Sandbox Reserved 477: Difference between revisions

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Glyceraldehyde-3-Phosphate dehydrogenase is included in a class of proteins known as oxidoreductases. Enzymes classified as oxidoreductases are involved in redox reactions, catalyzing the transfer of electrons from one molecule to another. Glyceraldehyde, commonly abbreviated as GAPDH, is approximately 37 kDa depending on the organism that particular enzyme was isolated from and is responsible for catalyzing the sixth step of a process called glycolysis, which serves to break down glucose for energy and carbon molecules for aerobic organisms. GAPDHs are cytoplasmic glycolytic enzymes, which although lacking identifiable secretion signals, have also been localized to the surface of several bacteria (and some eukaryotic organisms); where in some cases they have been shown to contribute to the colonization and invasion of host tissues. GAPDHs are designated as class I and II GAPDHs. Class I GAPDH is the classic enzyme of glycolysis and the Calvin Cycle in eubacteria and eukaryotes, while class II GAPDH has so far only been found in archaebacteria. In addition to the metabolic function, GAPDH has recently been implicated in several nonmetabolic processes, including transcription activation, initiation of programmed cell death, and ER to Golgi vesicle shuttling. GAPDH is considered a housekeeping gene due to its stability and expression at high levels in most tissues and cells. Housekeeping genes are genes that are required for the maintenance of basic cellular function, and are expressed in all cells of an organism. For this reason, GAPDH is commonly used by researchers as a loading control for the Western Blot and as a control for Real Time PCR.

Glyceraldehyde-3-Phosphate dehydrogenase is included in a class of proteins known as oxidoreductases. Enzymes classified as oxidoreductases are involved in redox reactions, catalyzing the transfer of electrons from one molecule to another. "Glyceraldehyde, commonly abbreviated as GAPDH, is approximately 37 kDa depending on the organism that particular enzyme was isolated from and is responsible for catalyzing the sixth step of a process called glycolysis, which serves to break down glucose for energy and carbon molecules for aerobic organisms. GAPDHs are cytoplasmic glycolytic enzymes, which although lacking identifiable secretion signals, have also been localized to the surface of several bacteria (and some eukaryotic organisms); where in some cases they have been shown to contribute to the colonization and invasion of host tissues." <ref>This is my reference</ref> GAPDHs are designated as class I and II GAPDHs. Class I GAPDH is the classic enzyme of glycolysis and the Calvin Cycle in eubacteria and eukaryotes, while class II GAPDH has so far only been found in archaebacteria. In addition to the metabolic function, GAPDH has recently been implicated in several nonmetabolic processes, including transcription activation, initiation of programmed cell death, and ER to Golgi vesicle shuttling. GAPDH is considered a housekeeping gene due to its stability and expression at high levels in most tissues and cells. Housekeeping genes are genes that are required for the maintenance of basic cellular function, and are expressed in all cells of an organism. For this reason, GAPDH is commonly used by researchers as a loading control for the Western Blot and as a control for Real Time PCR.

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# Reagents reacting with or oxidizing the catalytic site sulfhydryl group inhibit the enzyme. Heavy metal ions, pCMB, iodoacetate, o-iodosobenzoate, and tetrathionate are among known inhibitors. ATP, cyclic AMP, and other adenine-containing compounds have been indicated as resulting in reversible dissociation, competitive inhibition, and increased susceptibility to proteolysis.

# The antibiotic, Pentalenolactone (PL), is a specific irreversible inhibitor of glyceraldehyde-3-phosphate dehydrogenase. The effect of this antibiotic was studied in Trypanosoma brucei. In infected mice, due to the rapid metabolic inactivation of PL in vivo, trypanosomes were not affected by concentrations that were lethal to the host. Bloodstream trypanosomes in vitro were killed by low concentrations of PL, suggesting that there is no alternative to the glycolytic pathway for the generation of ATP in the bloodstream forms.

== '''References''' ==

Sandbox Reserved 477: Difference between revisions

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-Glyceraldehyde-3-Phosphate dehydrogenase is included in a class of proteins known as oxidoreductases. Enzymes classified as oxidoreductases are involved in redox reactions, catalyzing the transfer of electrons from one molecule to another. Glyceraldehyde, commonly abbreviated as GAPDH, is approximately 37 kDa depending on the organism that particular enzyme was isolated from and is responsible for catalyzing the sixth step of a process called glycolysis, which serves to break down glucose for energy and carbon molecules for aerobic organisms. GAPDHs are cytoplasmic glycolytic enzymes, which although lacking identifiable secretion signals, have also been localized to the surface of several bacteria (and some eukaryotic organisms); where in some cases they have been shown to contribute to the colonization and invasion of host tissues. GAPDHs are designated as class I and II GAPDHs. Class I GAPDH is the classic enzyme of glycolysis and the Calvin Cycle in eubacteria and eukaryotes, while class II GAPDH has so far only been found in archaebacteria. In addition to the metabolic function, GAPDH has recently been implicated in several nonmetabolic processes, including transcription activation, initiation of programmed cell death, and ER to Golgi vesicle shuttling. GAPDH is considered a housekeeping gene due to its stability and expression at high levels in most tissues and cells. Housekeeping genes are genes that are required for the maintenance of basic cellular function, and are expressed in all cells of an organism. For this reason, GAPDH is commonly used by researchers as a loading control for the Western Blot and as a control for Real Time PCR.
+Glyceraldehyde-3-Phosphate dehydrogenase is included in a class of proteins known as oxidoreductases. Enzymes classified as oxidoreductases are involved in redox reactions, catalyzing the transfer of electrons from one molecule to another. "Glyceraldehyde, commonly abbreviated as GAPDH, is approximately 37 kDa depending on the organism that particular enzyme was isolated from and is responsible for catalyzing the sixth step of a process called glycolysis, which serves to break down glucose for energy and carbon molecules for aerobic organisms. GAPDHs are cytoplasmic glycolytic enzymes, which although lacking identifiable secretion signals, have also been localized to the surface of several bacteria (and some eukaryotic organisms); where in some cases they have been shown to contribute to the colonization and invasion of host tissues." <ref>This is my reference</ref> GAPDHs are designated as class I and II GAPDHs. Class I GAPDH is the classic enzyme of glycolysis and the Calvin Cycle in eubacteria and eukaryotes, while class II GAPDH has so far only been found in archaebacteria. In addition to the metabolic function, GAPDH has recently been implicated in several nonmetabolic processes, including transcription activation, initiation of programmed cell death, and ER to Golgi vesicle shuttling. GAPDH is considered a housekeeping gene due to its stability and expression at high levels in most tissues and cells. Housekeeping genes are genes that are required for the maintenance of basic cellular function, and are expressed in all cells of an organism. For this reason, GAPDH is commonly used by researchers as a loading control for the Western Blot and as a control for Real Time PCR.
 <Structure load='1VC2' size='500' frame='true' align='right' caption='This is Glyceraldehyde-3-Phosphate Dehydrogenase isolated from Thermus thermophilus HB8' scene='Insert optional scene name here' />
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 # Reagents reacting with or oxidizing the catalytic site sulfhydryl group inhibit the enzyme. Heavy metal ions, pCMB, iodoacetate, o-iodosobenzoate, and tetrathionate are among known inhibitors. ATP, cyclic AMP, and other adenine-containing compounds have been indicated as resulting in reversible dissociation, competitive inhibition, and increased susceptibility to proteolysis.
 # The antibiotic, Pentalenolactone (PL), is a specific irreversible inhibitor of glyceraldehyde-3-phosphate dehydrogenase. The effect of this antibiotic was studied in Trypanosoma brucei. In infected mice, due to the rapid metabolic inactivation of PL in vivo, trypanosomes were not affected by concentrations that were lethal to the host. Bloodstream trypanosomes in vitro were killed by low concentrations of PL, suggesting that there is no alternative to the glycolytic pathway for the generation of ATP in the bloodstream forms.
+== '''References''' ==
+<references/>