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Literature summary extracted from

  • Arand, M.; Hemmer, H.; Duerk, H.; Barattis, J.; Archelas, A.; Furstoss, R.
    Cloning and molecular characterization of a soluble epoxide hydrolase from Aspergillus niger that is related to mammalian microsomal epoxide hydrolase (1999), Biochem. J., 344, 273-280.
No PubMed abstract available

Application

EC Number Application Comment Organism
3.3.2.10 synthesis the enzyme is useful for enantioselective bio-organic synthesis of chiral substances Aspergillus niger

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.3.2.10 DNA and amino acid sequence determination and analysis, phylogenetic tree, sequence comparisons, functional expression of wild-type enzyme and expression of enzyme mutants in Escherichia coli strain BL21(DE3) Aspergillus niger

Protein Variants

EC Number Protein Variants Comment Organism
3.3.2.10 D192A site directed mutagenesis, inactive or nearly inactive mutant Aspergillus niger
3.3.2.10 D192N site directed mutagenesis, inactive or nearly inactive mutant Aspergillus niger
3.3.2.10 D192S site directed mutagenesis, inactive or nearly inactive mutant Aspergillus niger
3.3.2.10 D348A site directed mutagenesis, inactive or nearly inactive mutant Aspergillus niger
3.3.2.10 D348E site directed mutagenesis, the mutant shows 48% of wild-type enzyme activity Aspergillus niger
3.3.2.10 H374K site directed mutagenesis, inactive or nearly inactive mutant Aspergillus niger
3.3.2.10 H374N site directed mutagenesis, inactive or nearly inactive mutant Aspergillus niger
3.3.2.10 H374S site directed mutagenesis, inactive or nearly inactive mutant, recombinantly expressed mutant enzyme is not soluble but remains in the particulate fraction of Escherichia coli cells Aspergillus niger

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.3.2.10 soluble the enzyme has no N-terminal membrane anchor in contrast to the microsomal epoxide hydrolase, 3.3.2.9 Aspergillus niger
-
-

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.3.2.10 100000
-
 recombinant enzyme, gel filtration Aspergillus niger

Organism

EC Number Organism UniProt Comment Textmining
3.3.2.10 Aspergillus niger Q9UR30
-
-
3.3.2.10 Aspergillus niger LCP521 Q9UR30
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.3.2.10 recombinant enzyme from Escherichia coli strain BL21(DE3) to homogeneity by ammonium sulfate fractionation, anion exchange and hydrophobic interaction chromatography, and gel filtration Aspergillus niger

Reaction

EC Number Reaction Comment Organism Reaction ID
3.3.2.10 an epoxide + H2O = a glycol the catalytic triad is formed by Asp192, Asp348, and His374 Aspergillus niger
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.3.2.10 (R)-4-nitrostyrene oxide + H2O
-
 Aspergillus niger ?
-
 ?
3.3.2.10 (R)-4-nitrostyrene oxide + H2O
-
 Aspergillus niger LCP521 ?
-
 ?

Subunits

EC Number Subunits Comment Organism
3.3.2.10 More the enzyme has no N-terminal membrane anchor in contrast to the microsomal epoxide hydrolase, EC 3.3.2.9 Aspergillus niger

Synonyms

EC Number Synonyms Comment Organism
3.3.2.10 EH
-
 Aspergillus niger

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.3.2.10 37
-
 assay at Aspergillus niger

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.3.2.10 7.4
-
 assay at Aspergillus niger