From Wikipedia, the free encyclopedia
Lysine 6-dehydrogenase (
EC
1.4.1.18, L-lysine epsilon-dehydrogenase, L-lysine 6-dehydrogenase, LysDH) is an
enzyme with
systematic name L-lysine:NAD+ 6-oxidoreductase (deaminating).
[1]
[2]
[3]
[4] This enzyme
catalyses the following
chemical reaction
-
L-lysine + NAD+
(S)-2,3,4,5-tetrahydropyridine-2-carboxylate + NADH + H+ + NH3 (overall reaction)
- (1a) L-lysine + NAD+ + H2O
(S)-2-amino-6-oxohexanoate + NADH + H+ + NH3
- (1b) (S)-2-amino-6-oxohexanoate
(S)-2,3,4,5-tetrahydropyridine-2-carboxylate + H2O (spontaneous)
The enzyme is highly specific for
L-lysine as substrate, although
S-(2-aminoethyl)-L-cysteine can act as a substrate, but more slowly.
References
-
^ Misono H, Nagasaki S (April 1982).
"Occurrence of L-lysine epsilon-dehydrogenase in Agrobacterium tumefaciens". Journal of Bacteriology. 150 (1): 398–401.
doi:
10.1128/jb.150.1.398-401.1982.
PMC
220128.
PMID
6801024.
-
^ Misono H, Uehigashi H, Morimoto E, Nagasaki S (1985).
"Purification and properties of L-lysine ε-dehydrogenase from Agrobacterium tumefaciens". Agric. Biol. Chem. 49 (7): 2253–2255.
doi:
10.1271/bbb1961.49.2253.
-
^ Misono H, Hashimoto H, Uehigashi H, Nagata S, Nagasaki S (June 1989). "Properties of L-lysine epsilon-dehydrogenase from Agrobacterium tumefaciens". Journal of Biochemistry. 105 (6): 1002–8.
doi:
10.1093/oxfordjournals.jbchem.a122757.
PMID
2768207.
-
^ Heydari M, Ohshima T, Nunoura-Kominato N, Sakuraba H (February 2004).
"Highly stable L-lysine 6-dehydrogenase from the thermophile Geobacillus stearothermophilus isolated from a Japanese hot spring: characterization, gene cloning and sequencing, and expression". Applied and Environmental Microbiology. 70 (2): 937–42.
Bibcode:
2004ApEnM..70..937H.
doi:
10.1128/aem.70.2.937-942.2004.
PMC
348916.
PMID
14766574.
External links
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