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Literature summary for 3.1.4.3 extracted from

  • Liao, R.Z.; Yu, J.G.; Himo, F.
    Reaction mechanism of the trinuclear zinc enzyme phospholipase C: a density functional theory study (2010), J. Phys. Chem. B, 114, 2533-2540.
    View publication on PubMed
Search for more literature for 3.1.4.3

Localization

Localization Comment Organism GeneOntology No. Textmining
extracellular
-
 Bacillus cereus
-
-

Metals/Ions

Metals/Ions Comment Organism Structure
Zn2+ phospholipase C is a trinuclear zinc enzyme, structure analysis, using also the crystal structure from PDB entry 1AH7, overview Bacillus cereus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Bacillus cereus PLCBC also catalyzes the hydrolysis of phosphatidylethanolamine and phosphatidylserine but with lower efficiency ?
-
 ?
phosphatidylcholine + H2O Bacillus cereus
-
 1,2-diacyl-sn-glycerol + choline phosphate
-
 ?

Organism

Organism UniProt Comment Textmining
Bacillus cereus
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information PLCBC also catalyzes the hydrolysis of phosphatidylethanolamine and phosphatidylserine but with lower efficiency Bacillus cereus ?
-
 ?
additional information modeling of active site and reaction mechanism, development of two different reaction mechanism models, overview Bacillus cereus ?
-
 ?
phosphatidylcholine + H2O
-
 Bacillus cereus 1,2-diacyl-sn-glycerol + choline phosphate
-
 ?

Subunits

Subunits Comment Organism
monomer (alpha/beta)8 TIM barrel fold Bacillus cereus

Synonyms

Synonyms Comment Organism
phosphatidylcholine-preferring PLC
-
 Bacillus cereus
PLCBC
-
 Bacillus cereus