ExplorEnz: EC 1.2.1.95

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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⁺

Glossary:

L-2-aminoadipate = (2S)-2-aminohexanedioate

Other name(s):

LYS2; α-aminoadipate reductase

Systematic name:

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

Comments:

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.

Links to other databases:

BRENDA, EXPASY, Gene, KEGG, MetaCyc

References:

1.	Ehmann, D.E., Gehring, A.M. and Walsh, C.T. Lysine biosynthesis in Saccharomyces cerevisiae: mechanism of α-aminoadipate reductase (Lys²) involves posttranslational phosphopantetheinylation by Lys⁵. Biochemistry 38 (1999) 6171–6177. [DOI] [PMID: 10320345]

[EC 1.2.1.95 created 2015]