Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Woo, M.H.;Kim, H.S.; Lee, E.Y.
    Development and characterization of recombinant whole cells expressing the soluble epoxide hydrolase of Danio rerio and its variant for enantioselective resolution of racemic styrene oxides (2012), J. Ind. Eng. Chem., 18, 384-391 .
No PubMed abstract available

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.3.2.10 gene ephx1, sequence comparisons Danio rerio

Protein Variants

EC Number Protein Variants Comment Organism
3.3.2.10 E88R/T102A/M368I/K398E/G412D site-directed mutagenesis, the enantiomeric ratio of the mutant sEH is 1.43fold higher than that of the wild-type sEH, and the maximum hydrolysis rates of the variant sEH for (S)-isomer are 1.2fold higher than that of the wild-type sEH. Based on the multiple sequence alignment and comparative homology modeling, both of the wild-type and mutant sEH have a similar topology with the structurally known human sEH, and are expected to have enantioselective hydrolytic activity to racemic epoxide substrate. The wild-type catalytic activity is lower than the mutant sEH, the yield (25.1%) is low and the time required to reach 99% increases up to 180 min at 10°C, indicating that the mutant Danio rerio sEH is better biocatalyst than the wild-type one Danio rerio

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.3.2.10 phenyl-1,2-ethanediol product inhibition, 50% inhibition at 50 mM Danio rerio

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.3.2.10 (S)-styrene oxide + H2O Danio rerio
-
 (S)-styrene glycol
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.3.2.10 Danio rerio Q7ZVB4
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.3.2.10 (S)-styrene oxide + H2O
-
 Danio rerio (S)-styrene glycol
-
 ?
3.3.2.10 (S)-styrene oxide + H2O wild-type and mutant enzymes prefer the S-enantiomer, enantioselective hydrolytic activity of sEH Danio rerio (S)-phenyl-1,2-ethanediol
-
 ?
3.3.2.10 additional information degradation kinetics of styrene oxide, overview. At 10°C, the enantiopurity of (R)-styrene oxide reaches 99% with 34.8% yield and 80 min reaction time. On the contrary, a 20.5% yield is obtained at 40°C. At 50°C, the enantiopurity more than 98% cannot be obtained for 30 min-reaction. As a conclusion, the yield increased 1.7fold at 10°C, compared to 30°C Danio rerio ?
-
 ?

Subunits

EC Number Subunits Comment Organism
3.3.2.10 ? x * 64800, recombinant His-tagged enzyme, SDS-PAGE Danio rerio

Synonyms

EC Number Synonyms Comment Organism
3.3.2.10 SEH
-
 Danio rerio

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.3.2.10 additional information
-
 the enantioselective resolution at low temperature, 10°C, shows the highest yield Danio rerio
3.3.2.10 30
-
 assay at Danio rerio

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.3.2.10 6
-
 assay at Danio rerio

General Information

EC Number General Information Comment Organism
3.3.2.10 evolution the structure of sEH from Danio rerio is compared to sEHs from mammalia, most of EHs possess the catalytic triad consisting of an acidic nucleophile and a basic charge relay system, two tyrosine residues in the cap domain and the characteristic oxyanion hole are also highly conserved Danio rerio
3.3.2.10 additional information catalytically important and highly conserved amino acids are Asp331, Tyr379, Tyr460, Asp496 and His524. Proposed active site of Danio rerio sEH based on homology structural modelling Danio rerio