CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
6 | Special |
|
6.20 | Other non-globular |
|
6.20.100 | Actin; Chain A, domain 2 |
|
6.20.100.10 |
Domain Context
CATH Clusters
| Superfamily | 6.20.100.10 |
| Functional Family |
Enzyme Information
| 2.3.1.12 |
Dihydrolipoyllysine-residue acetyltransferase.
based on mapping to UniProt P06959
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)
| P06959 |
ODP2_ECOLI
Escherichia coli K-12
Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
|
PDB Structure
| PDB | 2K7V |
| External Links | |
| Method | SOLUTION NMR |
| Organism | |
| Primary Citation |
A surface loop directs conformational switching of a lipoyl domain between a folded and a novel misfolded structure.
Structure
|
