EC Number   |
Substrates |
Organism |
Products  |
Reversibility |
|---|
   4.2.1.119 | (24E)-3alpha,7alpha,12alpha-trihydroxy-5beta-cholest-24-enoyl-CoA + H2O |
reaction of the recombinant enzyme, protein converted rapidly |
Rattus norvegicus |
(24R,25R)-3alpha,7alpha,12alpha,24-tetrahydroxy-5beta-cholestanoyl-CoA |
a physiological intermediate in bile acid synthesis |
? |
| 4.2.1.119 | (3R)-3-hydroxydecanoyl-CoA |
- |
Rattus norvegicus |
(2E)-2-decenoyl-CoA + H2O |
- |
r |
| 4.2.1.119 | (3R)-3-hydroxydecanoyl-CoA |
- |
Pseudomonas aeruginosa |
(2E)-2-decenoyl-CoA + H2O |
- |
? |
| 4.2.1.119 | (3R)-3-hydroxyacyl-CoA |
- |
Rattus norvegicus |
(2E)-2-enoyl-CoA + H2O |
- |
? |
| 4.2.1.119 | (3R)-3-hydroxyacyl-CoA |
- |
Pseudomonas aeruginosa |
(2E)-2-enoyl-CoA + H2O |
- |
? |
| 4.2.1.119 | (3R)-3-hydroxyacyl-CoA |
- |
Cupriavidus necator |
(2E)-2-enoyl-CoA + H2O |
- |
? |
| 4.2.1.119 | (3R)-3-hydroxyacyl-CoA |
AtECH2 participates in vivo in the conversion of the intermediate (3R)-hydroxyacyl-CoA, generated by the metabolism of fatty acids with a cis (Z)-unsaturated bond on an even-numbered carbon, to the (2E)-enoyl-CoA for further degradation through the core beta-oxidation cycle. AtECH2 is a monofunctional enzyme in Arabidopsis thaliana that is devoid of 3-hydroxyacyl-CoA dehydrogenase activity |
Arabidopsis thaliana |
(2E)-2-enoyl-CoA + H2O |
- |
? |
| 4.2.1.119 | (3R)-3-hydroxyacyl-CoA |
a peroxisomal beta-oxidation intermediate |
Rattus norvegicus |
(2E)-2-enoyl-CoA + H2O |
- |
? |
| 4.2.1.119 | (3R)-3-hydroxyacyl-CoA |
recombinant forms of the three proteins, PhaJ4aRe to PhaJ4cRe, show enoyl-CoA hydratase activity with R specificity, and the catalytic efficiencies are elevated as the substrate chain length increases from C4 to C8. PhaJ4aRe and PhaJ4bRe show over 10fold higher catalytic efficiency than PhaJ4cRe |
Cupriavidus necator |
(2E)-2-enoyl-CoA + H2O |
- |
? |
| 4.2.1.119 | (3R)-3-hydroxyacyl-CoA |
- |
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1 |
(2E)-2-enoyl-CoA + H2O |
- |
? |
