期刊
SCIENCE
卷 308, 期 5723, 页码 857-860出版社
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.1107387
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资金
- NCI NIH HHS [CA97328, R01 CA097328, R01 CA085939, CA85939] Funding Source: Medline
- NIGMS NIH HHS [GM49857, GM59224, R01 GM059224, R01 GM049857, T32-GM08268, T32 GM008268] Funding Source: Medline
Thermostabilizing an enzyme while maintaining its activity for industrial or biomedical applications can be difficult with traditional selection methods. We describe a rapid computational approach that identified three mutations within a model enzyme that produced a 10 degrees C increase in apparent melting temperature T(m) and a 30-fold increase in half-life at 50 degrees C, with no reduction in catalytic efficiency. The effects of the mutations were synergistic, giving an increase in excess of the sum of their individual effects. The redesigned enzyme induced an increased, temperature-dependent bacterial growth rate under conditions that required its activity, thereby coupling molecular and metabolic engineering.
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