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Science 5 June 1987:
Vol. 236. no. 4806, pp. 1252 - 1258
DOI: 10.1126/science.3296192
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Articles
Science, Vol 236, Issue 4806, 1252-1258
Copyright © 1987 by American Association for the Advancement of Science
Tinkering with enzymes: what are we learning?
Knowles JR
It is now possible, by site-directed mutagenesis of the gene, to change any amino acid residue in a protein to any other. In enzymology, application of this technique is leading to exciting new insights both into the mechanism of catalysis by particular enzymes, and into the basis of catalysis itself. The precise and often delicate changes that are being made in and near the active sites of enzymes are illuminating the interdependent roles of catalytic groups, and are allowing the first steps to be taken toward the rational alteration of enzyme specificity and reactivity.
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