L-erythro-3,5-diaminohexanoate dehydrogenase

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L-erythro-3,5-diaminohexanoate dehydrogenase
Identifiers
EC number 1.4.1.11
CAS number 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

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+ (S)-5-amino-3-oxohexanoate + NH3 + NADH + H+

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.

References[edit]

  • Baker JJ, Jeng I, Barker HA (1972). "Purification and properties of L-erythro-3,5-diaminohexanoate dehydrogenase from a lysine-fermenting Clostridium". J. Biol. Chem. 247 (23): 7724–34. PMID 4344229.