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Literature summary for 4.2.1.17 extracted from
- Comparative inhibition studies of enoyl-CoA hydratase 1 and enoyl-CoA hydratase 2 in long-chain fatty acid oxidation (2008), Org. Lett., 10, 3355-3358.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expression of a His6-tagged truncated ECH2 mutant enzyme | Rattus norvegicus |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| (R)-methylenecyclopropylformyl-CoA | methylenecyclopropylformyl-CoA is a better inhibitor for enoyl-CoA hydratase 2 than for enoyl-CoA hydratase 1 | Rattus norvegicus |  |
| (S)-methylenecyclopropylformyl-CoA | methylenecyclopropylformyl-CoA is a better inhibitor for enoyl-CoA hydratase 2 than for enoyl-CoA hydratase 1 | Rattus norvegicus | |
| 3-octynoyl-CoA | irreversibly inactivates only enoyl-CoA hydratase 2, the catalytic residue Glu47 is covalently labeled by the inhibitor | Rattus norvegicus | |
| methylenecyclopropylformyl-CoA | a metabolite derived from a natural amino acid, (methylenecyclopropyl)glycine, that inactivates enoyl-CoA hydratase 1 and enoyl-CoA hydratase 2. Competence of (R)- and (S)-MCPF-CoA to inactivate the ECH2 and kinetic analysis, enzyme-inhibitor complex structures, mass spectrometric analysis, inhibition mechanism, overview | Rattus norvegicus | |
| additional information | 3-octynoyl-CoA is not an inhibitor of enoyl-CoA hydratase 1 | Rattus norvegicus |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| mitochondrion | - |
Rattus norvegicus | 5739 | - |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | Rattus norvegicus | In eukaryotes, ECH2 is a 31 kDa integral part of multifunctional protein-2, MFP-2, also called multifunctional enzyme 2, D-bifunctional enzyme, or 17-beta-estradiol dehydrogenase type IV. The MFP-2 plays a central role in peroxisomal beta-oxidation as it handles most peroxisomal beta-oxidation substrates | ? | - |
? | |
| additional information | Rattus norvegicus | the beta-oxidation in mitochondria involves a (3S)-hydroxyacyl-CoA intermediate, while the beta-oxidation in peroxisomes has a (3R)-hydroxyacyl-CoA intermediate. The enzymes responsible for the formation of these two different intermediates are enoyl-CoA hydratase 1 (ECH1) in mitochondria and enoyl-CoA hydratase 2 (ECH2) in peroxisomes | ? | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Rattus norvegicus | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant His6-tagged truncated ECH2 mutant enzyme | Rattus norvegicus |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 3-octynoyl-CoA + H2O | reaction of ECH1, ECH2 is inactivated by the compound, it is possible that 3-octynoyl-CoA is isomerized to reactive 2,3-octadienoyl-CoA, overview | Rattus norvegicus | 3-ketooctanoyl-CoA | - |
? | |
| additional information | In eukaryotes, ECH2 is a 31 kDa integral part of multifunctional protein-2, MFP-2, also called multifunctional enzyme 2, D-bifunctional enzyme, or 17-beta-estradiol dehydrogenase type IV. The MFP-2 plays a central role in peroxisomal beta-oxidation as it handles most peroxisomal beta-oxidation substrates | Rattus norvegicus | ? | - |
? | |
| additional information | the beta-oxidation in mitochondria involves a (3S)-hydroxyacyl-CoA intermediate, while the beta-oxidation in peroxisomes has a (3R)-hydroxyacyl-CoA intermediate. The enzymes responsible for the formation of these two different intermediates are enoyl-CoA hydratase 1 (ECH1) in mitochondria and enoyl-CoA hydratase 2 (ECH2) in peroxisomes | Rattus norvegicus | ? | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| hexamer | mitochondrial ECH1 that exists as a hexamer | Rattus norvegicus |
| homodimer | ECH2 exists as a homodimer in its crystal structure | Rattus norvegicus |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| ECH1 | - |
Rattus norvegicus |
| ECH2 | - |
Rattus norvegicus |
| enoyl-CoA hydratase 1 | - |
Rattus norvegicus |
| enoyl-CoA hydratase 2 | - |
Rattus norvegicus |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 25 | - |
assay at | Rattus norvegicus |
Ki Value [mM]
| Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.041 | - |
(R)-methylenecyclopropylformyl-CoA | 25°C, ECH2 | Rattus norvegicus | |
| 0.047 | - |
(R)-methylenecyclopropylformyl-CoA | 25°C, ECH1 | Rattus norvegicus | |
| 0.049 | - |
(R)-methylenecyclopropylformyl-CoA | 25°C, ECH1 | Rattus norvegicus | |
| 0.0492 | - |
(R)-methylenecyclopropylformyl-CoA | 25°C | Rattus norvegicus | |
| 0.053 | - |
(S)-methylenecyclopropylformyl-CoA | 25°C, ECH2 | Rattus norvegicus | |
| 0.0571 | - |
(S)-methylenecyclopropylformyl-CoA | 25°C | Rattus norvegicus | |
| 0.065 | - |
3-octynoyl-CoA | ECH2 | Rattus norvegicus | |
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