ENZYME entry: EC

Accepted Name
Dihydrolipoyllysine-residue (2-methylpropanoyl)transferase.
Alternative Name(s)
Dihydrolipoyl transacylase.
Reaction catalysed
2-methylpropanoyl-CoA + enzyme N(6)-(dihydrolipoyl)lysine <=> CoA + enzyme N(6)-(S-(2-methylpropanoyl)dihydrolipoyl)lysine
  • A multimer (24-mer) of this enzyme forms the core of the multienzyme 3-methyl-2-oxobutanoate dehydrogenase complex, and binds tightly both EC and EC
  • The lipoyl group of this enzyme is reductively 2-methylpropanoylated by EC, and the only observed direction catalyzed by EC is that where this 2-methylpropanoyl is passed to coenzyme A.
  • In addition to the 2-methylpropanoyl group, formed when EC acts on the oxoacid that corresponds with valine, this enzyme also transfers the 3-methylbutanoyl and S-2-methylbutanoyl groups, donated to it when EC acts on the oxo acids corresponding with leucine and isoleucine.
PRIAM enzyme-specific profiles2.3.1.168
KEGG Ligand Database for Enzyme Nomenclature2.3.1.168
IUBMB Enzyme Nomenclature2.3.1.168
MEDLINEFind literature relating to
O06159, BKDC_MYCTU;  Q9M7Z1, ODB2_ARATH;  P37942, ODB2_BACSU;  
P11181, ODB2_BOVIN;  Q23571, ODB2_CAEEL;  P11182, ODB2_HUMAN;  
P53395, ODB2_MOUSE;  Q9I1M0, ODB2_PSEAE;  P09062, ODB2_PSEPU;  

View entry in original ENZYME format
View entry in raw text format (no links)

All UniProtKB/Swiss-Prot entries referenced in this entry, with possibility to download in different formats, align etc.
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 2.3.1.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 2.3.-.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 2.-.-.-