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EC 1.2.1.95 Details
EC number
1.2.1.95
Accepted name
L-2-aminoadipate reductase
Reaction
(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+
Other name(s)
LYS2, α-aminoadipate reductase
Systematic name
(S)-2-amino-6-oxohexanoate:NADP+ oxidoreductase (ATP-forming)
Comment
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.
History
created 2015
EC Tree
1.2.1.1 created 1961, modified 1982, modified 2002, deleted 2005
1.2.1.6 created 1961, deleted 1965
1.2.1.14 created 1961, deleted 1984
1.2.1.34 created 1972, deleted 1983 [transferred to EC 1.1.1.180, deleted 1984]
1.2.1.35 created 1972, deleted 1984
1.2.1.37 created 1972, deleted 1984
1.2.1.55 created 1990, deleted 2003
1.2.1.56 created 1990, deleted 2003