Journal
JOURNAL OF CHEMICAL INFORMATION AND MODELING
Volume -, Issue -, Pages -Publisher
AMER CHEMICAL SOC
DOI: 10.1021/acs.jcim.2c01337
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Funding
- FCT/MCTES through national funds [UIBD/50006/2020]
- FCT [PTDC/QUI-QFI/28714/2017]
- FCT (Fundacao para a Ciencia e Tecnologia) [2021.00391.CEECIND/CP1662/CT0003]
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Here we present an approach to identify enzyme mutants with increased turnover by recalculating barriers and analyzing charge interactions.
We describe an approach to identify enzyme mutants with increased turnover using the enzyme DszC as a case study. Our approach is based on recalculating the barriers of alanine mutants through single-point energy calculations at the hybrid QM/MM level in the wild-type reactant and transition state geometries. We analyze the difference in the electron density between the reactant and transition state to identify sites/residues where electrostatic interactions stabilize the transition state over the reactants. We also assess the insertion of a unit probe charge to identify positions in which the introduction of charged residues lowers the barrier.
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