Jump to content

L-erythro-3,5-diaminohexanoate dehydrogenase

From Wikipedia, the free encyclopedia

This is an old revision of this page, as edited by Dcirovic (talk | contribs) at 03:50, 21 May 2016 (References: clean up using AWB). The present address (URL) is a permanent link to this revision, which may differ significantly from the current revision.

L-erythro-3,5-diaminohexanoate dehydrogenase
Identifiers
EC no.1.4.1.11
CAS no.37377-90-5
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Search
PMCarticles
PubMedarticles
NCBIproteins

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

  • 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.