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. 1992 Nov;58(11):3779–3783. doi: 10.1128/aem.58.11.3779-3783.1992

Alteration of specific activity and stability of thermostable neutral protease by site-directed mutagenesis.

M Kubo 1, Y Mitsuda 1, M Takagi 1, T Imanaka 1
PMCID: PMC183176  PMID: 1482198

Abstract

On the basis of three-dimensional information, many amino acid substitutions were introduced in the thermostable neutral protease (NprM) of Bacillus stearothermophilus MK232 by site-directed mutagenesis. When Glu at position 143 (Glu-143), which is one of the proposed active sites, was substituted for by Gln and Asp, the proteolytic activity disappeared. F114A (Phe-114 to Ala), Y110W (Tyr-110 to Trp), and Y211W (Tyr-211 to Trp) mutant enzymes had higher activity (1.3- to 1.6-fold) than the wild-type enzyme. When an autolysis site, Tyr-93, was replaced by Gly and Ser, the remaining activities of those mutant enzymes were higher than that of the wild-type enzyme.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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