CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.90 | Alpha-Beta Complex |
|
3.90.226 | 2-enoyl-CoA Hydratase; Chain A, domain 1 |
|
3.90.226.10 | 2-enoyl-CoA Hydratase; Chain A, domain 1 |
Domain Context
CATH Clusters
| Superfamily | 2-enoyl-CoA Hydratase; Chain A, domain 1 |
| Functional Family | 3,2-trans-enoyl-CoA isomerase |
Enzyme Information
| 5.3.3.8 |
Delta(3)-Delta(2)-enoyl-CoA isomerase.
based on mapping to UniProt Q05871
(1) A (3Z)-alk-3-enoyl-CoA = a (2E)-alk-2-enoyl-CoA. (2) A (3E)-alk-3-enoyl-CoA = a (2E)-alk-2-enoyl-CoA.
-!- The enzyme participates in the beta-oxidation of fatty acids with double bonds at an odd position. -!- Processing of these substrates via the beta-oxidation system results in intermediates with a cis- or trans-double bond at position C(3), which cannot be processed further by the regular enzymes of the beta- oxidation system. -!- This enzyme isomerizes the bond to a trans bond at position C(2), which can be processed further. -!- The reaction rate is ten times higher for the (3Z) isomers than for (3E) isomers. -!- The enzyme can also catalyze the isomerization of 3-acetylenic fatty acyl thioesters to 2,3-dienoyl fatty acyl thioesters.
|
UniProtKB Entries (1)
| Q05871 |
ECI1_YEAST
Saccharomyces cerevisiae S288C
3,2-trans-enoyl-CoA isomerase
|
PDB Structure
| PDB | 1HNU |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
The crystal structure of delta(3)-delta(2)-enoyl-CoA isomerase.
J.Mol.Biol.
|
