| guanidinoacetase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.5.3.2 | ||||||||
| CAS no. | 9024-92-4 | ||||||||
| 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 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.
References
- ROCHE J, LACOMBE G, GIRARD H (1950). "[On the specificity of certain bacterial deguanidases generating urea and on arginindihydrolase.]". Biochim. Biophys. Acta. 6 (1): 210–6. doi: 10.1016/0006-3002(50)90093-x. PMID 14791411.
- Yorifuji T, Tamai H, Usami H (1977). "Purification, crystallization and properties of Mn2+ dependent guanidoacetate amidinohydrolase from a Pseudomonas". Agric. Biol. Chem. 41 (6): 959–966. doi: 10.1271/bbb1961.41.959.
| guanidinoacetase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.5.3.2 | ||||||||
| CAS no. | 9024-92-4 | ||||||||
| 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 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.
References
- ROCHE J, LACOMBE G, GIRARD H (1950). "[On the specificity of certain bacterial deguanidases generating urea and on arginindihydrolase.]". Biochim. Biophys. Acta. 6 (1): 210–6. doi: 10.1016/0006-3002(50)90093-x. PMID 14791411.
- Yorifuji T, Tamai H, Usami H (1977). "Purification, crystallization and properties of Mn2+ dependent guanidoacetate amidinohydrolase from a Pseudomonas". Agric. Biol. Chem. 41 (6): 959–966. doi: 10.1271/bbb1961.41.959.