Remarkable improvements of a neutral protease activity and stability share the same structural origins.
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PMID: 20513706
Four out of seven point mutations are able to promote both activity and thermostability individually and combinedly. The catalytic efficiency (k(cat)/K(m)) of four-amino acid substituted variant (quadruple mutant) at 60 degrees C is 18-fold higher than wild type, whereas a …
Four out of seven point mutations are able to promote both activity and thermostability individually and combinedly. The catalytic efficienc …