Minor Modifications of the C-terminal Helix Reschedule the Favored Chemical Reactions Catalyzed by Theta Class Glutathione Transferase T1-1:
2010 (English)In: Journal of Biological Chemistry, ISSN 0021-9258, E-ISSN 1083-351X, Vol. 285, no 8, 5639-5645 p.Article in journal (Refereed) Published
Adaptive responses to novel toxic challenges provide selective advantages to organisms in evolution. Glutathione transferases (GSTs) play a pivotal role in the cellular defense because they are main contributors to the inactivation of genotoxic compounds of exogenous as well as of endogenous origins. GSTs are promiscuous enzymes catalyzing a variety of chemical reactions with numerous alternative substrates. Despite broad substrate acceptance, individual GSTs display pronounced selectivities such that only a limited number of substrates are transformed with high catalytic efficiency. The present study shows that minor structural changes in the C-terminal helix of mouse GST T1-1 induce major changes in the substrate-activity profile of the enzyme to favor novel chemical reactions and to suppress other reactions catalyzed by the parental enzyme.
Place, publisher, year, edition, pages
2010. Vol. 285, no 8, 5639-5645 p.
Biochemistry and Molecular Biology
IdentifiersURN: urn:nbn:se:uu:diva-119507DOI: 10.1074/jbc.M109.074757ISI: 000275327200056PubMedID: 20022951OAI: oai:DiVA.org:uu-119507DiVA: diva2:300348