Lysine_6-dehydrogenase

Lysine 6-dehydrogenase

Lysine 6-dehydrogenase

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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)
Quick Facts Identifiers, EC no. ...

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

  1. [1]
    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.
  2. [2]
    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.
  3. [3]
    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.
  4. [4]
    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.


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