CATH Classification

Domain Context

CATH Clusters

Functional Family 2-oxoisovalerate dehydrogenase subunit alpha

Enzyme Information
3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring).
based on mapping to UniProt P12694
3-methyl-2-oxobutanoate + [dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] lipoyllysine = [dihydrolipoyllysine- residue (2-methylpropanoyl)transferase] S-(2-methylpropanoyl)dihydrolipoyllysine + CO(2).
-!- It acts not only on 3-methyl-2-oxobutanaoate, but also on 4-methyl-2- oxopentanoate and (S)-3-methyl-2-oxopentanoate, so that it acts on the 2-oxo acids that derive from the action of transaminases on valine, leucine and isoleucine. -!- It is a component of the multienzyme 3-methyl-2-oxobutanoate dehydrogenase complex in which multiple copies of it are bound to a core of molecules of EC, which also binds multiple copies of EC -!- It does not act on free lipoamide or lipoyllysine, but only on the lipoyllysine residue in EC -!- Formerly EC

UniProtKB Entries (1)

Homo sapiens
2-oxoisovalerate dehydrogenase subunit alpha, mitochondrial

PDB Structure

External Links
Organism Escherichia
Primary Citation
Crystal structure of human branched-chain alpha-ketoacid dehydrogenase and the molecular basis of multienzyme complex deficiency in maple syrup urine disease.
AEvarsson, A., Chuang, J.L., Wynn, R.M., Turley, S., Chuang, D.T., Hol, W.G.
Structure Fold.Des.