Lysine 6-dehydrogenase (LysDH) (LysDH)

Lysine 6-dehydrogenase (LysDH) is an oxidoreductase enzyme that catalyzes the NAD+-dependent oxidative deamination of the ε-amino group of L-lysine, yielding L-2-aminoadipate-6-semialdehyde and ammonia [UniProt, P23232]. Although not naturally occurring in the primary human lysine degradation pathway—which utilizes the saccharopine pathway—LysDH is widely distributed among various bacterial species and is a key component of their nitrogen metabolism [PubMed, 2675432]. In clinical medicine, the enzyme is highly significant as a diagnostic tool, specifically used in enzymatic assays to monitor L-lysine levels in patients with hyperlysinemia, a condition that can lead to neurological impairment if left untreated [PubMed, 15563365]. Research into LysDH also extends to its potential as an antimicrobial target, as its inhibition could selectively impair bacterial growth without affecting human metabolic pathways [PubMed, 10411744]. Additionally, its high substrate specificity and stability make it a preferred candidate for the development of biosensors and industrial biocatalytic processes [PubMed, 15123193]. While no FDA-approved drugs currently target LysDH, it remains a focal point for developing narrow-spectrum antibiotics and synthesizing chiral intermediates like pipecolic acid. Its role in the conversion of lysine to aminoadipate semialdehyde links it to the broader context of amino acid catabolism and energy production in microbes.

Other names

L-lysine 6-dehydrogenaseLysine dehydrogenaseL-lysine:NAD+ 6-oxidoreductase (deaminating)

Catalyzes the NAD+-dependent oxidative deamination of the epsilon-amino group of L-lysine to form L-2-aminoadipate-6-semialdehyde.