CATH Classification

Domain Context

CATH Clusters

Superfamily 2.40.50.100
Functional Family Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex

Enzyme Information

2.3.1.168
Dihydrolipoyllysine-residue (2-methylpropanoyl)transferase.
based on mapping to UniProt P11182
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 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.

UniProtKB Entries (1)

P11182
ODB2_HUMAN
Homo sapiens
Lipoamide acyltransferase component of branched-chain alpha-keto acid dehydrogenase complex, mitochondrial

PDB Structure

PDB 1K8O
External Links
Method SOLUTION NMR
Organism Escherichia
Primary Citation
Solution structure and dynamics of the lipoic acid-bearing domain of human mitochondrial branched-chain alpha-keto acid dehydrogenase complex
Chang, C.-F., Chou, H.-T., Chuang, J.L., Chuang, D.T., Huang, T.-h.
J.Biol.Chem.