5-guanidino-2-oxopentanoate decarboxylase
From Wikipedia, the free encyclopedia
In enzymology, a 5-guanidino-2-oxopentanoate decarboxylase (EC 4.1.1.75) is an enzyme that catalyzes the chemical reaction
- 5-guanidino-2-oxo-pentanoate 4-guanidinobutanal + CO2
Hence, this enzyme has one substrate, 5-guanidino-2-oxo-pentanoate, and two products, 4-guanidinobutanal and CO2.
This enzyme belongs to the family of lyases, specifically the carboxy-lyases, which cleave carbon-carbon bonds. The systematic name of this enzyme class is 5-guanidino-2-oxo-pentanoate carboxy-lyase (4-guanidinobutanal-forming). Other names in common use include alpha-ketoarginine decarboxylase, and 2-oxo-5-guanidinopentanoate carboxy-lyase. It has 2 cofactors: thiamin diphosphate, and Divalent cation.
[edit] References
- IUBMB entry for 4.1.1.75
- BRENDA references for 4.1.1.75 (Recommended.)
- PubMed references for 4.1.1.75
- PubMed Central references for 4.1.1.75
- Google Scholar references for 4.1.1.75
- Vanderbilt AS, Gaby NS, Rodwell VW (1975). "Intermediates and enzymes between alpha-ketoarginine and gamma-guanidinobutyrate in the L-arginine catabolic pathway of Pseudomonas putida". J. Biol. Chem. 250: 5322–9. PMID 237915.
[edit] External links
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- The CAS registry number for this enzyme class is 56831-67-5.