Effect of a charged residue at the 213th site of thermolysin on the enzymatic activity

Considering the electrostatic potential of active site, four mutants of thermolysin (EC 3.4.24.4) are designed in an attempt to change the optimum pH of the hydrolytic activity toward acidic regions. On the basis of the numerical calculation of the electrostatic potential in the thermolysin molecule...

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Veröffentlicht in:	Journal of molecular catalysis. B, Enzymatic Enzymatic, 1996, Vol.1 (3), p.191-199
Hauptverfasser:	Miki, Yoichiro, Kidokoro, Shun-ichi, Endo, Kimiko, Wada, Akiyoshi, Yoneya, Takashi, Aoyama, Atsuo, Kai, Kenichi, Miyake, Toshio, Nagao, Hiromasa
Format:	Artikel
Sprache:	eng
Schlagworte:	Activity Biological and medical sciences Biotechnology Electrostatic potential Fundamental and applied biological sciences. Psychology Methods. Procedures. Technologies Optimum pH Protein engineering Thermolysin
Online-Zugang:	Volltext
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