Rational modification of enzyme catalysis by engineering surface charge View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1987-08

AUTHORS

Alan J. Russell, Alan R. Fersht

ABSTRACT

Changing the surface charge of subtilisin by site-directed mutagenesis produces enzymes with significantly shifted pH-activity profiles, higher catalytic activities and altered specificities. Insight into water as a dielectric, the role of ions in electrostatic shielding and the field effects on catalysis is obtained and suggests rules for tailoring pH-activity profiles.

PAGES

496-500

Journal

TITLE

Nature

ISSUE

6130

VOLUME

328

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  • Identifiers

    URI

    http://scigraph.springernature.com/pub.10.1038/328496a0

    DOI

    http://dx.doi.org/10.1038/328496a0

    DIMENSIONS

    https://app.dimensions.ai/details/publication/pub.1033580843

    PUBMED

    https://www.ncbi.nlm.nih.gov/pubmed/3302724


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