Biology:L-erythro-3,5-diaminohexanoate dehydrogenase
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| L-erythro-3,5-diaminohexanoate dehydrogenase | |||||||||
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| 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 | ||||||||
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In enzymology, L-erythro-3,5-diaminohexanoate dehydrogenase (EC 1.4.1.11) is an enzyme that catalyzes the chemical reaction
- REDIRECT Template:Chemical reaction
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
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