Sandbox Reserved 1094: Difference between revisions

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<font color='grey'>External resource</font> : click on [https://www.rcsb.org/pdb/explore/remediatedSequence.do?structureId=1DPG] to see the graphical representation on the RCSB website.

[[Image:Pathology of G6PD deficiency.png|150x150px|upright|thumb| G6PD pathway. Obtained from [https://en.wikipedia.org/wiki/Glucose-6-phosphate_dehydrogenase Wikipedia]]]

== Catalytic activity ==

~~== Catalytic activity ==~~

<font color='red'>'''D-glucose 6-phosphate + NAD+ → 6-phospho-D-glucono-1,5-lactone + H+ + NADH'''<ref>PMID: 9485426</ref></font>

~~[[Image:Pathology of G6PD deficiency.png]]~~

KM=114 µM for '''G6PD''' (with NADP), KM=69 µM for '''G6PD''' (with NAD),

KM=8.0 µM for [[NADP]], KM=160 µM for [[NAD]].

KM=8.0 µM for [https://en.wikipedia.org/wiki/Nicotinamide_adenine_dinucleotide_phosphate NADP], KM=160 µM for [[NAD]].

Its regulation depends on the concentration of substrate and coenzyme, rate limiting step in pentose phosphate pathway<ref>PMID: 12033926</ref>.

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== Evolutionary conservation ==

[[Image:Consurf_key_small.gif|200px|right]]

The different structures conserved evolutionary can be observed according to the scale following.

~~[[Image:Consurf_key_small.gif|200px|right]]~~

Check<jmol>

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This sequence being the normal protein sequence found in L. ''mesenteroides''.

== Structural highlights ==

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The dimer is very extend compared to the monomer with a size of 112Å.

The enzyme is found into a dimeric form in vivo. The two subunits interface is made by the contact between the two antiparallels β-sheets of the carboxyl terminus domain. Their interaction is crucial and form a β-half-barrel ([https://en.wikipedia.org/wiki/Beta_barrel β-Barrel ]) on one side of the protein which is closed on the other side by helices of each monomer. The majority of dimer contacts are hydrophobic with hydrophobic residues in the inside of the β-half-barrel but there are three salt bridges, especially a conserved one between Glu183 and Lys386 ; Lys 32 with Asp 390 and Arg395 with Asp 407, and two main chain hydrogen bonds which participates to the cohesion of the structure. Glu183 is the last residue of the nine-residue conserved peptide.<ref name="struc"/>

The enzyme is found into a dimeric form in vivo. The two subunits interface is made by the contact between the two antiparallels β-sheets of the carboxyl terminus domain. Their interaction is crucial and form a <scene name='82/829347/Betahalfbarrel/1'>β-half-barrel</scene> ([https://en.wikipedia.org/wiki/Beta_barrel β-Barrel ]) on one side of the protein which is closed on the other side by helices of each monomer. The majority of dimer contacts are hydrophobic with hydrophobic residues in the inside of the β-half-barrel but there are <scene name='82/829347/Saltbridges/1'>three salt bridges</scene>, especially a conserved one between Glu183 and Lys386 ; Lys 32 with Asp 390 and Arg395 with Asp 407, and two main chain hydrogen bonds which participates to the cohesion of the structure. Glu183 is the last residue of the nine-residue conserved peptide.<ref name="struc"/>

The active site of the enzyme is contained in each monomer but the dimeric form is necessary to the biological activity indeed it confers the stability in aqueous medium.

Sandbox Reserved 1094: Difference between revisions

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@@ Line 19: / Line 19: @@
 <font color='grey'>External resource</font> : click on [https://www.rcsb.org/pdb/explore/remediatedSequence.do?structureId=1DPG] to see the graphical representation on the RCSB website.
+[[Image:Pathology of G6PD deficiency.png|150x150px|upright|thumb| G6PD pathway. Obtained from [https://en.wikipedia.org/wiki/Glucose-6-phosphate_dehydrogenase Wikipedia]]]
+== Catalytic activity ==
-== Catalytic activity ==
 <font color='red'>'''D-glucose 6-phosphate + NAD+ → 6-phospho-D-glucono-1,5-lactone + H+ + NADH'''<ref>PMID: 9485426</ref></font>
-[[Image:Pathology of G6PD deficiency.png]]
 KM=114 µM for '''G6PD''' (with NADP), KM=69 µM for '''G6PD''' (with NAD),
-KM=8.0 µM for [[NADP]], KM=160 µM for [[NAD]].
+KM=8.0 µM for [https://en.wikipedia.org/wiki/Nicotinamide_adenine_dinucleotide_phosphate NADP], KM=160 µM for [[NAD]].
 Its regulation depends on the concentration of substrate and coenzyme, rate limiting step in pentose phosphate pathway<ref>PMID: 12033926</ref>.
@@ Line 35: / Line 34: @@
 == Evolutionary conservation ==
+[[Image:Consurf_key_small.gif|200px|right]]
 The different structures conserved evolutionary can be observed according to the scale following.
-[[Image:Consurf_key_small.gif|200px|right]]
 Check<jmol>
    <jmolCheckbox>
@@ Line 55: / Line 55: @@
 This sequence being the normal protein sequence found in L. ''mesenteroides''.
-<Structure load='1dpg' size='450' frame='true' align='right' caption='Insert caption here' scene='' />
+<Structure load='1dpg' size='450' frame='true' align='right' caption='3D structure of G6PD' scene='' />
 == Structural highlights ==
@@ Line 94: / Line 94: @@
 The dimer is very extend compared to the monomer with a size of 112Å.
-The enzyme is found into a dimeric form in vivo. The two subunits interface is made by the contact between the two antiparallels β-sheets of the carboxyl terminus domain. Their interaction is crucial and form a β-half-barrel ([https://en.wikipedia.org/wiki/Beta_barrel β-Barrel ]) on one side of the protein which is closed on the other side by helices of each monomer. The majority of dimer contacts are hydrophobic with hydrophobic residues in the inside of the β-half-barrel but there are three salt bridges, especially a conserved one between Glu183 and Lys386 ; Lys 32 with Asp 390 and Arg395 with Asp 407, and two main chain hydrogen bonds which participates to the cohesion of the structure. Glu183 is the last residue of the nine-residue conserved peptide.<ref name="struc"/>
+The enzyme is found into a dimeric form in vivo. The two subunits interface is made by the contact between the two antiparallels β-sheets of the carboxyl terminus domain. Their interaction is crucial and form a <scene name='82/829347/Betahalfbarrel/1'>β-half-barrel</scene> ([https://en.wikipedia.org/wiki/Beta_barrel β-Barrel ]) on one side of the protein which is closed on the other side by helices of each monomer. The majority of dimer contacts are hydrophobic with hydrophobic residues in the inside of the β-half-barrel but there are <scene name='82/829347/Saltbridges/1'>three salt bridges</scene>, especially a conserved one between Glu183 and Lys386 ; Lys 32 with Asp 390 and Arg395 with Asp 407, and two main chain hydrogen bonds which participates to the cohesion of the structure. Glu183 is the last residue of the nine-residue conserved peptide.<ref name="struc"/>
 The active site of the enzyme is contained in each monomer but the dimeric form is necessary to the biological activity indeed it confers the stability in aqueous medium.