|
Your query returned 1 entry. Printable version
EC | 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: |
| ||