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 | Acetyltransferase component of pyruvate dehydrogenase complex |
Enzyme Information
| 2.3.1.12 |
Dihydrolipoyllysine-residue acetyltransferase.
based on mapping to UniProt Q8X966
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)
| Q8X966 |
Q8X966_ECO57
Escherichia coli O157:H7
Acetyltransferase component of pyruvate dehydrogenase complex
|
PDB Structure
| PDB | 4QOY |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Novel Binding Motif and New Flexibility Revealed by Structural Analyses of a Pyruvate Dehydrogenase-Dihydrolipoyl Acetyltransferase Subcomplex from the Escherichia coli Pyruvate Dehydrogenase Multienzyme Complex.
J.Biol.Chem.
|