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Literature summary for 4.2.1.119 extracted from

  • Qin, Y.M.; Haapalainen, A.M.; Kilpelainen, S.H.; Marttila, M.S.; Koski, M.K.; Glumoff, T.; Novikov, D.K.; Hiltunen, J.K.
    Human peroxisomal multifunctional enzyme type 2: site-directed mutagenesis studies show the importance of two protic residues for 2-enoyl-CoA hydratase 2 activity (2000), J. Biol. Chem., 275, 4965-4972.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
wild type (HsMFE-2) and its variants are expressed in Saccharomyces cerevisiae, the recombinant HsMFE-2(dhdelta) and its variants are expressed in Escherichia coli BL21(DE3)pLysS Homo sapiens

Protein Variants

Protein Variants Comment Organism
D370A reduced specific acitivity of 2-enoyl-CoA hydratase 2 when expressed in Saccharomyces cerevisiae Homo sapiens
D490A reduced specific acitivity of 2-enoyl-CoA hydratase 2 when expressed in Saccharomyces cerevisiae Homo sapiens
D510A inactive mutant enzyme Homo sapiens
D517A reduced specific acitivity of 2-enoyl-CoA hydratase 2 when expressed in Saccharomyces cerevisiae Homo sapiens
E366A kcat/Km 100times lower than that of the wild type Homo sapiens
E408A reduced specific acitivity of 2-enoyl-CoA hydratase 2 when expressed in Saccharomyces cerevisiae Homo sapiens
G16S reduced specific acitivity of 2-enoyl-CoA hydratase 2 when expressed in Saccharomyces cerevisiae Homo sapiens
H406A reduced specific acitivity of 2-enoyl-CoA hydratase 2 when expressed in Saccharomyces cerevisiae Homo sapiens
H515A inactive mutant enzyme Homo sapiens
H532A reduced specific acitivity of 2-enoyl-CoA hydratase 2 when expressed in Saccharomyces cerevisiae Homo sapiens
additional information mutant constructs are tested for complementation in Saccharomyces cerevisiae Homo sapiens
Y347A inactive mutant enzyme Homo sapiens
Y410A reduced specific acitivity of 2-enoyl-CoA hydratase 2 when expressed in Saccharomyces cerevisiae Homo sapiens
Y505A inactive mutant enzyme Homo sapiens

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0081
-
(2E)-2-decenoyl-CoA wild type, pH 8 Homo sapiens
0.0089
-
(2E)-2-decenoyl-CoA wild type, pH 5 Homo sapiens
0.0092
-
(2E)-2-decenoyl-CoA mutant enzyme E366A, pH 5 Homo sapiens
0.0131
-
(2E)-2-decenoyl-CoA mutant enzyme E366A, pH 8 Homo sapiens

Localization

Localization Comment Organism GeneOntology No. Textmining
peroxisome peroxisomal hydratase 2 together with (3R)-hydroxyacyl-CoA dehydrogenase, and hydratase 1 together with (3S)-hydroxyacyl-CoA dehydrogenase, are present as multifunctional enzymes. When present simultaneously in peroxisomes, beta-oxidation has two stereochemical possibilities Homo sapiens 5777
-

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
45000
-
x * 45000, HsMFE-2(dhdelta), HsMFE-2(dhdelta, E366A), HsMFE-2(dhdelta, D510A), SDS-PAGE Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Homo sapiens peroxisomal hydratase 2 together with (3R)-hydroxyacyl-CoA dehydrogenase, and peroxisomal hydratase 1 together with (3S)-hydroxyacyl-CoA dehydrogenase, are present as multifunctional enzymes. When present simultaneously in peroxisomes, beta-oxidation has two stereochemical possibilities ?
-
?

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Homo sapiens

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.12
-
strain HsMFE-2(D490A) Homo sapiens
0.16
-
strain HsMFE-2(G16S) Homo sapiens
0.2
-
strain HsMFE-2(H532A) Homo sapiens
0.21
-
strain HsMFE-2(D370A), strain HsMFE-2(H406A) Homo sapiens
0.24
-
strain HsMFE-2(Y410A) Homo sapiens
0.26
-
strain HsMFE-2(D517A), strain HsMFE-2(E408A) Homo sapiens
0.4
-
strain UTL-7A Homo sapiens
0.54
-
strain HsMFE-2 Homo sapiens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information peroxisomal hydratase 2 together with (3R)-hydroxyacyl-CoA dehydrogenase, and peroxisomal hydratase 1 together with (3S)-hydroxyacyl-CoA dehydrogenase, are present as multifunctional enzymes. When present simultaneously in peroxisomes, beta-oxidation has two stereochemical possibilities Homo sapiens ?
-
?
trans-2-decenoyl-CoA + H2O
-
Homo sapiens (3R)-3-hydroxydecanoyl-CoA
-
r

Subunits

Subunits Comment Organism
? x * 45000, HsMFE-2(dhdelta), HsMFE-2(dhdelta, E366A), HsMFE-2(dhdelta, D510A), SDS-PAGE Homo sapiens

Synonyms

Synonyms Comment Organism
2-enoyl-CoA hydratase 2
-
Homo sapiens
2-enoyl-CoA hydratase 2 domain in human MFE-2 Homo sapiens
MFE-2 peroxisomal hydratase 2 together with (3R)-hydroxyacyl-CoA dehydrogenase is present as multifunctional enzyme Homo sapiens

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
22
-
assay at Homo sapiens

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.3
-
(2E)-2-decenoyl-CoA mutant enzyme E366A, pH 5 Homo sapiens
17.9
-
(2E)-2-decenoyl-CoA mutant enzyme E366A, pH 8 Homo sapiens
105
-
(2E)-2-decenoyl-CoA wild type enzyme, pH 5 Homo sapiens
196
-
(2E)-2-decenoyl-CoA wild type enzyme, pH 8 Homo sapiens

pH Range

pH Minimum pH Maximum Comment Organism
5 10 pH dependence experiment is performed in 200 mM potassium phosphate buffer at pH values varying from 5 to 10 Homo sapiens