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Relaxed thiol substrate specificity of glutathione transferase effected by a non-substrate glutathione derivative
Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Biochemistry and Organic Chemistry, Biochemistry.
1988 (English)In: FEBS Letters, ISSN 0014-5793, E-ISSN 1873-3468, Vol. 231, no 1, 155-158 p.Article in journal (Refereed) Published
Abstract [en]

Rat glutathione transferase 4-4 catalysed the conjugation of 2-mercaptoethanol with 1-chloro-2,4-dinitrobenzene in the presence of S-methyl-glutathione. The reaction was linearly dependent on enzyme concentration and saturation was seen with respect to both 2-mercaptoethanol and S-methyl-glutathione concentration. High concentrations of S-methyl-gluta-thione were inhibitory. The results suggest that the natural substrate glutathione has two distinct functions in the normal catalytic reaction, (i) induction of a catalytically competent conformation of the enzyme and (ii) provision of the substrate sulfhydryl group in the reaction catalyzed.

Place, publisher, year, edition, pages
1988. Vol. 231, no 1, 155-158 p.
Keyword [en]
Conformational change, Thiol substrate specificity, Reaction mechanism, Glutathione transferase, Glutathione derivative
National Category
Natural Sciences
URN: urn:nbn:se:uu:diva-121184DOI: 10.1016/0014-5793(88)80722-1ISI: A1988M970000033PubMedID: 3360119OAI: oai:DiVA.org:uu-121184DiVA: diva2:343694
Available from: 2010-08-15 Created: 2010-03-18 Last updated: 2010-11-10Bibliographically approved

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