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EC Number

Catalytic Site Atlas

CSA LITERATURE entry for 1aq2

E.C. namephosphoenolpyruvate carboxykinase (ATP)
SpeciesEscherichia coli (Bacteria)
E.C. Number (IntEnz)
CSA Homologues of 1aq2There are 43 Homologs
CSA Entries With UniProtID P22259
CSA Entries With EC Number
PDBe Entry 1aq2
PDBSum Entry 1aq2
MACiE Entry M0051

Literature Report

IntroductionPhosphoenolpyruvate carboxykinase catalyses the decarboxylation and phosphorylation of oxaloacetate to form phosphoenolpyruvate. This conversion is the first committed step of gluconeogenesis in E. coli and is part of the gluconeogenic pathway in virtually all organisms.
MechansimThe substrate undergoes decarboxylation, resulting in the formation of an enol intermediate, stabilised by positively charged residues. The oxyanion formed attacks the gamma phosphate of ATP in a nucleophilic substitution, giving the products of ADP and phosphoenolpyruvate.

Catalytic Sites for 1aq2

Annotated By Reference To The Literature - Site 1 (Perform Site Search)
ResidueChainNumberUniProtKB NumberFunctional PartFunctionTargetDescription
HisA232232macie:sideChainStabilises intermediates.
LysA254254macie:sideChainNeutralises repulsions between phosphate oxygen atoms on ATP, promoting the formation of a high energy conformer.
ArgA333333macie:sideChainActivates substrate, stabilises enolate intermediate.

Literature References

Matte A
Structure and mechanism of phosphoenolpyruvate carboxykinase.
J Biol Chem 1997 272 8105-8108
PubMed: 9139042
Tari LW
Mg(2+)-Mn2+ clusters in enzyme-catalyzed phosphoryl-transfer reactions.
Nat Struct Biol 1997 4 990-994
PubMed: 9406547
Tari LW
Snapshot of an enzyme reaction intermediate in the structure of the ATP-Mg2+-oxalate ternary complex of Escherichia coli PEP carboxykinase.
Nat Struct Biol 1996 3 355-363
PubMed: 8599762
Bazaes S.
Identification of reactive conserved histidines in phosphoenolpyruvate carboxykinases from Escherichia coli and Saccharomyces cerevisiae
Biochim Biophys Acta. 1997 1337 166-174
PubMed: 9048893