Cloned (Comment) | Organism |
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expression in Escherichia coli BL21(DE3) | Homo sapiens |
Crystallization (Comment) | Organism |
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hanging-drop vapor diffusion method, crystal structure to 3 A resolution. MFE-2 has a two-domain subunit structure with a C-domain complete hot-dog fold housing the active site, and an N-domain incomplete hot-dog fold housing the cavity for the aliphatic acyl part of the substrate molecule. The ability of human hydratase 2 to utilize such bulky compounds which are not physiological substrates for the fungal ortholog, e.g. CoA esters of C26 fatty acids, pristanic acid and di/trihydroxycholestanoic acids, is explained by a large hydrophobic cavity formed upon the movements of the extremely mobile loops IIII in the N-domain. In the unliganded form of human hydratase 2, however, the loop I blocks the entrance of fatty enoyl-CoAs with chain-length above C8 | Homo sapiens |
Localization | Comment | Organism | GeneOntology No. | Textmining |
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Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
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(2E)-2-enoyl-CoA + H2O | Homo sapiens | 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 | (3R)-3-hydroxyacyl-CoA | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | P51659 | 2-enoyl-CoA hydratase 2 is the middle part of the mammalian peroxisomal multifunctional enzyme type 2 (MFE-2) | - |
Purification (Comment) | Organism |
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- |
Homo sapiens |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
(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 | Homo sapiens | (3R)-3-hydroxyacyl-CoA | - |
? |
Synonyms | Comment | Organism |
---|---|---|
2-enoyl-CoA hydratase 2 | the enzyme is the middle part of the mammalian peroxisomal multifunctional enzyme type 2 (MFE-2) | Homo sapiens |