CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
4 | Few Secondary Structures |
|
4.10 | Irregular |
|
4.10.320 | Dihydrolipoamide Transferase |
|
4.10.320.10 | E3-binding domain |
Domain Context
CATH Clusters
| Superfamily | E3-binding domain |
| Functional Family | Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex |
Enzyme Information
| 2.3.1.12 |
Dihydrolipoyllysine-residue acetyltransferase.
based on mapping to UniProt P11961
Acetyl-CoA + enzyme N(6)-(dihydrolipoyl)lysine = CoA + enzyme N(6)- (S-acetyldihydrolipoyl)lysine.
-!- A multimer (24-mer or 60-mer, depending on the source) of this enzyme forms the core of the pyruvate dehydrogenase multienzyme complex, and binds tightly both EC 1.2.4.1 and EC 1.8.1.4. -!- The lipoyl group of this enzyme is reductively acetylated by EC 1.2.4.1, and the only observed direction catalyzed by EC 2.3.1.12 is that where the acetyl group is passed to coenzyme A.
|
UniProtKB Entries (1)
| P21874 |
ODPB_GEOSE
Geobacillus stearothermophilus
Pyruvate dehydrogenase E1 component subunit beta
|
PDB Structure
| PDB | 1W85 |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
A molecular switch and proton wire synchronize the active sites in thiamine enzymes.
Science
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