From Wikipedia, the free encyclopedia
L-erythro-3,5-diaminohexanoate dehydrogenase | |||||||||
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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 | ||||||||
|
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.
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