IUBMB Enzyme Nomenclature

EC 1.4.1.18

Accepted name: lysine 6-dehydrogenase

Reaction: L-lysine + NAD+ = (S)-2,3,4,5-tetrahydropyridine-2-carboxylate + NADH + H+ + NH3 (overall reaction)
(1a) L-lysine + NAD+ + H2O = (S)-2-aminoadipate 6-semialdehyde + NADH + H+ + NH3
(1b) (S)-2-aminoadipate 6-semialdehyde = (S)-2,3,4,5-tetrahydropiperidine-2-carboxylate + H2O (spontaneous)

For diagram click here, another example.

Glossary: (S)-2-amino-6-oxohexanoate = L-2-aminoadipate 6-semialdehyde = L-allysine
L-1-piperideine 6-carboxylate = (S)-2,3,4,5-tetrahydropyridine-2-carboxylate = (S)-1,6-didehydropiperidine-2-carboxylate

Other name(s): L-lysine ε-dehydrogenase; L-lysine 6-dehydrogenase; LysDH

Systematic name: L-lysine:NAD+ 6-oxidoreductase (deaminating)

Comments: The enzyme is highly specific for L-lysine as substrate, although (S)-(β-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].

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 89400-30-6

References:

1. Misono, H. and Nagasaki, S. Occurrence of L-lysine ε-dehydrogenase in Agrobacterium tumefaciens. J. Bacteriol. 150 (1982) 398-401. [PMID: 6801024]

2. Misono, H., Uehigashi, H., Morimoto, E. and Nagasaki, S. Purification and properties of L-lysine ε-dehydrogenase from Agrobacterium tumefaciens. Agric. Biol. Chem. 49 (1985) 2253-2255.

3. Misono, H., Hashimoto, H., Uehigashi, H., Nagata, S. and Nagasaki, S. Properties of L-lysine ε-dehydrogenase from Agrobacterium tumefaciens. J. Biochem. (Tokyo) 105 (1989) 1002-1008. [PMID: 2768207]

4. Heydari, M., Ohshima, T., Nunoura-Kominato, N. and Sakuraba, H. Highly stable L-lysine 6-dehydrogenase from the thermophile Geobacillus stearothermophilus isolated from a Japanese hot spring: characterization, gene cloning and sequencing, and expression. Appl. Environ. Microbiol. 70 (2004) 937-942. [PMID: 14766574]

[EC 1.4.1.18 created 1989, modified 2006]


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