L-erythro-3,5-diaminohexanoate dehydrogenase

In enzymology, a L-erythro-3,5-diaminohexanoate dehydrogenase (EC 1.4.1.11) is an enzyme that catalyzes the chemical reaction

L-erythro-3,5-diaminohexanoate + H₂O + NAD⁺ ${\displaystyle \rightleftharpoons }$ (S)-5-amino-3-oxohexanoate + NH₃ + NADH + H⁺

L-erythro-3,5-diaminohexanoate dehydrogenase
Identifiers
EC no.	1.4.1.11
CAS no.	37377-90-5
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

The 3 substrates of this enzyme are L-erythro-3,5-diaminohexanoate, H₂O, and NAD⁺, whereas its 4 products are (S)-5-amino-3-oxohexanoate, NH₃, NADH, and H⁺.

This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH2 group of donors with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is L-erythro-3,5-diaminohexanoate:NAD+ oxidoreductase (deaminating). This enzyme is also called L-3,5-diaminohexanoate dehydrogenase. This enzyme participates in lysine degradation.