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Human glutathione transferase Al-1 demonstrates both half-of-the-sites and all-of-the-sites reactivity
Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Chemistry, Department of Biochemistry.
2001 (English)In: JOURNAL OF BIOLOGICAL CHEMISTRY, ISSN 0021-9258, Vol. 276, no 38, 35599-35605 p.Article in journal (Refereed) Published
Abstract [en]

A study of the kinetics of a heterodimeric variant of glutathione transferase (GST) A1-1 has led to the conclusion that, although the wild-type enzyme displays all-of-the-sites reactivity in nucleophilic aromatic substitution reactions, it demonstrates ha

Place, publisher, year, edition, pages
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC , 2001. Vol. 276, no 38, 35599-35605 p.
Keyword [en]
RAT-LIVER CYTOSOL; S-TRANSFERASE; ACTIVE-SITE; CATALYTIC ACTIVITY; SUBSTRATE-BINDING; CRYSTAL-STRUCTURE; DIRECTED MUTAGENESIS; PRODUCT COMPLEXES; ESCHERICHIA-COLI; MALIC ENZYME
Identifiers
URN: urn:nbn:se:uu:diva-38021OAI: oai:DiVA.org:uu-38021DiVA: diva2:65920
Note
Addresses: Mannervik B, Uppsala Univ, Dept Biochem, Biomed Ctr, Box 576, SE-75123 Uppsala, Sweden. Uppsala Univ, Dept Biochem, Biomed Ctr, SE-75123 Uppsala, Sweden.Available from: 2008-10-17 Created: 2008-10-17 Last updated: 2011-01-14

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