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BRENDA support

Literature summary for 3.1.4.11 extracted from

  • Yang, B.; Pu, M.; Khan, H.; Friedman, L.; Reuter, N.; Roberts, M.; Gershenson, A.
    Quantifying transient interactions between Bacillus phosphatidylinositol-specific phospholipase-C and phosphatidylcholine-rich vesicles (2015), J. Am. Chem. Soc., 137, 14-17 .
    View publication on PubMedView publication on EuropePMC

Localization

Localization Comment Organism GeneOntology No. Textmining

Organism

Organism UniProt Comment Textmining
Bacillus thuringiensis
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1-phosphatidyl-1D-myo-inositol + H2O
-
Bacillus thuringiensis 1D-myo-inositol 1-phosphate + diacylglycerol
-
?

Synonyms

Synonyms Comment Organism
phosphatidylinositol-specific phospholipase-C
-
Bacillus thuringiensis
PI-PLC
-
Bacillus thuringiensis

General Information

General Information Comment Organism
metabolism the enzyme specifically binds to phosphatidylcholine and cleaves glycosylphosphatidylinositol-anchored proteins of eukaryotic plasma membranes Bacillus thuringiensis