EC 1 - Oxidoreductases
EC 1.2 - Acting on the aldehyde or oxo group of donors
EC 1.2.1 - With NAD+ or NADP+ as acceptor
EC 1.2.1.95 - L-2-aminoadipate reductase
IntEnz view
ENZYME view
IntEnz Enzyme Nomenclature
EC 1.2.1.95
Names
Accepted name:
L-2-aminoadipate reductase
Other
names:
LYS2
α-aminoadipate reductase
α-aminoadipate reductase
Systematic name:
(S)-2-amino-6-oxohexanoate:NADP+ oxidoreductase (ATP-forming)
Reactions
- (1) (S)-2-amino-6-oxohexanoate + NADP+ + AMP + diphosphate = L-2-aminoadipate + NADPH + H+ + ATP
- (1a) L-2-aminoadipyl-S-LYS2 peptidyl-carrier-protein + AMP + diphosphate = holo-L-2-aminoadipate + LYS2 peptidyl-carrier-protein + ATP
- (1b) (S)-2-amino-6-oxohexanoate + holo-LYS2 peptidyl-carrier-protein + NADP+ = L-2-aminoadipyl-S-LYS2 peptidyl-carrier-protein + NADPH + H+
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
UniProtKB/Swiss-Prot:
LYS2_ASHGO
LYS2_CANAX
LYS2_CANGA
LYS2_PENCH
LYS2_SCHPO
LYS2_YEAST
References
-
Lysine biosynthesis in Saccharomyces cerevisiae: mechanism of alpha-aminoadipate reductase (Lys2) involves posttranslational phosphopantetheinylation by Lys5.Biochemistry 38 : 6171-6177 (1999). [PMID: 10320345]
[EC 1.2.1.95 created 2015]