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Search The CSA
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Catalytic Site Atlas

CSA LITERATURE entry for 1els

E.C. namephosphopyruvate hydratase
SpeciesSaccharomyces cerevisiae (Baker's yeast)
E.C. Number (IntEnz) 4.2.1.11
CSA Homologues of 1elsThere are 38 Homologs
CSA Entries With UniProtID P00924
CSA Entries With EC Number 4.2.1.11
PDBe Entry 1els
PDBSum Entry 1els
MACiE Entry M0311

Literature Report

IntroductionYeast enolase (2-phospho-D-glycerate hydrolase) is a metalloenzyme which catalyses the reversible dehydration of D-2-phos-phoglycerate (PGA) to phosphoenolpyruvate (PEP). The enzyme has an absolute requirement for the presence of a divalent cation, as is characteristic of the enolase family.
MechansimDehydration proceeds via an EC1B mechanism. Rate determining deprotonation of the substrate C-2 proton by the catalytic base leads to Sp2 hybridization of the C-2 atom, forming an enolate and then subsequent trans-elimination of the C-3 hydroxyl group is facilitated by the proton donor His 159 residue. The eliminated water molecule is incorporated into the coordination sphere of the catalytic divalent Mg ion.
Reaction

Catalytic Sites for 1els

Annotated By Reference To The Literature - Site 1 (Perform Site Search)
ResidueChainNumberUniProtKB NumberFunctional PartFunctionTargetDescription
HisA159160macie:sideChainThe residue acts as a general acid towards the departing hydroxyl group, facilitating its elimination. Electrostatic interactions with the catalytically essential divalent Mg ion tunes the pKa of the residue towards its function.
LysA396397macie:sideChainThe residue acts as a general base towards the C-2 atoms of the substrate, forming an enolate through a carbanion transition state.

Literature References

Notes:
Vinarov DA
pH dependence of the reaction catalyzed by yeast Mg-enolase.
Biochemistry 1998 37 15238-15246
PubMed: 9790688
Zhang E
Catalytic metal ion binding in enolase: the crystal structure of an enolase-Mn2+-phosphonoacetohydroxamate complex at 2.4-A resolution.
Biochemistry 1994 33 6295-6300
PubMed: 8193144
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