Formimidoylaspartate deiminase

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

formimidoylaspartate deiminase
Identifiers
EC no.	3.5.3.5
CAS no.	9025-07-4
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
Search PMC articles PubMed articles NCBI proteins

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.