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Literature summary extracted from

  • Haataja, T.J.; Koski, M.K.; Hiltunen, J.K.; Glumoff, T.
    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.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
4.2.1.119 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)

EC Number Crystallization (Comment) Organism
4.2.1.119 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]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
4.2.1.119 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
4.2.1.119 0.00114
-
 (2E)-decenoyl-CoA pH 7.5, 22°C, recombinant full-length enzyme Drosophila melanogaster
4.2.1.119 0.0667
-
 (2E)-hexenoyl-CoA pH 7.5, 22°C, recombinant full-length enzyme Drosophila melanogaster
4.2.1.119 0.0853
-
 (2E)-butenoyl-CoA pH 7.5, 22°C, recombinant full-length enzyme Drosophila melanogaster

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
4.2.1.119 peroxisome
-
 Drosophila melanogaster 5777
-

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
4.2.1.119 64100
-
 2 * 64100, MFE-2, SDS-PAGE Drosophila melanogaster

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
4.2.1.119 (2E)-enoyl-CoA + H2O Drosophila melanogaster
-
 (3R)-hydroxyacyl-CoA
-
 ?
4.2.1.119 additional information Drosophila melanogaster the bifunctional peroxisomal multifunctional enzyme type 2 exhibits dehydrogenase and hydratase activity from separate entities ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
4.2.1.119 Drosophila melanogaster
-
 gene CG3415
-

Purification (Commentary)

EC Number Purification (Comment) Organism
4.2.1.119 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

EC Number Source Tissue Comment Organism Textmining

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.2.1.119 (2E)-butenoyl-CoA + H2O
-
 Drosophila melanogaster (3R)-hydroxybutanoyl-CoA
-
 ?
4.2.1.119 (2E)-decenoyl-CoA + H2O
-
 Drosophila melanogaster (3R)-3-hydroxydecanoyl-CoA
-
 ?
4.2.1.119 (2E)-enoyl-CoA + H2O
-
 Drosophila melanogaster (3R)-hydroxyacyl-CoA
-
 ?
4.2.1.119 (2E)-hexenoyl-CoA + H2O
-
 Drosophila melanogaster (3R)-3-hydroxyhexanoyl-CoA
-
 ?
4.2.1.119 additional information the bifunctional peroxisomal multifunctional enzyme type 2 exhibits dehydrogenase and hydratase activity from separate entities Drosophila melanogaster ?
-
 ?
4.2.1.119 additional information MFE-2 structure-function studies, overview Drosophila melanogaster ?
-
 ?

Subunits

EC Number Subunits Comment Organism
4.2.1.119 dimer 2 * 64100, MFE-2, SDS-PAGE Drosophila melanogaster
4.2.1.119 More necessity of dimerization, domain organization, MFE-2 structure-function studies, overview Drosophila melanogaster

Synonyms

EC Number Synonyms Comment Organism
4.2.1.119 2E-enoyl-CoA hydratase 2
-
 Drosophila melanogaster
4.2.1.119 MFE-2
-
 Drosophila melanogaster

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
4.2.1.119 22
-
 assay at room temperature Drosophila melanogaster

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
4.2.1.119 0.38
-
 (2E)-butenoyl-CoA pH 7.5, 22°C, recombinant full-length enzyme Drosophila melanogaster
4.2.1.119 210
-
 (2E)-hexenoyl-CoA pH 7.5, 22°C, recombinant full-length enzyme Drosophila melanogaster
4.2.1.119 1100
-
 (2E)-decenoyl-CoA pH 7.5, 22°C, recombinant full-length enzyme Drosophila melanogaster

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
4.2.1.119 7.5
-
 assay at Drosophila melanogaster

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
4.2.1.119 0.00000446
-
 (2E)-butenoyl-CoA pH 7.5, 22°C, recombinant full-length enzyme Drosophila melanogaster
4.2.1.119 0.0032
-
 (2E)-hexenoyl-CoA pH 7.5, 22°C, recombinant full-length enzyme Drosophila melanogaster
4.2.1.119 0.97
-
 (2E)-decenoyl-CoA pH 7.5, 22°C, recombinant full-length enzyme Drosophila melanogaster