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Literature summary 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

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.1.4.3 extracellular
-
Bacillus cereus
-
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.1.4.3 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)

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

Organism

EC Number Organism UniProt Comment Textmining
3.1.4.3 Bacillus cereus
-
-
-

Substrates and Products (Substrate)

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

Subunits

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

Synonyms

EC Number Synonyms Comment Organism
3.1.4.3 phosphatidylcholine-preferring PLC
-
Bacillus cereus
3.1.4.3 PLCBC
-
Bacillus cereus