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Identification of Emerging Quasi-Species in Directed Enzyme Evolution
Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Biochemistry and Organic Chemistry.
Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Biochemistry and Organic Chemistry.
2009 (English)In: Biochemistry, ISSN 0006-2960, E-ISSN 1520-4995, Vol. 48, no 40, 9330-9339 p.Article in journal (Refereed) Published
Abstract [en]

The bases of enzyme evolution are structural changes in protein scaffolds combined with recognition and propagation of novel variants with valuable functional properties. Structural diversification may be accomplished by a variety of methods, including random mutations, homologous recombinations, and insertions and deletions of coding DNA sequences. The functional consequences of mutations are manifested at the protein level and are dependent on a substrate matrix, when catalytic properties are requested. Libraries of variant enzymes showing promiscuous activities can be interrogated with a set of alternative substrates. We demonstrate using a library of glutathione transferases (GSTs) that the functional properties are not uniformly distributed in substrate-activity space but form clusters, or quasi-species. Multivariate analysis facilitates the identification of such quasi-species, which can be regarded as the proper developing units in molecular evolution.

Place, publisher, year, edition, pages
2009. Vol. 48, no 40, 9330-9339 p.
National Category
Chemical Sciences
Identifiers
URN: urn:nbn:se:uu:diva-127507DOI: 10.1021/bi901168qISI: 000270459100004OAI: oai:DiVA.org:uu-127507DiVA: diva2:330479
Available from: 2010-07-15 Created: 2010-07-13 Last updated: 2017-12-12Bibliographically approved

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