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Literature summary for 4.2.1.119 extracted from
- Peroxisomal multifunctional enzyme type 2 from the fruitfly: dehydrogenase and hydratase act as separate entities, as revealed by structure and kinetics (2011), Biochem. J., 435, 771-781.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| gene CG3415, Drosophila melanogaster MFE-2 complements a Saccharomyces cerevisiae MFE-2 deletion strain, functional expression of His-tagged MFE-2 in Escherichia coli strain BL21(DE3) pLysS | Drosophila melanogaster |
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| purified recombinant detagged MFE-2, 5 mg/ml protein in 0.1 Msodium phosphate, pH 7.2, and 0.2 M NaF, sitting and hanging drop vapour diffusion methods are used at 21°C, mixing of equal volumes of protein and reservoir solutions, the latter contains 100 mM Tris-HCl, pH 8.0, 1.0 M NaCl, 20% w/v PEG 5000 MME and 5 mM NAD+, X-ray diffraction structure determination and analysis at 2.15 A resolution | Drosophila melanogaster |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | kinetics using the DmDH and DmH2 domains of DmMFE-2 as separate monofunctional enzymes at a 1:1 ratio, overview | Drosophila melanogaster | |
| 0.00114 | - |
(2E)-decenoyl-CoA | pH 7.5, 22°C, recombinant full-length enzyme | Drosophila melanogaster |  |
| 0.0667 | - |
(2E)-hexenoyl-CoA | pH 7.5, 22°C, recombinant full-length enzyme | Drosophila melanogaster | |
| 0.0853 | - |
(2E)-butenoyl-CoA | pH 7.5, 22°C, recombinant full-length enzyme | Drosophila melanogaster | |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| peroxisome | - |
Drosophila melanogaster | 5777 | - |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 64100 | - |
2 * 64100, MFE-2, SDS-PAGE | Drosophila melanogaster |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| (2E)-enoyl-CoA + H2O | Drosophila melanogaster | - |
(3R)-hydroxyacyl-CoA | - |
? | |
| additional information | Drosophila melanogaster | the bifunctional peroxisomal multifunctional enzyme type 2 exhibits dehydrogenase and hydratase activity from separate entities | ? | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Drosophila melanogaster | - |
gene CG3415 | - |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant His-tagged MFE-2 from Escherichia coli strain BL21(DE3) pLysS by nickel affinity chromatography, removal of the His tag | Drosophila melanogaster |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| (2E)-butenoyl-CoA + H2O | - |
Drosophila melanogaster | (3R)-hydroxybutanoyl-CoA | - |
? | |
| (2E)-decenoyl-CoA + H2O | - |
Drosophila melanogaster | (3R)-3-hydroxydecanoyl-CoA | - |
? | |
| (2E)-enoyl-CoA + H2O | - |
Drosophila melanogaster | (3R)-hydroxyacyl-CoA | - |
? | |
| (2E)-hexenoyl-CoA + H2O | - |
Drosophila melanogaster | (3R)-3-hydroxyhexanoyl-CoA | - |
? | |
| additional information | the bifunctional peroxisomal multifunctional enzyme type 2 exhibits dehydrogenase and hydratase activity from separate entities | Drosophila melanogaster | ? | - |
? | |
| additional information | MFE-2 structure-function studies, overview | Drosophila melanogaster | ? | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| dimer | 2 * 64100, MFE-2, SDS-PAGE | Drosophila melanogaster |
| More | necessity of dimerization, domain organization, MFE-2 structure-function studies, overview | Drosophila melanogaster |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| 2E-enoyl-CoA hydratase 2 | - |
Drosophila melanogaster |
| MFE-2 | - |
Drosophila melanogaster |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 22 | - |
assay at room temperature | Drosophila melanogaster |
Turnover Number [1/s]
| Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.38 | - |
(2E)-butenoyl-CoA | pH 7.5, 22°C, recombinant full-length enzyme | Drosophila melanogaster | |
| 210 | - |
(2E)-hexenoyl-CoA | pH 7.5, 22°C, recombinant full-length enzyme | Drosophila melanogaster | |
| 1100 | - |
(2E)-decenoyl-CoA | pH 7.5, 22°C, recombinant full-length enzyme | Drosophila melanogaster | |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.5 | - |
assay at | Drosophila melanogaster |
kcat/KM [mM/s]
| kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.00000446 | - |
(2E)-butenoyl-CoA | pH 7.5, 22°C, recombinant full-length enzyme | Drosophila melanogaster | |
| 0.0032 | - |
(2E)-hexenoyl-CoA | pH 7.5, 22°C, recombinant full-length enzyme | Drosophila melanogaster | |
| 0.97 | - |
(2E)-decenoyl-CoA | pH 7.5, 22°C, recombinant full-length enzyme | Drosophila melanogaster | |
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