EC Number   |
Natural Substrates |
|---|
   4.2.1.119 | (2E)-2-enoyl-CoA + H2O |
- |
| 4.2.1.119 | (2E)-2-enoyl-CoA + H2O |
2-enoyl-CoA hydratase 2 is a part of multifunctional enzyme type 2, hydrates trans-2-enoyl-CoA to 3-hydroxyacyl-CoA as a key enzyme in the (3R)-hydroxy-dependent route of peroxisomal beta-oxidation of fatty acids |
| 4.2.1.119 | (2E)-2-enoyl-CoA + H2O |
peroxisomal multifunctional enzyme type 2 (MFE-2) is a 79000 Da enzyme composed of three functional units: (3R)-hydroxyacyl-CoA dehydrogenase, 2-enoyl-CoA hydratase 2 and sterol carrier protein 2-like units. It catalyzes the second and third steps of peroxisomal beta-oxidation, and its importance in human lipid metabolism is shown by the severe clinical symptoms (dysmorphic features, such as macrocephaly and large fontanelles, hypotonia, seizures, etc.) in patients having defects in the gene encoding MFE-2. Typical biochemical observations include a high ratio of C26:0 to C22:0 fatty acids and elevated levels of pristanic acid (2,6,10,14-tetramethylpentadecanoic acid) in the patients plasma and fibroblasts, indicating the significance of MFE-2 in the breakdown of very-long-chain and alpha-methylbranched-chain fatty acids. The patients also have high levels of di- and trihydroxycholestanoic acids, which are precursors of bile acids, showing that MFE-2 also participates in bile acid synthesis |
| 4.2.1.119 | (2E)-enoyl-CoA + H2O |
- |
| 4.2.1.119 | (3R)-3-hydroxyacyl-CoA |
- |
| 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 |
| 4.2.1.119 | (3R)-3-hydroxyacyl-CoA |
a peroxisomal beta-oxidation intermediate |
| 4.2.1.119 | (3R)-3-hydroxydecanoyl-CoA |
- |
| 4.2.1.119 | more |
channelling pathway for supplying (R)-3-hydroxyacyl-CoA monomer units from fatty acid beta-oxidation to poly(3-hydroxybutyrate-co-3-hydroxyhexanoate) biosynthesis |
| 4.2.1.119 | more |
domains A and B have different enzymatic properties and both domains play a functional role in the beta-oxidation of fatty acids in yeast peroxisomes |
