Guanidinoacetase
From Wikipedia, the free encyclopedia
In enzymology, a guanidinoacetase (EC 3.5.3.2) is an enzyme that catalyzes the chemical reaction
- guanidinoacetate + H2O glycine + urea
Thus, the two substrates of this enzyme are guanidinoacetate and H2O, whereas its two products are glycine and urea.
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amidines. The systematic name of this enzyme class is guanidinoacetate amidinohydrolase. This enzyme is also called glycocyaminase. It employs one cofactor, manganese.
[edit] References
- IUBMB entry for 3.5.3.2
- BRENDA references for 3.5.3.2 (Recommended.)
- PubMed references for 3.5.3.2
- PubMed Central references for 3.5.3.2
- Google Scholar references for 3.5.3.2
- ROCHE J, LACOMBE G, GIRARD H (1950). "[On the specificity of certain bacterial deguanidases generating urea and on arginindihydrolase.]". Biochim. Biophys. Acta. 6: 210–6. PMID 14791411.
- Yorifuji T, Tamai H and Usami H (1977). "Purification, crystallization and properties of Mn2+ dependent guanidoacetate amidinohydrolase from a Pseudomonas". Agric. Biol. Chem. 41: 959–966.
[edit] External links
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- The CAS registry number for this enzyme class is 9024-92-4.