Formimidoylaspartate deiminase
From Wikipedia, the free encyclopedia
In enzymology, a formimidoylaspartate deiminase (EC 3.5.3.5) is an enzyme that catalyzes the chemical reaction
- N-formimidoyl-L-aspartate + H2O N-formyl-L-aspartate + NH3
Thus, the two substrates of this enzyme are N-formimidoyl-L-aspartate and H2O, whereas its two products are N-formyl-L-aspartate and NH3.
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-formimidoyl-L-aspartate iminohydrolase. This enzyme is also called formiminoaspartate deiminase. This enzyme participates in histidine metabolism.
[edit] References
- IUBMB entry for 3.5.3.5
- BRENDA references for 3.5.3.5 (Recommended.)
- PubMed references for 3.5.3.5
- PubMed Central references for 3.5.3.5
- Google Scholar references for 3.5.3.5
- HAYAISHI O, TABOR H, HAYAISHI T (1957). "N-formimino-L-aspartic acid as an intermediate in the enzymatic conversion of imidazoleacetic acid to formylaspartic acid". J. Biol. Chem. 227: 161–80. PMID 13449062.
[edit] External links
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- The CAS registry number for this enzyme class is 9025-07-4.