserved until then for use by the Chemistry 307 class at UNBC taught by Prof. [[User:Andrea Gorrell|Andrea Gorrell]].</td></tr>

Glycerol-3-Phosphate Dehydrogenase

2010-04-01T00:29:00Z

Indu Toora:

'''Glycerol 3-Phosphate Dehydrogenase'''

{{STRUCTURE_2r4e| PDB=2r4e | SCENE=Sandbox_172/Mynewscene/1 }}

== Introduction ==

Glycerol 3-Phosphate Dehydrogenase (GlpD) is an oxidoreductase enzyme which catalyzes the reaction of transfer of electrons between molecules. GlpD is a membrane associated enzyme that is involved in glycerol metabolism, ubiquinone, glyceroneogenesis and respiratrion in E. coli. In Ecoli, many newly discovered structures of GlpD are being used to aid in transfer of electrons into the respiratory pathway and also for the metabolism of glycerol into its precursors for other pathways. The GlpD enzyme contains a flavin adenine dinucleotide (FAD)active site which plays a major role in the respiratory electron transport chain and in synthesis of cellular components. <ref>PubMed:18296637</ref1>

===Structure===
GlpD is a dimer that consists of two chains; α and β. The GlpD structure also consists of a Cap Domain Site, FAD-Binding Domain and a ubiquinone substrate analogue, menadione (MD).

<scene name='Sandbox_189/Fad/2'>FAD Active Site</scene>

The N-terminal FAD-Binding Domain (also known as FAD-Domain) consists of residues 1 to 388. The FAD-Domain of GlpD is embedded into the phospholipid membrane bilayer.

===Function===
GlpD is associated in the intracellular membrane of E. coli and in the inner-mitochondrial membrane of eukaryotes.
GlpD in E. Coli catalyzes the reaction and oxidizes glycerol 3-phosphate to dihydroxyacetone phosphate in the glycerol metabolic pathway. Upon the oxidation of glycerol 3-phosphate, flavin adenine dinucleotide (FAD) reduces to FADH2, passing on electrons to Ubiquinone(UQ). UQ then reduces to UQH2 which allows for electrons to pass to nitrate or oxygen.
====Metabolism====
===Diseases===
===References===

[[Image:FINAL.png|thumb|Glycerol 3-Phosphate Dehydrogenase]]

<table style="background-color:#ffffc0" cellpadding="8" width="95%" border="0"><tr><td>Please do NOT make changes to this Sandbox until after April 23, 2010. Sandboxes 151-200 are reserved until then for use by the Chemistry 307 class at UNBC taught by Prof. [[User:Andrea Gorrell|Andrea Gorrell]].</td></tr>

Glycerol-3-Phosphate Dehydrogenase

2010-04-01T00:24:40Z

Indu Toora:

'''Glycerol 3-Phosphate Dehydrogenase'''

{{STRUCTURE_2r4e| PDB=2r4e | SCENE=Sandbox_172/Mynewscene/1 }}

== Introduction ==

Glycerol 3-Phosphate Dehydrogenase (GlpD) is an oxidoreductase enzyme which catalyzes the reaction of transfer of electrons between molecules. GlpD is a membrane associated enzyme that is involved in glycerol metabolism, ubiquinone, glyceroneogenesis and respiratrion in E. coli. In Ecoli, many newly discovered structures of GlpD are being used to aid in transfer of electrons into the respiratory pathway and also for the metabolism of glycerol into its precursors for other pathways. The GlpD enzyme contains a flavin adenine dinucleotide (FAD)active site which plays a major role in the respiratory electron transport chain and in synthesis of cellular components.

===Structure===
GlpD is a dimer that consists of two chains; α and β. The GlpD structure also consists of a Cap Domain Site, FAD-Binding Domain and a ubiquinone substrate analogue, menadione (MD).

<scene name='Sandbox_189/Fad/2'>FAD Active Site</scene>

The N-terminal FAD-Binding Domain (also known as FAD-Domain) consists of residues 1 to 388. The FAD-Domain of GlpD is embedded into the phospholipid membrane bilayer.

===Function===
GlpD is associated in the intracellular membrane of E. coli and in the inner-mitochondrial membrane of eukaryotes.
GlpD in E. Coli catalyzes the reaction and oxidizes glycerol 3-phosphate to dihydroxyacetone phosphate in the glycerol metabolic pathway. Upon the oxidation of glycerol 3-phosphate, flavin adenine dinucleotide (FAD) reduces to FADH2, passing on electrons to Ubiquinone(UQ). UQ then reduces to UQH2 which allows for electrons to pass to nitrate or oxygen.
====Metabolism====
===Diseases===

[[Image:FINAL.png|thumb|Glycerol 3-Phosphate Dehydrogenase]]

<table style="background-color:#ffffc0" cellpadding="8" width="95%" border="0"><tr><td>Please do NOT make changes to this Sandbox until after April 23, 2010. Sandboxes 151-200 are reserved until then for use by the Chemistry 307 class at UNBC taught by Prof. [[User:Andrea Gorrell|Andrea Gorrell]].</td></tr>

Glycerol-3-Phosphate Dehydrogenase

2010-04-01T00:21:56Z

Indu Toora:

'''Glycerol 3-Phosphate Dehydrogenase'''

{{STRUCTURE_2r4e| PDB=2r4e | SCENE=Sandbox_172/Mynewscene/1 }}

== Introduction ==

Glycerol 3-Phosphate Dehydrogenase (GlpD) is an oxidoreductase enzyme which catalyzes the reaction of transfer of electrons between molecules. GlpD is a membrane associated enzyme that is involved in glycerol metabolism, ubiquinone, glyceroneogenesis and respiratrion in E. coli. In Ecoli, many newly discovered structures of GlpD are being used to aid in transfer of electrons into the respiratory pathway and also for the metabolism of glycerol into its precursors for other pathways. The GlpD enzyme contains a flavin adenine dinucleotide (FAD)active site which plays a major role in the respiratory electron transport chain and in synthesis of cellular components.

===Structure===
GlpD is a dimer that consists of two chains; α and β. The GlpD structure also consists of a Cap Domain Site, FAD-Binding Domain and a ubiquinone substrate analogue, menadione (MD).

<scene name='Sandbox_189/Fad/2'>FAD Active Site</scene>

The N-terminal FAD-Binding Domain region consists of residues from 1 to 388. The FAD-Binding Domain of GlpD is embedded into the phospholipid membrane bilayer.

===Function===
GlpD is associated in the intracellular membrane of E. coli and in the inner-mitochondrial membrane of eukaryotes.
GlpD in E. Coli catalyzes the reaction and oxidizes glycerol 3-phosphate to dihydroxyacetone phosphate in the glycerol metabolic pathway. Upon the oxidation of glycerol 3-phosphate, flavin adenine dinucleotide (FAD) reduces to FADH2, passing on electrons to Ubiquinone(UQ). UQ then reduces to UQH2 which allows for electrons to pass to nitrate or oxygen.
====Metabolism====
===Diseases===

[[Image:FINAL.png|thumb|Glycerol 3-Phosphate Dehydrogenase]]

<table style="background-color:#ffffc0" cellpadding="8" width="95%" border="0"><tr><td>Please do NOT make changes to this Sandbox until after April 23, 2010. Sandboxes 151-200 are reserved until then for use by the Chemistry 307 class at UNBC taught by Prof. [[User:Andrea Gorrell|Andrea Gorrell]].</td></tr>

Glycerol-3-Phosphate Dehydrogenase

2010-04-01T00:21:05Z

Indu Toora:

'''Glycerol 3-Phosphate Dehydrogenase'''

{{STRUCTURE_2r4e| PDB=2r4e | SCENE=Sandbox_172/Mynewscene/1 }}

== Introduction ==

Glycerol 3-Phosphate Dehydrogenase (GlpD) is an oxidoreductase enzyme which catalyzes the reaction of transfer of electrons between molecules. GlpD is a membrane associated enzyme that is involved in glycerol metabolism, ubiquinone, glyceroneogenesis and respiratrion in E. coli. In Ecoli, many newly discovered structures of GlpD are being used to aid in transfer of electrons into the respiratory pathway and also for the metabolism of glycerol into its precursors for other pathways. The GlpD enzyme contains a flavin adenine dinucleotide (FAD)active site which plays a major role in the respiratory electron transport chain and in synthesis of cellular components.

===Structure===
GlpD is a dimer that consists of two chains; α and β. The GlpD structure also consists of a Cap Domain Site, FAD-Binding Domain and a ubiquinone substrate analogue, menadione (MD).

<scene name='Sandbox_189/Fad/2'>FAD Active Site</scene>
The N-terminal FAD-Binding Domain region consists of residues from 1 to 388. The FAD-Binding Domain of GlpD is embedded into the phospholipid membrane bilayer.

===Function===
GlpD is associated in the intracellular membrane of E. coli and in the inner-mitochondrial membrane of eukaryotes.
GlpD in E. Coli catalyzes the reaction and oxidizes glycerol 3-phosphate to dihydroxyacetone phosphate in the glycerol metabolic pathway. Upon the oxidation of glycerol 3-phosphate, flavin adenine dinucleotide (FAD) reduces to FADH2, passing on electrons to Ubiquinone(UQ). UQ then reduces to UQH2 which allows for electrons to pass to nitrate or oxygen.
====Metabolism====
===Diseases===

[[Image:FINAL.png|thumb|Glycerol 3-Phosphate Dehydrogenase]]

<table style="background-color:#ffffc0" cellpadding="8" width="95%" border="0"><tr><td>Please do NOT make changes to this Sandbox until after April 23, 2010. Sandboxes 151-200 are reserved until then for use by the Chemistry 307 class at UNBC taught by Prof. [[User:Andrea Gorrell|Andrea Gorrell]].</td></tr>

Glycerol-3-Phosphate Dehydrogenase

2010-04-01T00:15:23Z

Indu Toora:

'''Glycerol 3-Phosphate Dehydrogenase'''

{{STRUCTURE_2r4e| PDB=2r4e | SCENE=Sandbox_172/Mynewscene/1 }}

== Introduction ==

Glycerol 3-Phosphate Dehydrogenase (GlpD) is an oxidoreductase enzyme which catalyzes the reaction of transfer of electrons between molecules. GlpD is a membrane associated enzyme that is involved in glycerol metabolism, ubiquinone, glyceroneogenesis and respiratrion in E. coli. In Ecoli, many newly discovered structures of GlpD are being used to aid in transfer of electrons into the respiratory pathway and also for the metabolism of glycerol into its precursors for other pathways. The GlpD enzyme contains a flavin adenine dinucleotide (FAD)active site which plays a major role in the respiratory electron transport chain and in synthesis of cellular components.

===Structure===
GlpD is a dimer that consists of two chains; α and β. The GlpD structure also consists of a Cap Domain Site, FAD-Binding Domain and a ubiquinone substrate analogue, menadione (MD).

FAD Active Site
<scene name='Sandbox_189/Fad/2'>FAD Active Site</scene>

===Function===
GlpD is associated in the intracellular membrane of E. coli and in the inner-mitochondrial membrane of eukaryotes.
GlpD in E. Coli catalyzes the reaction and oxidizes glycerol 3-phosphate to dihydroxyacetone phosphate in the glycerol metabolic pathway. Upon the oxidation of glycerol 3-phosphate, flavin adenine dinucleotide (FAD) reduces to FADH2, passing on electrons to Ubiquinone(UQ). UQ then reduces to UQH2 which allows for electrons to pass to nitrate or oxygen.
====Metabolism====
===Diseases===

[[Image:FINAL.png|thumb|Glycerol 3-Phosphate Dehydrogenase]]

<table style="background-color:#ffffc0" cellpadding="8" width="95%" border="0"><tr><td>Please do NOT make changes to this Sandbox until after April 23, 2010. Sandboxes 151-200 are reserved until then for use by the Chemistry 307 class at UNBC taught by Prof. [[User:Andrea Gorrell|Andrea Gorrell]].</td></tr>

Glycerol-3-Phosphate Dehydrogenase

2010-03-31T23:45:27Z

Indu Toora:

Glycerol-3-Phosphate Dehydrogenase

2010-03-31T23:35:15Z

Indu Toora:

Glycerol-3-Phosphate Dehydrogenase

2010-03-28T09:22:49Z

Indu Toora:

Glycerol-3-Phosphate Dehydrogenase

2010-03-28T09:21:53Z

Indu Toora: