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Reversible acetonitrile-induced inactivation/activation of thermolysin

Ulijn, R.V. and Janssen, A.E.M. and Moore, B.D. and Halling, P.J. and Kelly, S.M. and Price, N.C. (2002) Reversible acetonitrile-induced inactivation/activation of thermolysin. Chembiochem, 3 (11). pp. 1112-1116. ISSN 1439-4227

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Abstract

Thermolysin is catalytically inactive in mixtures or 70-15% acetonitrile in aqueous buffer. Unexpectedly, dilution of the inactive enzyme with acetonitrile leads to complete recovery of the catalytic activity in a similar way to dilution with aqueous buffer. Circular dichroism and fluorescence studies of thermolysin in the same solvent mixtures reveal discontinuous changes in the overall secondary and tertiary protein structure that correlate well with the reversible differences in catalytic activity. The spectra on either side of the minimum activity point are different from each other, a fact indicating that the enzyme may be able to access two active conformations which are thermodynamically stable in different solvent environments.

Item type: Article
ID code: 326
Keywords: activity studies, biocatalysis, enzymes, protein structures, solvent effects, Aqueous-organic media, alpha-chymotrypsin, catalytic activity, solvents, fluorescence, denaturation, mixtures, relevant, Chemistry
Subjects: Science > Chemistry
Department: Faculty of Science > Pure and Applied Chemistry
Faculty of Science > Institute of Photonics
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    Depositing user: Users 16 not found.
    Date Deposited: 13 Mar 2006
    Last modified: 06 Dec 2013 16:39
    URI: http://strathprints.strath.ac.uk/id/eprint/326

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