The relationship between physical property and function of highly activated mutants of thermolysin |
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| Authors: | Shun-Ichi Kidokoro Yoichiro Miki Kimiko Endo Akiyoshi Wada |
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| Affiliation: | (1) Sagami Chemical Research Center, Nishiohnuma 4-4-1, 229 Sagamihara, Kanagawa, Japan |
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| Abstract: | Thermolysin mutants having a variety of amino acid at the 119th position are designed by considering electrostatic field effect upon the active area. The most activated mutant has five times higher hydrolytic activity than the wild type. Negative correlation between the activity and the thermal stability is observed. A combined effect of the flexibility of the substrate binding site and the negative electrostatic field around the site is suggested as a key to enhance the activity. |
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| Keywords: | Protein engineering thermolysin activity stability |
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