Lecithinase C

Phospholipase C (EC 3.1.4.3, lipophosphodiesterase I, Clostridium welchii alpha-toxin, Clostridium oedematiens beta- and gamma-toxins, lipophosphodiesterase C, phosphatidase C, heat-labile hemolysin, alpha-toxin) is an enzyme with systematic name phosphatidylcholine cholinephosphohydrolase.^[1]^[2]^[3]^[4] This enzyme catalyses the following chemical reaction

a phosphatidylcholine + H₂O

\rightleftharpoons

1,2-diacyl-sn-glycerol + phosphocholine

The bacterial enzyme is a zinc protein. It also acts on sphingomyelin and phosphatidylinositol.

References

↑ Druzhinina, K.V. and Kritzman, M.G. (1952). "[Lecithinase from animal tissues.]". Biokhimiya 17: 77–81. PMID 13066482.
↑ Little, C. and Otnass, A.-B. (1975). "The metal ion dependence of phospholipase C from Bacillus cereus". Biochim. Biophys. Acta 391: 326–333. doi:10.1016/0005-2744(75)90256-9. PMID 807246.
↑ Sheiknejad, R.G. and Srivastava, P.N. (1986). "Isolation and properties of a phosphatidylcholine-specific phospholipase C from bull seminal plasma". J. Biol. Chem. 261: 7544–7549. PMID 3086312.
↑ Takahashi, T., Sugahara, T. and Ohsaka, A. (1974). "Purification of Clostridium perfringens phospholipase C (α-toxin) by affinity chromatography on agarose-linked egg-yolk lipoprotein". Biochim. Biophys. Acta 351: 155–171. doi:10.1016/0005-2795(74)90074-9. PMID 4365891.

External links

Phospholipase C at the US National Library of Medicine Medical Subject Headings (MeSH)

Hydrolase: esterases (EC 3.1)

3.1.1: Carboxylic
ester hydrolases

Lipase

Phospholipase
- A1
- A2
- B

3.1.2: Thioesterase

3.1.3: Phosphatase

3.1.4: Phosphodiesterase

3.1.6: Sulfatase

Nuclease (includes
deoxyribonuclease and
ribonuclease)

3.1.11-16: Exonuclease

Exodeoxyribonuclease	RecBCD

Exoribonuclease	Oligonucleotidase

3.1.21-31: Endonuclease

Endodeoxyribonuclease	Deoxyribonuclease I Deoxyribonuclease II Deoxyribonuclease IV Restriction enzyme UvrABC endonuclease

Endoribonuclease	RNase III RNase H 1 2A 2B 2C RNase P RNase A 1 2 3 4/5 RNase T1 RNA-induced silencing complex

either deoxy- or ribo-	Aspergillus nuclease S1 Micrococcal nuclease

Enzymes

Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Catalytically perfect enzyme Coenzyme Cofactor Enzyme catalysis Enzyme kinetics Lineweaver–Burk plot Michaelis–Menten kinetics

Regulation	Allosteric regulation Cooperativity Enzyme inhibitor

Classification	EC number Enzyme superfamily Enzyme family List of enzymes

Types	EC1 Oxidoreductases(list) EC2 Transferases(list) EC3 Hydrolases(list) EC4 Lyases(list) EC5 Isomerases(list) EC6 Ligases(list)

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