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Redesign of substrate-selectivity determining modules of glutathione transferase A1-1 installs high catalytic efficiency with toxic alkenal products of lipid peroxidation
Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Chemistry, Department of Biochemistry.
2000 (English)In: PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, ISSN 0027-8424, Vol. 97, no 17, 9408-9412 p.Article in journal (Refereed) Published
Abstract [en]

The evolution of proteins for novel functions involves point mutations and recombinations of domains or structural segments. Mimicking this process by rational design in vitro is still a major challenge. The present report demonstrates that the active sit

Place, publisher, year, edition, pages
NATL ACAD SCIENCES , 2000. Vol. 97, no 17, 9408-9412 p.
Keyword [en]
hydroxyalkenal; protein redesign; sequential design; S-TRANSFERASES; ACTIVE-SITE; HETEROLOGOUS EXPRESSION; COENZYME SPECIFICITY; EVOLUTION; ACID; DEHYDROGENASE; ENZYME; DETOXICATION; MUTAGENESIS
Identifiers
URN: urn:nbn:se:uu:diva-37990OAI: oai:DiVA.org:uu-37990DiVA: diva2:65889
Note
Addresses: Mannervik B, Univ Uppsala, Biomed Ctr, Dept Biochem, Box 576, SE-75123 Uppsala, Sweden. Univ Uppsala, Biomed Ctr, Dept Biochem, SE-75123 Uppsala, Sweden.Available from: 2008-10-17 Created: 2008-10-17 Last updated: 2011-01-14

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