Tinkering with enzymes: what are we learning?
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.
Knowles
J R
JR
D000596:Amino Acids / Q000378:metabolism; D001665:Binding Sites; D002384:Catalysis; D055598:Chemical Phenomena; D002627:Chemistry, Physical; D004795:Enzyme Stability; D004798:Enzymes / Q000235:genetics* / Q000378:metabolism; D009154:Mutation; D013379:Substrate Specificity; D013816:Thermodynamics
D000596:Amino Acids; D004798:Enzymes