CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.40 | 3-Layer(aba) Sandwich |
|
3.40.50 | Rossmann fold |
|
3.40.50.1220 | TPP-binding domain |
Domain Context
CATH Clusters
| Superfamily | TPP-binding domain |
| Functional Family | Pyruvate decarboxylase isozyme |
Enzyme Information
| 4.1.1.74 |
Indolepyruvate decarboxylase.
based on mapping to UniProt P06169
3-(indol-3-yl)pyruvate = 2-(indol-3-yl)acetaldehyde + CO(2).
-!- More specific than EC 4.1.1.1.
|
| 4.1.1.- |
Carboxy-lyases.
based on mapping to UniProt P06169
|
| 4.1.1.72 |
Branched-chain-2-oxoacid decarboxylase.
based on mapping to UniProt P06169
(3S)-3-methyl-2-oxopentanoate = 2-methylbutanal + CO(2).
-!- Acts on a number of 2-oxo acids, with a high affinity toward branched-chain substrates. -!- The aldehyde formed may be enzyme-bound, and may be an intermediate in the bacterial system for biosynthesis of branched-chain fatty acids.
|
| 4.1.1.43 |
Phenylpyruvate decarboxylase.
based on mapping to UniProt P06169
Phenylpyruvate = phenylacetaldehyde + CO(2).
-!- Also acts on (indol-3-yl)pyruvate.
|
UniProtKB Entries (1)
| P06169 |
PDC1_YEAST
Saccharomyces cerevisiae S288C
Pyruvate decarboxylase isozyme 1
|
PDB Structure
| PDB | 2VK8 |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Covalently Bound Substrate at the Regulatory Site of Yeast Pyruvate Decarboxylases Triggers Allosteric Enzyme Activation.
J.Biol.Chem.
|
