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Search The CSA
PDB ID
UNIPROT ID
EC Number

Catalytic Site Atlas

CSA LITERATURE entry for 1pym

E.C. namephosphoenolpyruvate mutase
SpeciesMytilus edulis (Blue mussel)
E.C. Number (IntEnz) 5.4.2.9
CSA Homologues of 1pymThere are 10 Homologs
CSA Entries With UniProtID P56839
CSA Entries With EC Number 5.4.2.9
PDBe Entry 1pym
PDBSum Entry 1pym
MACiE Entry M0271

Literature Report

IntroductionPhosphoenolpyruvate (PEP) mutase catalyses the conversion of PEP to 3-phosphonopyruvate which is the P-C bond forming step of the biosynthetic pathways leading to phosphonate natural products. Phosphonates are secondary metabolites, some of which have antibiotic activity. The structure of the enzyme is that of a modified alpha-beta barrel with only 7 beta sheets in the core of the barrel.
MechansimUnknown mechanism.
Reaction

Catalytic Sites for 1pym

Annotated By Reference To The Literature - Site 1 (Perform Site Search)
ResidueChainNumberUniProtKB NumberFunctional PartFunctionTargetDescription
AspA5858macie:sideChain
LeuA4848macie:mainChainAmide
GlyA4747macie:mainChainAmide
LysA120120macie:sideChain

Annotated By Reference To The Literature - Site 2 (Perform Site Search)
ResidueChainNumberUniProtKB NumberFunctional PartFunctionTargetDescription
AspB5858macie:sideChain
LeuB4848macie:mainChainAmide
GlyB4747macie:mainChainAmide
LysB120120macie:sideChain

Literature References

Notes:
Huang K
Helix swapping between two alpha/beta barrels: crystal structure of phosphoenolpyruvate mutase with bound Mg(2+)-oxalate.
Structure 1999 7 539-548
PubMed: 10378273
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