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

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 f...

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Bibliografiske detaljer

Udgivet i:	Appl Environ Microbiol
Principais autores:	Kubo, M, Mitsuda, Y, Takagi, M, Imanaka, T
Format:	Artigo
Sprog:	Inglês
Udgivet:	American Society for Microbiology (ASM) 1992
Fag:	Research Article
Online adgang:	https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC183176/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/1482198/ https://ncbi.nlm.nih.govhttps://doi.org/10.1128/aem.58.11.3779-3783.1992
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