CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
1 | Mainly Alpha |
|
1.20 | Up-down Bundle |
|
1.20.1270 | Substrate Binding Domain Of Dnak; Chain:A; Domain 2 |
|
1.20.1270.370 |
Domain Context
CATH Clusters
| Superfamily | 1.20.1270.370 |
| Functional Family |
Enzyme Information
| 4.2.1.157 |
(R)-2-hydroxyisocaproyl-CoA dehydratase.
based on mapping to UniProt Q5U923
(R)-2-hydroxy-4-methylpentanoyl-CoA = 4-methylpent-2-enoyl-CoA + H(2)O.
-!- The enzyme, isolated from the bacterium Peptoclostridium difficile, is involved in the reductive branch of L-leucine fermentation. -!- It catalyzes an alpha/beta-dehydration, which depends on the reductive formation of ketyl radicals on the substrate generated by injection of a single electron from the ATP-dependent activator protein HadI.
|
UniProtKB Entries (1)
| Q5U923 |
HADC_CLODI
Clostridioides difficile
(R)-2-hydroxyisocaproyl-CoA dehydratase beta subunit
|
PDB Structure
| PDB | 3O3N |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Structural Basis for Reductive Radical Formation and Electron Recycling in (R)-2-Hydroxyisocaproyl-CoA Dehydratase.
J.Am.Chem.Soc.
|
