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Search The CSA
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Catalytic Site Atlas

CSA LITERATURE entry for 1psd

E.C. namephosphoglycerate dehydrogenase
SpeciesEscherichia coli k12 ()
E.C. Number (IntEnz) 1.1.1.95
CSA Homologues of 1psdThere are 45 Homologs
CSA Entries With UniProtID P0A9T0
CSA Entries With EC Number 1.1.1.95
PDBe Entry 1psd
PDBSum Entry 1psd
MACiE Entry 1psd

Literature Report

Introduction3-phosphoglycerate dehydrogenase catalyses the oxidation of D-3-phosphoglycerate to 3-phosphohydroxypyruvate with concurrent reduction of NAD+ to NADH. This reaction is the first committed step in serine biosynthesis. In the following steps transamination of 3-phosphohydroxypyruvate with glutamate yields phosphoserine and the action of a phosphatase completes the biosynthesis. In prokaryotes and plants 3-phosphoglycerate dehydrogenase is inhibited by serine in an allosteric fashion.
Mechansim3-phosphoglycerate utilises a charge-relay system involving His 292 and Glu 269. His 292 deprotonates the C2 hydroxyl group of 3-phosphoglycerate as a hydride ion is transferred from C2 to NAD+. Glu 269 functions to modify the pKa of His 292, allowing it to carry out its catalytic role.
Reaction

Catalytic Sites for 1psd

Annotated By Reference To The Literature - Site 1 (Perform Site Search)
ResidueChainNumberUniProtKB NumberFunctional PartFunctionTargetDescription
GluA269269macie:sideChainModifies the pKa of His 292, allowing it to carry out its role in catalysis.
HisA292292macie:sideChainDeprotonates the C2 hydroxyl group as hydride is transferred from C2 to NAD.

Annotated By Reference To The Literature - Site 2 (Perform Site Search)
ResidueChainNumberUniProtKB NumberFunctional PartFunctionTargetDescription
GluB269269macie:sideChainModifies the pKa of His 292, allowing it to carry out its role in catalysis.
HisB292292macie:sideChainDeprotonates the C2 hydroxyl group as hydride is transferred from C2 to NAD.

Literature References

Notes:
Schuller DJ
The allosteric ligand site in the Vmax-type cooperative enzyme phosphoglycerate dehydrogenase.
Nat Struct Biol 1995 2 69-76
PubMed: 7719856
Stefan Funfrocken
Mobile Agents as an Architectural Concept for Internet-based Distributed Applications - The WASP Project Approach
J Biol Chem 1977 252 1539-1551
PubMed: 14154
Birktoft JJ
The presence of a histidine-aspartic acid pair in the active site of 2-hydroxyacid dehydrogenases. X-ray refinement of cytoplasmic malate dehydrogenase.
J Biol Chem 1983 258 472-482
PubMed: 6848515
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