KEGG   ENZYME: 1.4.1.18
Entry
EC 1.4.1.18                 Enzyme                                 

Name
lysine 6-dehydrogenase;
L-lysine epsilon-dehydrogenase;
L-lysine 6-dehydrogenase;
LysDH
Class
Oxidoreductases;
Acting on the CH-NH2 group of donors;
With NAD+ or NADP+ as acceptor
Sysname
L-lysine:NAD+ 6-oxidoreductase (deaminating)
Reaction(IUBMB)
L-lysine + NAD+ = (S)-2,3,4,5-tetrahydropyridine-2-carboxylate + NADH + H+ + NH3 (overall reaction) [RN:R10054];
(1a) L-lysine + NAD+ + H2O = (S)-2-amino-6-oxohexanoate + NADH + H+ + NH3 [RN:R00446];
(1b) (S)-2-amino-6-oxohexanoate = (S)-2,3,4,5-tetrahydropyridine-2-carboxylate + H2O (spontaneous) [RN:R02317]
Reaction(KEGG)
Substrate
L-lysine [CPD:C00047];
NAD+ [CPD:C00003];
H2O [CPD:C00001];
(S)-2-amino-6-oxohexanoate [CPD:C04076]
Product
(S)-2,3,4,5-tetrahydropyridine-2-carboxylate [CPD:C00450];
NADH [CPD:C00004];
H+ [CPD:C00080];
NH3 [CPD:C00014];
(S)-2-amino-6-oxohexanoate [CPD:C04076];
H2O [CPD:C00001]
Comment
The enzyme is highly specific for L-lysine as substrate, although S-(2-aminoethyl)-L-cysteine can act as a substrate, but more slowly. While the enzyme from Agrobacterium tumefaciens can use only NAD+, that from the thermophilic bacterium Geobacillus stearothermophilus can also use NADP+, but more slowly [1,4].
History
EC 1.4.1.18 created 1989, modified 2006, modified 2011
Pathway
ec00960  Tropane, piperidine and pyridine alkaloid biosynthesis
ec01100  Metabolic pathways
ec01110  Biosynthesis of secondary metabolites
Orthology
K19064  lysine 6-dehydrogenase
Genes
BACO: OXB_1319
BSM: BSM4216_3155
BFD: NCTC4823_01480(lys1_1)
OIH: OB0862
OCN: CUC15_05270
OCB: CV093_05535
GKA: GK0375
GTE: GTCCBUS3UF5_4780
GTK: GT3570_01870
GTM: GT3921_17330
GTN: GTNG_0350
GEA: GARCT_00423(lysDH)
PCAL: BV455_01368(lysDH)
AFL: Aflv_1247
LSP: Bsph_0857
HLI: HLI_20185
VPN: A21D_02343(lysDH)
PSYO: PB01_02625
BLEN: NCTC4824_00341(lys1_1)
SIV: SSIL_3578
GAU: GAU_0501
GBA: J421_2400
 » show all
Reference
1  [PMID:6801024]
  Authors
Misono H, Nagasaki S.
  Title
Occurrence of L-lysine epsilon-dehydrogenase in Agrobacterium tumefaciens.
  Journal
J Bacteriol 150:398-401 (1982)
DOI:10.1128/JB.150.1.398-401.1982
Reference
2
  Authors
Misono, H., Uehigashi, H., Morimoto, E. and Nagasaki, S.
  Title
Purification and properties of L-lysine epsilon-dehydrogenase from Agrobacterium tumefaciens.
  Journal
Agric Biol Chem 49:2253-2255 (1985)
Reference
3  [PMID:2768207]
  Authors
Misono H, Hashimoto H, Uehigashi H, Nagata S, Nagasaki S.
  Title
Properties of L-lysine epsilon-dehydrogenase from Agrobacterium tumefaciens.
  Journal
J Biochem (Tokyo) 105:1002-8 (1989)
DOI:10.1093/oxfordjournals.jbchem.a122757
Reference
4  [PMID:14766574]
  Authors
Heydari M, Ohshima T, Nunoura-Kominato N, Sakuraba H
  Title
Highly stable L-lysine 6-dehydrogenase from the thermophile Geobacillus stearothermophilus isolated from a Japanese hot spring: characterization, gene cloning and sequencing, and expression.
  Journal
Appl Environ Microbiol 70:937-42 (2004)
DOI:10.1128/AEM.70.2.937-942.2004
  Sequence
Other DBs
ExplorEnz - The Enzyme Database: 1.4.1.18
IUBMB Enzyme Nomenclature: 1.4.1.18
ExPASy - ENZYME nomenclature database: 1.4.1.18
BRENDA, the Enzyme Database: 1.4.1.18
CAS: 89400-30-6

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