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ENZYME

ENZYME entry: EC 1.2.1.95

PURL: https://purl.expasy.org/enzyme/EC/1.2.1.95
Accepted Name
L-2-aminoadipate reductase
Alternative Name(s)
alpha-aminoadipate reductase
Reaction catalysed
(S)-2-amino-6-oxohexanoate + AMP + diphosphate + NADP(+) = L-2-aminoadipate + ATP + NADPH + H(+)
Comment(s)
  • This enzyme, characterized from the yeast Saccharomyces cerevisiae, catalyzes 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 which catalyzes a similar transformation in the opposite direction without ATP hydrolysis.
Cross-references
BRENDA1.2.1.95
EC2PDB1.2.1.95
ExplorEnz1.2.1.95
KEGG Ligand Database for Enzyme Nomenclature1.2.1.95
IUBMB Enzyme Nomenclature1.2.1.95
MEDLINEFind literature relating to 1.2.1.95
MetaCyc1.2.1.95
Rhea expert-curated reactions1.2.1.95
UniProtKB/Swiss-Prot
Q12572, LYS2_CANAXQ6FMI5, LYS2_CANGAQ75BB3, LYS2_EREGS
O74298, LYS2_PENCHP40976, LYS2_SCHPOP07702, LYS2_YEAST

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All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 1.2.1.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 1.2.-.-
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