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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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Publikašuvnnas:Appl Environ Microbiol
Váldodahkkit: Kubo, M, Mitsuda, Y, Takagi, M, Imanaka, T
Materiálatiipa: Artigo
Giella:Inglês
Almmustuhtton: American Society for Microbiology (ASM) 1992
Fáttát:
Liŋkkat: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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