CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.30 | 2-Layer Sandwich |
|
3.30.559 | Chloramphenicol Acetyltransferase |
|
3.30.559.10 | Chloramphenicol acetyltransferase-like domain |
Domain Context
CATH Clusters
| Superfamily | Chloramphenicol acetyltransferase-like domain |
| Functional Family | Acetyltransferase component of pyruvate dehydrogenase complex |
Enzyme Information
| 2.3.1.12 |
Dihydrolipoyllysine-residue acetyltransferase.
based on mapping to UniProt P10802
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)
| P10802 |
ODP2_AZOVI
Azotobacter vinelandii
Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
|
PDB Structure
| PDB | 1DPC |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Crystallographic and enzymatic investigations on the role of Ser558, His610, and Asn614 in the catalytic mechanism of Azotobacter vinelandii dihydrolipoamide acetyltransferase (E2p).
Biochemistry
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