Biology:Guanidinobutyrase
| guanidinobutyrase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 3.5.3.7 | ||||||||
| CAS number | 9013-69-8 | ||||||||
| 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 | ||||||||
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In enzymology, a guanidinobutyrase (EC 3.5.3.7) is an enzyme that catalyzes the chemical reaction
- 4-guanidinobutanoate + H2O [math]\displaystyle{ \rightleftharpoons }[/math] 4-aminobutanoate + urea
Thus, the two substrates of this enzyme are 4-guanidinobutanoate and H2O, whereas its two products are 4-aminobutanoate 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 4-guanidinobutanoate amidinohydrolase. Other names in common use include gamma-guanidobutyrase, 4-guanidinobutyrate amidinobutyrase, gamma-guanidinobutyrate amidinohydrolase, G-Base, GBH, and guanidinobutyrate ureahydrolase. This enzyme participates in urea cycle and metabolism of amino groups. It employs one cofactor, manganese.
References
- "Characteristics of arginases from ureotelic and non-ureotelic animals". Biochem. J. 96 (3): 588–94. 1965. doi:10.1042/bj0960588. PMID 5862400.
- "[Induction and specificity of enzymes of the new catabolic arginine pathway]". Biochim. Biophys. Acta 115 (1): 73–80. 1966. doi:10.1016/0304-4165(66)90050-x. PMID 5936244.
- "4-Guanidinobutyrate amidinohydrolase from Pseudomonas sp ATCC 14676: purification to homogeneity and properties". Agric. Biol. Chem. 44 (5): 1127–1134. 1980. doi:10.1271/bbb1961.44.1127.
- K; Kobayashi, Toru; Tabuchi, Akira; Shiritani, Yoshinori; Yonaha, Kazuo (1983). "Distribution of amidinohydrolases among Pseudomonas and comparative studies of some purified enzymes by one-dimensional peptide mapping". Agric. Biol. Chem. 47 (12): 2825–2830. doi:10.1271/bbb1961.47.2825.
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