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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Εκδόθηκε σε:	Appl Environ Microbiol
Κύριοι συγγραφείς:	Kubo, M, Mitsuda, Y, Takagi, M, Imanaka, T
Μορφή:	Artigo
Γλώσσα:	Inglês
Έκδοση:	American Society for Microbiology (ASM) 1992
Θέματα:	Research Article
Διαθέσιμο Online:	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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