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Catalytic Mechanisms Revealed by Protein Engineering of Tyrosyl-tRNA Synthetase

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Enzyme Dynamics and Regulation
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Abstract

Enzymology has been revolutionized by genetic engineering: Any amino acid residue in a protein may be replaced by mutation of its gene using variations of oligodeoxynucleotide-directed mutagenesis (1) or cassette mutagenesis (2). Thus given a gene for an enzyme, a means for its expression, and detailed knowledge of its three-dimensional structure, the relation between its structure and activity may be studied in a rational and systematic manner by preparing mutants and examining them by kinetics and spectroscopy. The first enzyme to be analyzed in such a manner is the tyrosyl-tRNA synthetase from Bacillus stearothermophilus (3). After 4 years of intensive efforts by my research group and that of G. Winter in preparing and analyzing mutants, what have we learnt about catalysis in general and the tyrosyl-tRNA synthetase in particular?

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Fersht, A.R. (1988). Catalytic Mechanisms Revealed by Protein Engineering of Tyrosyl-tRNA Synthetase. In: Chock, P.B., Huang, C.Y., Tsou, C.L., Wang, J.H. (eds) Enzyme Dynamics and Regulation. Springer, New York, NY. https://doi.org/10.1007/978-1-4612-3744-0_46

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  • DOI: https://doi.org/10.1007/978-1-4612-3744-0_46

  • Publisher Name: Springer, New York, NY

  • Print ISBN: 978-1-4612-8330-0

  • Online ISBN: 978-1-4612-3744-0

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