Lysine 6-dehydrogenase

Lysine 6-dehydrogenase
Identifiers
EC number 1.4.1.18
CAS number 89400-30-6
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum

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+ \rightleftharpoons (S)-2,3,4,5-tetrahydropyridine-2-carboxylate + NADH + H+ + NH3 (overall reaction)
(1a) L-lysine + NAD+ + H2O \rightleftharpoons (S)-2-amino-6-oxohexanoate + NADH + H+ + NH3
(1b) (S)-2-amino-6-oxohexanoate \rightleftharpoons (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

  1. ↑ Misono, H. and Nagasaki, S. (1982). "Occurrence of L-lysine ε-dehydrogenase in Agrobacterium tumefaciens". J. Bacteriol. 150 (1): 398–401. PMC 220128. PMID 6801024.
  2. ↑ Misono, H., Uehigashi, H., Morimoto, E. and Nagasaki, S. (1985). "Purification and properties of L-lysine ε-dehydrogenase from Agrobacterium tumefaciens". Agric. Biol. Chem. 49: 2253–2255. doi:10.1271/bbb1961.49.2253.
  3. ↑ Misono, H., Hashimoto, H., Uehigashi, H., Nagata, S. and Nagasaki, S. (1989). "Properties of L-lysine ε-dehydrogenase from Agrobacterium tumefaciens". J. Biochem. (Tokyo) 105 (6): 1002–1008. PMID 2768207.
  4. ↑ Heydari, M., Ohshima, T., Nunoura-Kominato, N. and Sakuraba, H. (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". Appl. Environ. Microbiol. 70 (2): 937–942. doi:10.1128/aem.70.2.937-942.2004. PMC 348916. PMID 14766574.

External links


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