## Abstract The spleen of the exhypoxic polycythemic mouse was employed as a model system to study the effect of erythropoietin on enzymes that chemically modify nuclear proteins. At selected time intervals after in vivo administration of erythropoietin, acetyltransferase and methyltransferase acti
Enzyme design by chemical modification of protein scaffolds
โ Scribed by Cheng-Min Tann; Dongfeng Qi; Mark D Distefano
- Publisher
- Elsevier Science
- Year
- 2001
- Tongue
- English
- Weight
- 288 KB
- Volume
- 5
- Category
- Article
- ISSN
- 1367-5931
No coin nor oath required. For personal study only.
โฆ Synopsis
Covalent modification methods allow an almost unlimited range of functionality to be introduced into proteins. In concert with genetic techniques, chemical strategies have had significant impact in the field of enzyme design. Major recent developments include introducing catalytic activity into inactive proteins, modifying the selectivity and/or reactivity of existing enzymes and designing novel enzyme-based biosensors. New chemical methods promise to further increase the range of functionality that can be incorporated into proteins. These results suggest that semi-synthetic methods will play a key role in the development of future biocatalysts.
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