ENZYME entry: EC 2.3.1.168
Accepted Name |
dihydrolipoyllysine-residue (2-methylpropanoyl)transferase.
|
Alternative Name(s) |
dihydrolipoyl transacylase. |
Reaction catalysed |
(R)-N(6)-dihydrolipoyl-L-lysyl-[protein] + 2-methylpropanoyl-CoA <=> (R)-N(6)-(S(8)-2-methylpropanoyldihydrolipoyl)-L-lysyl-[protein] + CoA |
Comment(s) |
- A multimer (24-mer) of this enzyme forms the core of the multienzyme
3-methyl-2-oxobutanoate dehydrogenase complex, and binds tightly both
EC 1.2.4.4 and EC 1.8.1.4.
- The lipoyl group of this enzyme is reductively 2-methylpropanoylated
by EC 1.2.4.4, and the only observed direction catalyzed by
EC 2.3.1.168 is that where this 2-methylpropanoyl is passed to
coenzyme A.
- In addition to the 2-methylpropanoyl group, formed when EC 1.2.4.4
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 1.2.4.4 acts on the oxo acids corresponding with
leucine and isoleucine.
|
Cross-references |
BRENDA | 2.3.1.168 |
EC2PDB | 2.3.1.168 |
ExplorEnz | 2.3.1.168 |
PRIAM enzyme-specific profiles | 2.3.1.168 |
KEGG Ligand Database for Enzyme Nomenclature | 2.3.1.168 |
IUBMB Enzyme Nomenclature | 2.3.1.168 |
IntEnz | 2.3.1.168 |
MEDLINE | Find literature relating to 2.3.1.168 |
MetaCyc | 2.3.1.168 |
Rhea expert-curated reactions | 2.3.1.168 |
UniProtKB/Swiss-Prot |
|
View entry in original ENZYME format
View entry in raw text format (no links)
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.-.-.-