EC Explorer

1.2.1.95

L-2-aminoadipate reductase

(S)-2-amino-6-oxohexanoate + NADP⁺ + AMP + diphosphate = L-2-aminoadipate + NADPH + H⁺ + ATP (overall reaction);;(1a) L-2-aminoadipyl-[LYS2 peptidyl-carrier-protein] + AMP + diphosphate = L-2-aminoadipate + holo-[LYS2 peptidyl-carrier-protein] + ATP;;(1b) (S)-2-amino-6-oxohexanoate + holo-[LYS2 peptidyl-carrier-protein] + NADP⁺ = L-2-aminoadipyl-[LYS2 peptidyl-carrier-protein] + NADPH + H⁺

LYS2, α-aminoadipate reductase

(S)-2-amino-6-oxohexanoate:NADP⁺ oxidoreductase (ATP-forming)

This enzyme, characterized from the yeast Saccharomyces cerevisiae, catalyses the reduction of L-2-aminoadipate to (S)-2-amino-6-oxohexanoate during L-lysine biosynthesis. An adenylation domain activates the substrate at the expense of ATP hydrolysis, and forms L-2-aminoadipate adenylate, which is attached to a peptidyl-carrier protein (PCP) domain. Binding of NADPH results in reductive cleavage of the acyl-S-enzyme intermediate, releasing (S)-2-amino-6-oxohexanoate. Different from EC 1.2.1.31, L-aminoadipate-semialdehyde dehydrogenase, which catalyses a similar transformation in the opposite direction without ATP hydrolysis.

created 2015