5-guanidino-2-oxopentanoate decarboxylase
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
| 5-guanidino-2-oxopentanoate decarboxylase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 4.1.1.75 | ||||||||
| CAS number | 56831-67-5 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
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.
References
- 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 (14): 5322–9. PMID 237915.
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