In silico screening of 393 mutants facilitates enzyme engineering of amidase activity in CalB

PeerJ. 2013 Aug 29:1:e145. doi: 10.7717/peerj.145. eCollection 2013.

Abstract

Our previously presented method for high throughput computational screening of mutant activity (Hediger et al., 2012) is benchmarked against experimentally measured amidase activity for 22 mutants of Candida antarctica lipase B (CalB). Using an appropriate cutoff criterion for the computed barriers, the qualitative activity of 15 out of 22 mutants is correctly predicted. The method identifies four of the six most active mutants with ≥3-fold wild type activity and seven out of the eight least active mutants with ≤0.5-fold wild type activity. The method is further used to screen all sterically possible (386) double-, triple- and quadruple-mutants constructed from the most active single mutants. Based on the benchmark test at least 20 new promising mutants are identified.

Keywords: Computational Chemistry; Enzyme Engineering.

Grants and funding

The work was funded by the EU through the In Silico Rational Engineering of Novel Enzymes (IRENE) project. The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript.