Amidinoaspartase
From Wikipedia, the free encyclopedia
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.
[edit] References
- IUBMB entry for 3.5.3.14
- BRENDA references for 3.5.3.14 (Recommended.)
- PubMed references for 3.5.3.14
- PubMed Central references for 3.5.3.14
- Google Scholar references for 3.5.3.14
- Milstien S, Goldman P (1972). "Metabolism of guanidinosuccinic acid. I. Characterization of a specific amidino hydrolase from Pseudomonas chlororaphis". J. Biol. Chem. 247: 6280–3. PMID 4651648.
[edit] External links
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- The CAS registry number for this enzyme class is 37325-60-3.