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In enzymology, a formimidoylaspartate deiminase (EC 3.5.3.5) is an enzyme that catalyzes the chemical reaction

N-formimidoyl-L-aspartate + H₂O ${\displaystyle \rightleftharpoons }$ 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.

References

• 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 (1): 161–80. PMID 13449062.

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