Biology:Amidinoaspartase
From HandWiki
| amidinoaspartase | |||||||||
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| Identifiers | |||||||||
| EC number | 3.5.3.14 | ||||||||
| CAS number | 37325-60-3 | ||||||||
| 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, an amidinoaspartase (EC 3.5.3.14) is an enzyme that catalyzes the chemical reaction
- N-amidino-L-aspartate + H2O [math]\displaystyle{ \rightleftharpoons }[/math] L-aspartate + urea
Thus, the two substrates of this enzyme are N-amidino-L-aspartate and H2O, whereas its two products are L-aspartate 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 N-amidino-L-aspartate amidinohydrolase. This enzyme is also called amidinoaspartic amidinohydrolase.
References
- "Metabolism of guanidinosuccinic acid. I. Characterization of a specific amidino hydrolase from Pseudomonas chlororaphis". J. Biol. Chem. 247 (19): 6280–3. 1972. PMID 4651648.
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