QSAR-assisted design of an environmental catalyst for enhanced estrogen remediation.

ABSTRACT: A quantitative structure-activity relationship (QSAR) was used to streamline re-design of a model environmental catalyst, horseradish peroxidase (HRP), for enhanced reactivity towards a target pollutant, steroid hormone 17β-estradiol. This QSAR, embodying relationship between reaction rate and intermolecular binding distance, was used in silico to screen for mutations improving enzyme reactivity. Eight mutations mediating significant reductions in binding distances were expressed in Saccharomyces cerevisiae, and resulting recombinant HRP strains were analyzed to determine Michaelis-Menten parameters during reaction with the target substrate. Enzyme turnover rate, ln(kCAT), exhibited inverse relationship with model-predicted binding distances (R2=0.81), consistent with the QSAR. Additional

SUBMITTER: Colosi LM 

PROVIDER: S-EPMC2952686 | biostudies-literature | 2010 Nov

REPOSITORIES: biostudies-literature