These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


Pubmed for Handhelds

PUBMED FOR HANDHELDS

Search MEDLINE/PubMed

  • Title: Modification of substrate specificity resulting in an epoxide hydrolase with shifted enantiopreference for (2,3-epoxypropyl)benzene.
    Author: Gurell A, Widersten M.
    Journal: Chembiochem; 2010 Jul 05; 11(10):1422-9. PubMed ID: 20544772.
    Abstract:
    Random mutagenesis targeted at hotspots of noncatalytic active-site residues of potato epoxide hydrolase StEH1 combined with an enzyme-activity screen allowed the isolation of enzyme variants displaying altered enantiopreference in the catalyzed hydrolysis of (2,3-epoxypropyl)benzene. The wild-type enzyme favored the S enantiomer with a ratio of 2.5:1, whereas the variant displaying the most radical functional changes showed a 15:1 preference for the R enantiomer. This mutant had accumulated four substitutions distributed over two out of four mutated hotspots: W106L, L109Y, V141K, and I151V. The underlying causes of the enantioselectivity were a decreased catalytic efficiency in the catalyzed hydrolysis of the S enantiomer combined with retained activity with the R enantiomer. The results demonstrate the feasibility of molding the stereoselectivity of this biocatalytically relevant enzyme.
    [Abstract] [Full Text] [Related] [New Search]