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Overview for MACiE Entry M0027

Version history

General Information

EC Number: 3.1.4.3 (A member of the Hydrolases, Acting on ester bonds, Phosphoric-diester hydrolases)

Enzyme Name: phospholipase C

Biological Species: Bacillus cereus (Bacteria)

Catalytic Chain UniprotKB Accession Codes:

Representative PDB Code: 1ah7 - PHOSPHOLIPASE C FROM BACILLUS CEREUS (Resolution = 1.50 Å).

Catalytic CATH Codes:

Display structure information

Overall Reaction:

Image of phosphatidylcholine

Image of water

right arrow

Image of 1,2-diacylglycerol

Image of choline phosphate

phosphatidylcholine
C00157
CHEBI:16110
water
C00001
CHEBI:15377
1,2-diacylglycerol
C00641
CHEBI:17815
choline phosphate
C00588
CHEBI:18132

This reaction is irreversible.


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Stepwise Description of the Reaction

Step 1Asp55 deprotonates water, which initiates nucleophilic attack on the phosphate in a substitution reaction, eliminating 1,2-diacylglycerol.
Step 2the phosphate of choline phosphate deprotonates Asp55 in an inferred return step.

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Catalytic Residues Involved

Type Number Chain Location of Function
Asp 55 A Side Chain

Metal Cofactors for M0027

Type Het group Number Chain
zinc ZN 246 x Overview
zinc ZN 247 x Overview
zinc ZN 248 x Overview

References

  1. S. F. Martin et al. (1999), Biochemistry, 38, 4403-4408. Catalytic cycle of the phosphatidylcholine-preferring phospholipase C from Bacillus cereus. Solvent viscosity, deuterium isotope effects, and proton inventory studies.
    Medline: 10194360

Homologue information for M0027 (1ah7)

CSA Homologues

MACiE Homologues (within the PDB)

MACiE Homologues (within UniprotKB/SwissProt)


Links to this entry in other databases

Link to EC-PDB-SUM Link to PDB-SUM Link to RCSB PDB Link to PDBe Link to CSA
Link to MetaCyc Link to KEGG Link to BRENDA Link to ExplorENZ

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phospholipase C activity (molecular function)
zinc ion binding (molecular function)
hydrolase activity (molecular function)
hydrolase activity, acting on ester bonds (molecular function)
cytolysis (biological process)
phosphatidylcholine phospholipase C activity (molecular function)
hemolysis in other organism (biological process)
metal ion binding (molecular function)
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