In enzymology, L-erythro-3,5-diaminohexanoate dehydrogenase (EC 1.4.1.11) is an enzyme that catalyzes the chemical reaction
| 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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-3,5-diaminohexanoic_acid.svg)
-5-amino-3-oxohexanoic_acid.svg)
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
edit- ↑ Enzyme 1.4.1.11 at KEGG Pathway Database.
- ↑ 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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