Analysis of Enzyme Structure and Activity by Protein Engineering (pages 467–473)
Prof. Dr. Alan R. Fersht, Jian-Ping Shi, Anthony J. Wilkinson, Prof. David M. Blow, Paul Carter, Dr. Mary M. Y. Waye and Dr. Greg P. Winter
Article first published online: 22 DEC 2003 | DOI: 10.1002/anie.198404673
The systematic alteration of proteins by site-directed mutagenesis of the corresponding gene is facilitated, on the one hand, by recombinant DNA technology and, on the other, by the chemical synthesis of DNA fragments. The altered activity of the mutant enzymes can then be directly correlated with structural changes, which in the ideal case can be investigated by high-resolution X-ray crystallography. For example, with tyrosyl-tRNA synthetase from Bacillus stearothermophilus it has been possible to tailor-make an enzyme with increased substrate specificity.