Improving enzyme properties: when are closer mutations better?
| Autor: | Krista L. Morley, Romas J. Kazlauskas |
|---|---|
| Rok vydání: | 2005 |
| Předmět: |
chemistry.chemical_classification
Genetics Mutation biology Mutagenesis Active site Substrate (chemistry) Bioengineering Directed evolution medicine.disease_cause Amino acid Enzymes Substrate Specificity Enzyme Biochemistry chemistry biology.protein medicine Substrate specificity Animals Humans Biotechnology |
| Zdroj: | Trends in biotechnology. 23(5) |
| ISSN: | 0167-7799 |
| Popis: | Study of mutations that improve enzyme properties reveals that in many, but not all, cases closer mutations are more effective than distant ones. For enantioselectivity, substrate selectivity and new catalytic activity (catalytic promiscuity) closer mutations improved enzymes more effectively than distant ones. However, both close and distant mutations can improve activity, thermal stability and also probably stability toward organic solvents. Typical random mutagenesis methods, such as error-prone PCR, create greater numbers of distant mutations than close mutations because enzymes contain more amino acids distant from the active site than close to the active site. This suggests that instead of mutating the entire enzyme, focusing mutations near the substrate-binding site might dramatically increase the success rate in many directed evolution experiments. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
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