Alteration of enzyme specificity and catalysis by protein engineering
- 31 August 1991
- journal article
- review article
- Published by Elsevier in Current Opinion in Biotechnology
- Vol. 2 (4) , 561-567
- https://doi.org/10.1016/0958-1669(91)90081-f
Abstract
No abstract availableKeywords
This publication has 12 references indexed in Scilit:
- Design and synthesis of new enzymes based on the lactate dehydrogenase frameworkPhilosophical Transactions Of The Royal Society B-Biological Sciences, 1991
- Enhancement of the catalytic properties of human carbonic anhydrase III by site-directed mutagenesisBiochemistry, 1991
- Alteration of the specificity of subtilisin BPN' by site-directed mutagenesis in its S1 and S1' binding sitesJournal of the American Chemical Society, 1991
- Designs for a broad substrate specificity keto acid dehydrogenaseBiochemistry, 1990
- Phospholipase A2 engineering. 3. Replacement of lysine-56 by neutral residues improves catalytic efficiency significantly, alters substrate specificity, and clarifies the mechanism of interfacial recognitionJournal of the American Chemical Society, 1990
- Enzymes in organic synthesis: use of subtilisin and a highly stable mutant derived from multiple site-specific mutationsJournal of the American Chemical Society, 1990
- Engineering a novel β-Iactamase by a single point mutationProtein Engineering, Design and Selection, 1990
- Redesign of the coenzyme specificity of a dehydrogenase by protein engineeringNature, 1990
- A single amino acid substitution in lactate dehydrogenase improves the catalytic efficiency with an alternative coenzymeBiochemical and Biophysical Research Communications, 1990
- Nature's rules and chemist's tools: a way for creating novel proteinsTrends in Biochemical Sciences, 1988