Leveraging intrinsic flexibility to engineer enhanced enzyme catalytic activity | Proceedings of the National Academy of Sciences
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increased KYN hydrolysis activity using a genetic selection screen Protein flexibility has been recognized as a key contributor to enzyme evolution and catalytic activity However, it is unknown whether structural information regarding conformational flexibility can be exploited for directed evolutio
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- increased KYN hydrolysis activity using a genetic selection screen
- Protein flexibility has been recognized as a key contributor to enzyme evolution and catalytic activity
- However, it is unknown whether structural information regarding conformational flexibility can be exploited for directed evolution of enzymes with higher catalytic activity.
- Our results suggest that modulation of intrinsic flexibility through mutagenesis of remote flexible regions constitutes a promising strategy for directed enzyme evolution.
- Dynamic motions of enzymes occurring on a broad range of timescales play a pivotal role in all steps of the reaction pathway, including substrate binding, catalysis, and product release.
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