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

Reactions

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

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB
UniProtKB/Swiss-Prot:

References

  1. Ehmann, D. E., Gehring, A. M., Walsh, C. T.
    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]