CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
1 | Mainly Alpha |
|
1.20 | Up-down Bundle |
|
1.20.140 | Butyryl-CoA Dehydrogenase, subunit A; domain 3 |
|
1.20.140.20 | Alpha-ketoacid/pyruvate dehydrogenase kinase, N-terminal domain |
Domain Context
CATH Clusters
| Superfamily | Alpha-ketoacid/pyruvate dehydrogenase kinase, N-terminal domain |
| Functional Family | [Pyruvate dehydrogenase (acetyl-transferring)] kinase isozyme 2, mitochondrial |
Enzyme Information
| 2.7.11.2 |
[Pyruvate dehydrogenase (acetyl-transferring)] kinase.
based on mapping to UniProt Q64536
ATP + [pyruvate dehydrogenase (acetyl-transferring)] = ADP + [pyruvate dehydrogenase (acetyl-transferring)] phosphate.
-!- Has no activating compound but is specific for its substrate. -!- A mitochondrial enzyme associated with the pyruvate dehydrogenase complex in mammals. -!- Phosphorylation inactivates EC 1.2.4.1. -!- Formerly EC 2.7.1.99.
|
UniProtKB Entries (2)
| Q64536 |
PDK2_RAT
Rattus norvegicus
[Pyruvate dehydrogenase (acetyl-transferring)] kinase isozyme 2, mitochondrial
|
| P10515 |
ODP2_HUMAN
Homo sapiens
Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial
|
PDB Structure
| PDB | 3CRK |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
Structural and functional insights into the molecular mechanisms responsible for the regulation of pyruvate dehydrogenase kinase 2.
J.Biol.Chem.
|