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- W3216571205 endingPage "2100441" @default.
- W3216571205 startingPage "2100441" @default.
- W3216571205 abstract "Carboxylic acid reductases (CARs) represent useful tools for the production of aldehydes from ubiquitous organic carboxylic acids. However, the low catalytic efficiency of these enzymes hampers their application.Herein, a CAR originating from Mycobacterium smegmatis was redesigned through rational hinge engineering to enhance the catalytic efficiency.Based on the unique domain architecture of CARs and their superfamily, a mutagenesis library of the hinge region was designed. The best mutant R505I/N506K showed a 6.57-fold improved catalytic efficiency. Molecular dynamics simulations showed the increased catalytic efficiency was due to the strong binding of the acyl-AMP complex with it. Meanwhile, the ε-nitrogen atom of Lys610 frequently interacted with the ribose-ring oxygen atom of the complex, the distance (d1) between them represents a great indicator for that. The d1 value was used as a nimble indicator to evaluate unexplored mutants of that region for enhanced activity by in silico mutational experiments. Overall, eight mutants were identified to show higher enhanced activity compared with wild-type enzyme and R505F/N506G showed the highest catalytic efficiency.Altogether, the two-step strategy used here provided useful references for the engineering of CARs and other similar multiple-domain enzymes." @default.
- W3216571205 created "2021-12-06" @default.
- W3216571205 creator A5007145637 @default.
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- W3216571205 creator A5054031995 @default.
- W3216571205 creator A5076356372 @default.
- W3216571205 date "2021-12-15" @default.
- W3216571205 modified "2023-09-27" @default.
- W3216571205 title "Rational hinge engineering of carboxylic acid reductase from <i>Mycobacterium smegmatis</i> enhances its catalytic efficiency in biocatalysis" @default.
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- W3216571205 doi "https://doi.org/10.1002/biot.202100441" @default.
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