CATH Classification

Domain Context

CATH Clusters

Superfamily E3-binding domain
Functional Family Branched-chain alpha-keto acid dihydrolipoyl acyltransferase

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 1ZWV
External Links
Method SOLUTION NMR
Organism Escherichia
Primary Citation
Solution Structure of the subunit binding domain (hbSBD) of the human mitochondrial branched-chain alpha-ketoacid dehydrogenase
Chang, C.F., Chuang, D.T., Huang, T.h.
to be published