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L-erythro-3,5-diaminohexanoate dehydrogenase

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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
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PMC articles
PubMed articles
NCBI proteins

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

+ NAD+
 
 
H2O
H+
L-erythro-3,5-diaminohexanoate dehydrogenase
H2O
H+
 
+ NADH + NH3
 

The three substrates of this enzyme are L-erythro-3,5-diaminohexanoic acid, water, and oxidised nicotinamide adenine dinucleotide (NAD+). Its products are (S)-5-amino-3-oxohexanoic acid, reduced NADH, ammonia, and a proton. [1] [2]

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

  1. Enzyme 1.4.1.11 at KEGG Pathway Database.
  2. 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. doi: 10.1016/S0021-9258(19)44584-5 . PMID   4344229.


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