CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.40 | 3-Layer(aba) Sandwich |
|
3.40.50 | Rossmann fold |
|
3.40.50.970 | Thiamin diphosphate (ThDP)-binding fold, Pyr/PP domains |
Domain Context
CATH Clusters
| Superfamily | 3.40.50.970 |
| Functional Family | Pyruvate dehydrogenase E1 beta subunit |
Enzyme Information
| 1.2.4.4 |
3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring).
based on mapping to UniProt P21953
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 2.3.1.168, which also binds multiple copies of EC 1.8.1.4. -!- It does not act on free lipoamide or lipoyllysine, but only on the lipoyllysine residue in EC 2.3.1.168. -!- Formerly EC 1.2.4.3.
|
UniProtKB Entries (1)
| P12694 |
ODBA_HUMAN
Homo sapiens
2-oxoisovalerate dehydrogenase subunit alpha, mitochondrial
|
PDB Structure
| PDB | 1X7Y |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
Molecular mechanism for regulation of the human mitochondrial branched-chain alpha-ketoacid dehydrogenase complex by phosphorylation
Structure
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