Abstract
Catalytic mechanisms of glutathione S-transferases (GSTs) were viewed in terms of the independent steps of GSH binding and activation and the productive reorientation of the electrophilic substituent of the second substrate. NMR and isothermal titration microcalorimetric methods were used to study GST-ligand interactions. The family of five human Mu-class GSTs was employed as a paradigm to study structure, catalysis and subunit assembly mechanisms.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 170-172 |
| Number of pages | 3 |
| Journal | Chemico-Biological Interactions |
| Volume | 133 |
| Issue number | 1-3 |
| State | Published - Feb 28 2001 |
Keywords
- Catalysis
- Glutathione transferase
- Substrate reorientation
- Thiolate anion
ASJC Scopus subject areas
- Toxicology
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In: Chemico-Biological Interactions, Vol. 133, No. 1-3, 28.02.2001, p. 170-172.
Research output: Contribution to journal › Article › peer-review
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TY - JOUR
T1 - Interpreting the broad substrate specificities of glutathione S-transferases
AU - Tchaikovskaya, Tatyana
AU - Patskovsky, Yury V.
AU - Federov, Alexander
AU - Almo, Steven C.
AU - Girvin, Mark
AU - Listowsky, Irving
N1 - Funding Information: This work was supported by a grant from the US Army Medical Research and Material Command (Breast Cancer Research Program). Funding Information: This work was supported by an Australian Research Council Project Grant and an Australian Research Council Senior Research Fellowship (to M.W.P.), a National Health and Medical Research Council Postgraduate Research Scholarship and an International Centre for Diffraction Data Crystallography Scholarship (to A.J.O.), an Australian Research Council Postdoctoral Fellowship (to J.R.) and a National Research Council of Italy Grant (to G.R. and M.L.B.). Funding Information: The author would like to acknowledge the invaluable contributions by the postgraduate students and staff of the Protein Structure-Function Research Programme and Richard Armstrong (Vanderbilt University) to this work. Financial support was provided by Wits University, National Research Foundation, Alexander von Humboldt Foundation and FIRCA(NIH) grant TW00779. Funding Information: This work was supported in part by SNF grant 3100-050602.97 to S.V. Funding Information: The Finnish studies were supported by the Academy of Finland, the Finnish Konkordia Foundation, and EVO funds from Kuopio University Hospital. The French study was supported by the Swiss Cancer League, the League against Cancer of Fribourg, the Cancer Research (Switzerland) and the Gustave–Roussy Institute (France). Funding Information: This work was supported by United States Public Health Service Grants CA-66561 and T32-GM-08550. Funding Information: This work was supported by the University of the Witwatersrand, the South African National Research Foundation and the Fogarty International Research Collaboration Award TW00779. Funding Information: This study is part of special projects supported by Italian Ministry of University and of Scientific and Technological Research, Italian National Research Council and Italian Ministry of Health. Funding Information: The authors would like to acknowledge Jim Parsons, Gaoyi Xioa, and Marcia Newcomer for their assistance with various aspects of this project. Monetary support from the NIH and the Training Program in Molecular Biophysics is also acknowledged. Funding Information: This work is supported by the DFG (grant Li 1-3, 1-4). Funding Information: The work presented here was partially supported by the Deutsche Forschungsge-meinschaft (SFB 475). Funding Information: The author would like to thank Ralph Hermanns for technical assistance and Professor Peter van Bladeren for the rat GST isoenzymes. This research was funded by the Dutch Cancer Society (project RUL017-1407). Funding Information: This work was supported by grants from the U.S. National Cancer Institute (76420), the Howard Hughes Medical Institute, and the Oakland University Research Excellence Fund. Funding Information: The ATPase activity of recombinant RalBP1 was only marginally stimulated by DNP-SG (by approximately 30%). This may indicate that the protein, as isolated from the bacterial lysate, is saturated with a tightly bound ligand and already near-maximally stimulated. Antibiotics used for plasmid selection are possible candidates for such ligands. This interpretation was supported by the fact that omitting chloramphenicol from the bacterial growth medium improved stimulation. Funding Information: Support for the research has been obtained from the Swedish Research Council for Engineering Sciences, the Swedish Natural Science Research Council, the Swedish Cancer Society, and the Carl Trygger Foundation. Funding Information: I gratefully acknowledge Jim Parsons at the Vanderbilt University School of Medicine for the generation of the recombinant mutant plasmids. This work was supported by the University of the Witwatersrand, the South African National Research Foundation, the Fogarty International Collaboration Award TW00779, Grant GM30910 from the National Institutes of Health and the Alexander von Humboldt Foundation. Funding Information: The Andrew Mellon Foundation, the University of the Witwatersrand and the South African National Research Foundation for financial support. Funding Information: This work is supported by National Institute of Health Grants AI22531, AI31599, AR36308, ES06105, HL03208. Funding Information: Supported by the British Lung Foundation, MURST, Ministero del Lavoro e della Previdenza Sociale, Danish Research Academy and North Staffordshire Medical Institute. Funding Information: This work was supported by MURST-40%; grants telethon-E872, AIRC, EU (QRLT-1999-00739); Ministero Sanità. Funding Information: Support from the Swedish Medical Research Council (projects no 31X-12573), the Swedish Society of Medicine, the Swedish Cancer Society, Harald Jeansson’s and Harald and Greta Jeansson’s, and the Karolinska Institutet foundations are gratefully acknowledged. Funding Information: Financial support is acknowledged with grateful thanks from the International Programs in Chemical Sciences (IPICS), Uppsala University and the Research Board, University of Zimbabwe. Funding Information: We thank the staff of ESRF synchrotron, Grenoble and the SRS synchrotron, Daresbury for help with data collection. Financial support from ESRF for our visit to Grenoble is gratefully acknowledged. We also acknowledge Aventis Crop Science UK Ltd. for funding this project. Funding Information: Supported by The North Staffordshire Medical Institute and the McCall Foundation. Funding Information: This work was supported in part by NIH:NIEHS grant ES07804 (to PZ) and by a pilot grant from the University of Arkansas for Medical Science. Funding Information: Funding for this project was provided by grants from the National Institutes of Health (R01-EOS9427) and the U.S. Environmental Protection Agency (R 827441)– Funding Information: The research in our laboratory is supported by grants from The Swedish Medical Research Council and from AstraZeneca. Funding Information: This work was funded by Aventis Crop Science UK Ltd. Funding Information: This study was supported by the Swedish Cancer Society, The National Board for Laboratory Animals, Carl Tryggers Foundation and funds from Karolinska Institutet. Funding Information: This work was funded by a grant from the Association of International Cancer Research (99-041, awarded to JDH and MY). Simon A. Chanas thanks the MRC and Zeneca for a collaborative Ph.D. studentship. Funding Information: This study was supported by the Swedish Cancer Society, The National Board for Laboratory Animals, Carl Tryggers Foundation and funds from Karolinska Insitutet. Funding Information: H.J.L. was supported by NIH grants 1R01CA66782 and 1R01CA73403. Funding Information: This work was supported in part by NIH:NIEHS grant ES07804 (to PZ). Funding Information: This work was supported by the Research Science Funds of Serbia, Grant c03E18. Funding Information: This work was supported in part by a grant from the Ministero dell’ Università e della Ricerca Scientifica e Tecnologica. Funding Information: We thank the Cancer Research Campaign, British Medical Association and British Lung Foundation for support. Funding Information: In part supported by grants GM32304 (YCA), CA77495 (SA), VA Merit Review (PZ), and CA55589 (SVS). Funding Information: The authors would like to acknowledge invaluable contributions of L.T. Laugh-lin, B. Bernat and Professor John Helman (Cornell University) to various aspects of this work. NIH Grants A142756 and GM30910 and the Training Program in Molecular Biophysics at Vanderbilt provided support for this work. Funding Information: We thank Pedro Miguel Santos for sending pPR9TT plasmid and E. coli strains used in this work and P. Di Nardo for checking the English. This work was supported in part by European Community contract no. QLK3-CT1999–00041. Funding Information: This work was supported in part by grant from the Ministero dell’ Università e della Ricerca Scientifica e Tecnologica. Funding Information: This investigation received financial support from the UNDP:WORLD BANK: WHO Special Programme for Research and Training in Tropical Medicine (TDR0096 and TDR 980281). Funding Information: This work was supported by a grant from the National Science Foundation (MCB-9723308). Funding Information: This research was supported in part by National Institute of Environmental Health Sciences grant ES03127 to M.W.A.
PY - 2001/2/28
Y1 - 2001/2/28
N2 - Catalytic mechanisms of glutathione S-transferases (GSTs) were viewed in terms of the independent steps of GSH binding and activation and the productive reorientation of the electrophilic substituent of the second substrate. NMR and isothermal titration microcalorimetric methods were used to study GST-ligand interactions. The family of five human Mu-class GSTs was employed as a paradigm to study structure, catalysis and subunit assembly mechanisms.
AB - Catalytic mechanisms of glutathione S-transferases (GSTs) were viewed in terms of the independent steps of GSH binding and activation and the productive reorientation of the electrophilic substituent of the second substrate. NMR and isothermal titration microcalorimetric methods were used to study GST-ligand interactions. The family of five human Mu-class GSTs was employed as a paradigm to study structure, catalysis and subunit assembly mechanisms.
KW - Catalysis
KW - Glutathione transferase
KW - Substrate reorientation
KW - Thiolate anion
UR - http://www.scopus.com/inward/record.url?scp=0003129131&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0003129131&partnerID=8YFLogxK
M3 - Article
AN - SCOPUS:0003129131
SN - 0009-2797
VL - 133
SP - 170
EP - 172
JO - Chemico-Biological Interactions
JF - Chemico-Biological Interactions
IS - 1-3
ER -