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
Full text not available in this repository. (Request a copy from the Strathclyde author)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, biocatalysis, enzymes, fluorescence, denaturation, mixtures, relevant, Chemistry |
| Subjects: | Science > Chemistry |
| Department: | Faculty of Science > Pure and Applied Chemistry Faculty of Science > Institute of Photonics |
| Related URLs: | |
| Depositing user: | Users 16 not found. |
| Date Deposited: | 13 Mar 2006 |
| Last modified: | 04 Oct 2012 15:26 |
| URI: | http://strathprints.strath.ac.uk/id/eprint/326 |
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