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Search The CSA
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Catalytic Site Atlas

CSA LITERATURE entry for 1ah7

E.C. namephospholipase C
SpeciesBacillus cereus (Bacteria)
E.C. Number (IntEnz) 3.1.4.3
CSA Homologues of 1ah7There are 16 Homologs
CSA Entries With UniProtID P09598
CSA Entries With EC Number 3.1.4.3
PDBe Entry 1ah7
PDBSum Entry 1ah7
MACiE Entry M0027

Literature Report

IntroductionPhospholipase C, PLC, from Bacillus cereus is a monomeric protein similar to mammalian PLCs and can mimic the action of mammalian PLCs eg. by stimulating prostaglandin synthesis. There are three Zn2+ ions in the active site. The enzyme cleaves membrane phospholipids liberating the polar head group and leaving diacylglycerol. Although phosphatidylcholine is the preferred substrate, phosphatidylserine and phosphatidylethanolamine are also accepted.
MechansimThe general base residue deprotonates water, which initiates a nucleophilic attack on the phosphorus atom of the phosphodiester linkage. This results in two products, phosphorylcholine and diacylglycerol. Diacylglycerol should be activated by a general acid, which could be one of the Zn2+ ions or could be another amino acid, but the identity of this is unknown.
Reaction

Catalytic Sites for 1ah7

Annotated By Reference To The Literature - Site 1 (Perform Site Search)
ResidueChainNumberUniProtKB NumberFunctional PartFunctionTargetDescription
AspA5593macie:sideChainGeneral base.

Literature References

Notes:
Martin SF
Catalytic cycle of the phosphatidylcholine-preferring phospholipase C from Bacillus cereus. Solvent viscosity, deuterium isotope effects, and proton inventory studies.
Biochemistry 1999 38 4403-4408
PubMed: 10194360
Martin SF
Expression and site-directed mutagenesis of the phosphatidylcholine-preferring phospholipase C of Bacillus cereus: probing the role of the active site Glu146.
Biochemistry 1996 35 12970-12977
PubMed: 8841144
Martin SF
General base catalysis by the phosphatidylcholine-preferring phospholipase C from Bacillus cereus: the role of Glu4 and Asp55.
Biochemistry 1998 37 5755-5760
PubMed: 9548962
Hough E
High-resolution (1.5 A) crystal structure of phospholipase C from Bacillus cereus.
Nature 1989 338 357-360
PubMed: 2493587
Hansen S
Crystal structure of phospholipase C from Bacillus cereus complexed with a substrate analog.
J Mol Biol 1993 234 179-187
PubMed: 8230197
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