Amidinoaspartase
| amidinoaspartase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| 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 / EGO | ||||||||
| |||||||||
In enzymology, an amidinoaspartase (EC 3.5.3.14) is an enzyme that catalyzes the chemical reaction
- N-amidino-L-aspartate + H2O 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
- Milstien S, Goldman P (1972). "Metabolism of guanidinosuccinic acid. I. Characterization of a specific amidino hydrolase from Pseudomonas chlororaphis". J. Biol. Chem. 247 (19): 6280–3. PMID 4651648.
This article is issued from Wikipedia - version of the 8/10/2016. The text is available under the Creative Commons Attribution/Share Alike but additional terms may apply for the media files.