CATH Classification

Domain Context

CATH Clusters

Superfamily Chloramphenicol acetyltransferase-like domain
Functional Family Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex

Enzyme Information
Dihydrolipoyllysine-residue (2-methylpropanoyl)transferase.
based on mapping to UniProt P11181
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.

UniProtKB Entries (1)

Bos taurus
Lipoamide acyltransferase component of branched-chain alpha-keto acid dehydrogenase complex, mitochondrial

PDB Structure

External Links
Organism Escherichia
Primary Citation
A synchronized substrate-gating mechanism revealed by cubic-core structure of the bovine branched-chain alpha-ketoacid dehydrogenase complex.
Kato, M., Wynn, R.M., Chuang, J.L., Brautigam, C.A., Custorio, M., Chuang, D.T.
Embo J.