Guanidinopropionase
From Wikipedia the free encyclopedia
| guanidinopropionase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.5.3.17 | ||||||||
| CAS no. | 68821-77-2 | ||||||||
| 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 | ||||||||
| |||||||||
In enzymology, a guanidinopropionase (EC 3.5.3.17) is an enzyme that catalyzes the chemical reaction
- 3-guanidinopropanoate + H2O beta-alanine + urea
Thus, the two substrates of this enzyme are 3-guanidinopropanoate and H2O, whereas its two products are beta-alanine 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 3-guanidinopropanoate amidinopropionase. Other names in common use include GPase and GPH. It employs one cofactor, manganese.
References[edit]
- Yorifuji T, Sugai I, Matsumoto H, Tabuchi A (1982). "Characterization of 3-guanidinopropionate amidinohydrolase from Pseudomonas aeruginosa and a comparative study with 4- guanidinobutyrate amidinohydrolase from another Pseudomonas". Agric. Biol. Chem. 46 (5): 1361–1363. doi:10.1271/bbb1961.46.1361.
