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      Biocatalysis with Unnatural Amino Acids: Enzymology Meets Xenobiology

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          Adding new chemistries to the genetic code.

          The development of new orthogonal aminoacyl-tRNA synthetase/tRNA pairs has led to the addition of approximately 70 unnatural amino acids (UAAs) to the genetic codes of Escherichia coli, yeast, and mammalian cells. These UAAs represent a wide range of structures and functions not found in the canonical 20 amino acids and thus provide new opportunities to generate proteins with enhanced or novel properties and probes of protein structure and function.
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            Electrostatic basis for enzyme catalysis.

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              Kemp elimination catalysts by computational enzyme design.

              The design of new enzymes for reactions not catalysed by naturally occurring biocatalysts is a challenge for protein engineering and is a critical test of our understanding of enzyme catalysis. Here we describe the computational design of eight enzymes that use two different catalytic motifs to catalyse the Kemp elimination-a model reaction for proton transfer from carbon-with measured rate enhancements of up to 10(5) and multiple turnovers. Mutational analysis confirms that catalysis depends on the computationally designed active sites, and a high-resolution crystal structure suggests that the designs have close to atomic accuracy. Application of in vitro evolution to enhance the computational designs produced a >200-fold increase in k(cat)/K(m) (k(cat)/K(m) of 2,600 M(-1)s(-1) and k(cat)/k(uncat) of >10(6)). These results demonstrate the power of combining computational protein design with directed evolution for creating new enzymes, and we anticipate the creation of a wide range of useful new catalysts in the future.
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                Author and article information

                Journal
                Angewandte Chemie International Edition
                Angew. Chem. Int. Ed.
                Wiley-Blackwell
                14337851
                August 07 2017
                August 07 2017
                : 56
                : 33
                : 9680-9703
                Article
                10.1002/anie.201610129
                28085996
                582263db-a404-4878-96b3-70d686d7e583
                © 2017

                http://doi.wiley.com/10.1002/tdm_license_1.1

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