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A new class EC 7, Translocases, has been added to the EC list. It will be part of ENZYME from release 2018_10. Read more about EC 7 here.

ENZYME entry: EC 1.2.1.95

Accepted Name
L-2-aminoadipate reductase.
Alternative Name(s)
Alpha-aminoadipate reductase.
Reaction catalysed
(S)-2-amino-6-oxohexanoate + NADP(+) + AMP + diphosphate <=> L-2-aminoadipate + NADPH + ATP
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
PRIAM enzyme-specific profiles1.2.1.95
KEGG Ligand Database for Enzyme Nomenclature1.2.1.95
IUBMB Enzyme Nomenclature1.2.1.95
IntEnz1.2.1.95
MEDLINEFind literature relating to 1.2.1.95
MetaCyc1.2.1.95
UniProtKB/Swiss-Prot
Q75BB3, LYS2_ASHGO;  Q12572, LYS2_CANAX;  Q6FMI5, LYS2_CANGA;  
O74298, LYS2_PENCH;  P40976, LYS2_SCHPO;  P07702, 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.-.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 1.-.-.-