ACS Publications. Most Trusted. Most Cited. Most Read
My Activity
CONTENT TYPES

Figure 1Loading Img

Structure, Catalytic Mechanism, and Evolution of the Glutathione Transferases

View Author Information
Department of Biochemistry and Center in Molecular Toxicology, Vanderbilt University School of Medicine, Nashville, Tennessee 37232
Cite this: Chem. Res. Toxicol. 1997, 10, 1, 2–18
Publication Date (Web):January 20, 1997
https://doi.org/10.1021/tx960072x
Copyright © 1997 American Chemical Society

    Article Views

    4729

    Altmetric

    -

    Citations

    918
    LEARN ABOUT THESE METRICS
    Other access options

    Note: In lieu of an abstract, this is the article's first page.

    Free first page

    Read this article

    To access this article, please review the available access options below.

    Get instant access

    Purchase Access

    Read this article for 48 hours. Check out below using your ACS ID or as a guest.

    Recommended

    Access through Your Institution

    You may have access to this article through your institution.

    Your institution does not have access to this content. You can change your affiliated institution below.

    *

     Phone:  (615) 343-2920; FAX:  (615) 343-2921; email:  armstrong@ toxicology.mc.vanderbilt.edu.

    Cited By

    This article is cited by 918 publications.

    1. Fan Du, Chen-Xi Feng, Di-Fei Zhou, Xiaomin Hou. Evaluation of the Two Typical Diamide Insecticide-Induced Oxidative Damages and the Molecular Mechanism Underlying Their Toxicity in Triticum aestivum. Journal of Agricultural and Food Chemistry 2023, 71 (21) , 8008-8015. https://doi.org/10.1021/acs.jafc.3c01085
    2. Nicolai Lehnert, Eunsuk Kim, Hai T. Dong, Jill B. Harland, Andrew P. Hunt, Elizabeth C. Manickas, Kady M. Oakley, John Pham, Garrett C. Reed, Victor Sosa Alfaro. The Biologically Relevant Coordination Chemistry of Iron and Nitric Oxide: Electronic Structure and Reactivity. Chemical Reviews 2021, 121 (24) , 14682-14905. https://doi.org/10.1021/acs.chemrev.1c00253
    3. Alena Tierbach, Ksenia J. Groh, René Schoenenberger, Kristin Schirmer, Marc J.-F. Suter. Characterization of the Mercapturic Acid Pathway, an Important Phase II Biotransformation Route, in a Zebrafish Embryo Cell Line. Chemical Research in Toxicology 2020, 33 (11) , 2863-2871. https://doi.org/10.1021/acs.chemrestox.0c00315
    4. Matthew A. Cerny, Amit S. Kalgutkar, R. Scott Obach, Raman Sharma, Douglas K. Spracklin, Gregory S. Walker. Effective Application of Metabolite Profiling in Drug Design and Discovery. Journal of Medicinal Chemistry 2020, 63 (12) , 6387-6406. https://doi.org/10.1021/acs.jmedchem.9b01840
    5. Mohd. Jameel, Mohd Shoeb, Mohd Talib Khan, Rizwan Ullah, Mohammad Mobin, Mohd Kaleemullah Farooqi, Sayed Mohammed Adnan. Enhanced Insecticidal Activity of Thiamethoxam by Zinc Oxide Nanoparticles: A Novel Nanotechnology Approach for Pest Control. ACS Omega 2020, 5 (3) , 1607-1615. https://doi.org/10.1021/acsomega.9b03680
    6. Reece G. Kenny, Celine J. Marmion. Toward Multi-Targeted Platinum and Ruthenium Drugs—A New Paradigm in Cancer Drug Treatment Regimens?. Chemical Reviews 2019, 119 (2) , 1058-1137. https://doi.org/10.1021/acs.chemrev.8b00271
    7. Jiyuan Liu, Yifan Li, Zhen Tian, Hong Sun, Xi’en Chen, Shengli Zheng, Yalin Zhang. Identification of Key Residues Associated with the Interaction between Plutella xylostella Sigma-Class Glutathione S-Transferase and the Inhibitor S-Hexyl Glutathione. Journal of Agricultural and Food Chemistry 2018, 66 (39) , 10169-10178. https://doi.org/10.1021/acs.jafc.8b03967
    8. Zhangjian Huang, Jianbing Wu, Yu Zou, Haoliang Yuan, Yinqiu Zhang, Yue Fei, Atul Bhardwaj, Jatinder Kaur, Edward E. Knaus, Yihua Zhang. Glutathione S-Transferase π-Activatable O2-(Sulfonylethyl Derived) Diazeniumdiolates Potently Suppress Melanoma in Vitro and in Vivo. Journal of Medicinal Chemistry 2018, 61 (5) , 1833-1844. https://doi.org/10.1021/acs.jmedchem.7b01178
    9. Lazaros Stefanidis, Krystal V. Scinto, Monica I. Strada, and Benjamin J. Alper . Bisubstrate Kinetics of Glutathione S-Transferase: A Colorimetric Experiment for the Introductory Biochemistry Laboratory. Journal of Chemical Education 2018, 95 (1) , 146-151. https://doi.org/10.1021/acs.jchemed.7b00535
    10. Linda Spahiu, Johan Ålander, Astrid Ottosson-Wadlund, Richard Svensson, Carina Lehmer, Richard N. Armstrong, and Ralf Morgenstern . Global Kinetic Mechanism of Microsomal Glutathione Transferase 1 and Insights into Dynamic Enzyme Activation. Biochemistry 2017, 56 (24) , 3089-3098. https://doi.org/10.1021/acs.biochem.7b00285
    11. F. Baier, J. N. Copp, and N. Tokuriki . Evolution of Enzyme Superfamilies: Comprehensive Exploration of Sequence–Function Relationships. Biochemistry 2016, 55 (46) , 6375-6388. https://doi.org/10.1021/acs.biochem.6b00723
    12. Erica Del Grosso, Anne-Marie Dallaire, Alexis Vallée-Bélisle, and Francesco Ricci . Enzyme-Operated DNA-Based Nanodevices. Nano Letters 2015, 15 (12) , 8407-8411. https://doi.org/10.1021/acs.nanolett.5b04566
    13. Kazuko Inoue, Katsuyuki Fukuda, Tsutomu Yoshimura, and Kazutomi Kusano . Comparison of the Reactivity of Trapping Reagents toward Electrophiles: Cysteine Derivatives Can Be Bifunctional Trapping Reagents. Chemical Research in Toxicology 2015, 28 (8) , 1546-1555. https://doi.org/10.1021/acs.chemrestox.5b00129
    14. Chi Zhang, Peng Dai, Alexander M. Spokoyny, and Bradley L. Pentelute . Enzyme-Catalyzed Macrocyclization of Long Unprotected Peptides. Organic Letters 2014, 16 (14) , 3652-3655. https://doi.org/10.1021/ol501609y
    15. Guang Qiang Dong, Sara Calhoun, Hao Fan, Chakrapani Kalyanaraman, Megan C. Branch, Susan T. Mashiyama, Nir London, Matthew P. Jacobson, Patricia C. Babbitt, Brian K. Shoichet, Richard N. Armstrong, and Andrej Sali . Prediction of Substrates for Glutathione Transferases by Covalent Docking. Journal of Chemical Information and Modeling 2014, 54 (6) , 1687-1699. https://doi.org/10.1021/ci5001554
    16. Alden E. Voelker and Rajesh Viswanathan . Synthesis of a Suite of Bioorthogonal Glutathione S-Transferase Substrates and Their Enzymatic Incorporation for Protein Immobilization. The Journal of Organic Chemistry 2013, 78 (19) , 9647-9658. https://doi.org/10.1021/jo401278x
    17. Alden E. Voelker and Rajesh Viswanathan . Self-Catalyzed Immobilization of GST-Fusion Proteins for Genome-Encoded Biochips. Bioconjugate Chemistry 2013, 24 (8) , 1295-1301. https://doi.org/10.1021/bc400128g
    18. Junjie Fu, Ling Liu, Zhangjian Huang, Yisheng Lai, Hui Ji, Sixun Peng, Jide Tian, and Yihua Zhang . Hybrid Molecule from O2-(2,4-Dinitrophenyl)diazeniumdiolate and Oleanolic Acid: A Glutathione S-Transferase π-Activated Nitric Oxide Prodrug with Selective Anti-Human Hepatocellular Carcinoma Activity and Improved Stability. Journal of Medicinal Chemistry 2013, 56 (11) , 4641-4655. https://doi.org/10.1021/jm400393u
    19. Rong-Zhen Liao and Walter Thiel . Determinants of Regioselectivity and Chemoselectivity in Fosfomycin Resistance Protein FosA from QM/MM Calculations. The Journal of Physical Chemistry B 2013, 117 (5) , 1326-1336. https://doi.org/10.1021/jp4002719
    20. Georgia E. Koutsoumpli, Virginia D. Dimaki, Trias N. Thireou, Elias E. Eliopoulos, Nikolaos E. Labrou, George I. Varvounis, and Yannis D. Clonis . Synthesis and Study of 2-(Pyrrolesulfonylmethyl)-N-arylimines: A New Class of Inhibitors for Human Glutathione Transferase A1-1. Journal of Medicinal Chemistry 2012, 55 (15) , 6802-6813. https://doi.org/10.1021/jm300385f
    21. Agnes Rinaldo-Matthis, Shabbir Ahmad, Anders Wetterholm, Peter Lachmann, Ralf Morgenstern, and Jesper Z. Haeggström . Pre-Steady-State Kinetic Characterization of Thiolate Anion Formation in Human Leukotriene C4 Synthase. Biochemistry 2012, 51 (4) , 848-856. https://doi.org/10.1021/bi201402s
    22. John A. Gerlt, Karen N. Allen, Steven C. Almo, Richard N. Armstrong, Patricia C. Babbitt, John E. Cronan, Debra Dunaway-Mariano, Heidi J. Imker, Matthew P. Jacobson, Wladek Minor, C. Dale Poulter, Frank M. Raushel, Andrej Sali, Brian K. Shoichet, and Jonathan V. Sweedler . The Enzyme Function Initiative. Biochemistry 2011, 50 (46) , 9950-9962. https://doi.org/10.1021/bi201312u
    23. Nishal Parbhoo, Stoyan H. Stoychev, Sylvia Fanucchi, Ikechukwu Achilonu, Roslin J. Adamson, Manuel Fernandes, Samantha Gildenhuys, and Heini W. Dirr . A Conserved Interdomain Interaction Is a Determinant of Folding Cooperativity in the GST Fold. Biochemistry 2011, 50 (32) , 7067-7075. https://doi.org/10.1021/bi2006509
    24. Nina V. Stourman, Megan C. Branch, Matthew R. Schaab, Joel M. Harp, Jane E. Ladner, and Richard N. Armstrong . Structure and Function of YghU, a Nu-Class Glutathione Transferase Related to YfcG from Escherichia coli. Biochemistry 2011, 50 (7) , 1274-1281. https://doi.org/10.1021/bi101861a
    25. Mostafa I. Fekry, Nathan E. Price, Hong Zang, Chaofeng Huang, Michael Harmata, Paul Brown, J. Scott Daniels, and Kent S. Gates . Thiol-Activated DNA Damage by α-Bromo-2-cyclopentenone. Chemical Research in Toxicology 2011, 24 (2) , 217-228. https://doi.org/10.1021/tx100282b
    26. Amit S. Kalgutkar, Vincent Mascitti, Raman Sharma, Gregory W. Walker, Tim Ryder, Thomas S. McDonald, Yue Chen, Cathy Preville, Arindrajit Basak, Kim F. McClure, Jeffrey T. Kohrt, Ralph P. Robinson, Michael J. Munchhof, and Peter Cornelius . Intrinsic Electrophilicity of a 4-Substituted-5-cyano-6-(2-methylpyridin-3-yloxy)pyrimidine Derivative: Structural Characterization of Glutathione Conjugates in Vitro. Chemical Research in Toxicology 2011, 24 (2) , 269-278. https://doi.org/10.1021/tx100429x
    27. Larissa M. Balogh, Isolde Le Trong, Kimberly A. Kripps, Laura M. Shireman, Ronald E. Stenkamp, Wei Zhang, Bengt Mannervik and William M. Atkins . Substrate Specificity Combined with Stereopromiscuity in Glutathione Transferase A4-4-Dependent Metabolism of 4-Hydroxynonenal. Biochemistry 2010, 49 (7) , 1541-1548. https://doi.org/10.1021/bi902038u
    28. Holly J. Atkinson and Patricia C. Babbitt . Glutathione Transferases Are Structural and Functional Outliers in the Thioredoxin Fold. Biochemistry 2009, 48 (46) , 11108-11116. https://doi.org/10.1021/bi901180v
    29. Larissa M. Balogh, Isolde Le Trong, Kimberly A. Kripps, Kaspars Tars, Ronald E. Stenkamp, Bengt Mannervik and William M. Atkins . Structural Analysis of a Glutathione Transferase A1-1 Mutant Tailored for High Catalytic Efficiency with Toxic Alkenals. Biochemistry 2009, 48 (32) , 7698-7704. https://doi.org/10.1021/bi900895b
    30. Megan C. Wadington, Jane E. Ladner, Nina V. Stourman, Joel M. Harp and Richard N. Armstrong . Analysis of the Structure and Function of YfcG from Escherichia coli Reveals an Efficient and Unique Disulfide Bond Reductase. Biochemistry 2009, 48 (28) , 6559-6561. https://doi.org/10.1021/bi9008825
    31. Daniela Andrei, Anna E. Maciag, Harinath Chakrapani, Michael L. Citro, Larry K. Keefer and Joseph E. Saavedra. Aryl Bis(diazeniumdiolates): Potent Inducers of S-Glutathionylation of Cellular Proteins and Their in Vitro Antiproliferative Activities. Journal of Medicinal Chemistry 2008, 51 (24) , 7944-7952. https://doi.org/10.1021/jm800831y
    32. Yuuta Fujikawa, Yasuteru Urano, Toru Komatsu, Kenjiro Hanaoka, Hirotatsu Kojima, Takuya Terai, Hideshi Inoue and Tetsuo Nagano . Design and Synthesis of Highly Sensitive Fluorogenic Substrates for Glutathione S-Transferase and Application for Activity Imaging in Living Cells. Journal of the American Chemical Society 2008, 130 (44) , 14533-14543. https://doi.org/10.1021/ja802423n
    33. Xiao Le Yin, Lei Jiang, Ning Hui Song and Hong Yang. Toxic Reactivity of Wheat (Triticum aestivum) Plants to Herbicide Isoproturon. Journal of Agricultural and Food Chemistry 2008, 56 (12) , 4825-4831. https://doi.org/10.1021/jf800795v
    34. Johan Viljanen, Jenny Larsson, Andréas Larsson and Kerstin S. Broo. A Multipurpose Receptor Composed of Promiscuous Proteins. Analyte Detection through Pattern Recognition. Bioconjugate Chemistry 2007, 18 (6) , 1935-1945. https://doi.org/10.1021/bc700247x
    35. Joseph R. Warner and, Shelley D. Copley. Pre-Steady-State Kinetic Studies of the Reductive Dehalogenation Catalyzed by Tetrachlorohydroquinone Dehalogenase. Biochemistry 2007, 46 (45) , 13211-13222. https://doi.org/10.1021/bi701069n
    36. Chinavenmeni S. Velu,, Suryakant K. Niture,, Catalin E. Doneanu,, Nagarajan Pattabiraman, and, Kalkunte S. Srivenugopal. Human p53 Is Inhibited by Glutathionylation of Cysteines Present in the Proximal DNA-Binding Domain during Oxidative Stress,. Biochemistry 2007, 46 (26) , 7765-7780. https://doi.org/10.1021/bi700425y
    37. Lawrence C. Thompson,, Jane E. Ladner,, Simona G. Codreanu,, Joel Harp,, Gary L. Gilliland, and, Richard N. Armstrong. 2-Hydroxychromene-2-carboxylic Acid Isomerase:  A Kappa Class Glutathione Transferase from Pseudomonas putida,,. Biochemistry 2007, 46 (23) , 6710-6722. https://doi.org/10.1021/bi700356u
    38. Anna L. Bowman,, Lars Ridder,, Ivonne M. C. M. Rietjens,, Jacques Vervoort, and, Adrian J. Mulholland. Molecular Determinants of Xenobiotic Metabolism:  QM/MM Simulation of the Conversion of 1-Chloro-2,4-dinitrobenzene Catalyzed by M1-1 Glutathione S-Transferase. Biochemistry 2007, 46 (21) , 6353-6363. https://doi.org/10.1021/bi0622827
    39. Péter Nagy and, Michael T. Ashby. Kinetics and Mechanism of the Oxidation of the Glutathione Dimer by Hypochlorous Acid and Catalytic Reduction of the Chloroamine Product by Glutathione Reductase. Chemical Research in Toxicology 2007, 20 (1) , 79-87. https://doi.org/10.1021/tx060184g
    40. Luis A. Ralat and, Roberta F. Colman. Identification of Tyrosine 79 in the Tocopherol Binding Site of Glutathione S-Transferase Pi. Biochemistry 2006, 45 (41) , 12491-12499. https://doi.org/10.1021/bi061330k
    41. Sumit S. Mahajan,, Liming Hou,, Catalin Doneanu,, Rajan Paranji,, Dean Maeda,, John Zebala, and, William M. Atkins. Optimization of Bivalent Glutathione S-Transferase Inhibitors by Combinatorial Linker Design. Journal of the American Chemical Society 2006, 128 (26) , 8615-8625. https://doi.org/10.1021/ja061766n
    42. Johan Viljanen,, Lotta Tegler,, Jenny Larsson, and, Kerstin S. Broo. Surface-Assisted Delivery of Fluorescent Groups to hGST A1-1 and a Lysine Mutant. Bioconjugate Chemistry 2006, 17 (2) , 429-437. https://doi.org/10.1021/bc0502762
    43. Yury Patskovsky,, Larysa Patskovska,, Steven C. Almo, and, Irving Listowsky. Transition State Model and Mechanism of Nucleophilic Aromatic Substitution Reactions Catalyzed by Human Glutathione S-Transferase M1a-1a. Biochemistry 2006, 45 (12) , 3852-3862. https://doi.org/10.1021/bi051823+
    44. John R. Soglia,, Leonard G. Contillo,, Amit S. Kalgutkar,, Sabrina Zhao,, Cornelis E. C. A. Hop,, James G. Boyd, and, Mark J. Cole. A Semiquantitative Method for the Determination of Reactive Metabolite Conjugate Levels in Vitro Utilizing Liquid Chromatography−Tandem Mass Spectrometry and Novel Quaternary Ammonium Glutathione Analogues. Chemical Research in Toxicology 2006, 19 (3) , 480-490. https://doi.org/10.1021/tx050303c
    45. Antonio Procopio,, Stefano Alcaro,, Sante Cundari,, Antonio De Nino,, Francesco Ortuso,, Paolo Sacchetta,, Alfonso Pennelli, and, Giovanni Sindona. Molecular Modeling, Synthesis, and Preliminary Biological Evaluation of Glutathione-S-Transferase Inhibitors as Potential Therapeutic Agents. Journal of Medicinal Chemistry 2005, 48 (19) , 6084-6089. https://doi.org/10.1021/jm0504609
    46. Joseph R. Warner,, Sherry L. Lawson, and, Shelley D. Copley. A Mechanistic Investigation of the Thiol−Disulfide Exchange Step in the Reductive Dehalogenation Catalyzed by Tetrachlorohydroquinone Dehalogenase. Biochemistry 2005, 44 (30) , 10360-10368. https://doi.org/10.1021/bi050666b
    47. Simona G. Codreanu,, Lawrence C. Thompson,, David L. Hachey,, Heini W. Dirr, and, Richard N. Armstrong. Influence of the Dimer Interface on Glutathione Transferase Structure and Dynamics Revealed by Amide H/D Exchange Mass Spectrometry. Biochemistry 2005, 44 (31) , 10605-10612. https://doi.org/10.1021/bi050836k
    48. Sofia Hederos,, Beatrice Karlsson,, Lotta Tegler, and, Kerstin S. Broo. Ligand-Directed Labeling of a Single Lysine Residue in hGST A1-1 Mutants. Bioconjugate Chemistry 2005, 16 (4) , 1009-1018. https://doi.org/10.1021/bc050111t
    49. Stephanie A. Misquitta and, Roberta F. Colman. Communication between the Two Active Sites of Glutathione S-Transferase A1-1, Probed Using Wild-Type−Mutant Heterodimers. Biochemistry 2005, 44 (24) , 8608-8619. https://doi.org/10.1021/bi050449a
    50. Jinping Gan,, Timothy W. Harper,, Mei-Mann Hsueh,, Qinling Qu, and, W. Griffith Humphreys. Dansyl Glutathione as a Trapping Agent for the Quantitative Estimation and Identification of Reactive Metabolites. Chemical Research in Toxicology 2005, 18 (5) , 896-903. https://doi.org/10.1021/tx0496791
    51. Montserrat Andújar-Sánchez,, Alex W. Smith,, Josefa María Clemente-Jimenez,, Felipe Rodriguez-Vico,, Francisco Javier Las Heras-Vazquez,, Vicente Jara-Pérez, and, Ana Cámara-Artigas. Crystallographic and Thermodynamic Analysis of the Binding of S-Octylglutathione to the Tyr 7 to Phe Mutant of Glutathione S-Transferase from Schistosoma japonicum,. Biochemistry 2005, 44 (4) , 1174-1183. https://doi.org/10.1021/bi0483110
    52. Christine E. Hand and, John F. Honek. Biological Chemistry of Naturally Occurring Thiols of Microbial and Marine Origin. Journal of Natural Products 2005, 68 (2) , 293-308. https://doi.org/10.1021/np049685x
    53. Alistair P. Henderson,, Martine L. Barnes,, Christine Bleasdale,, Richard Cameron,, William Clegg,, Sarah L. Heath,, Andrew B. Lindstrom,, Stephen M. Rappaport,, Suramya Waidyanatha,, William P. Watson, and, Bernard T. Golding. Reactions of Benzene Oxide with Thiols Including Glutathione. Chemical Research in Toxicology 2005, 18 (2) , 265-270. https://doi.org/10.1021/tx049781y
    54. Yijun Gu,, Jianxia Guo,, Ajay Pal,, Su-Shu Pan,, Piotr Zimniak,, Shivendra V. Singh, and, Xinhua Ji. Crystal Structure of Human Glutathione S-Transferase A3-3 and Mechanistic Implications for Its High Steroid Isomerase Activity,. Biochemistry 2004, 43 (50) , 15673-15679. https://doi.org/10.1021/bi048757g
    55. Johan Viljanen,, Lotta Tegler, and, Kerstin S. Broo. Combinatorial Chemical Reengineering of the Alpha Class Glutathione Transferases. Bioconjugate Chemistry 2004, 15 (4) , 718-727. https://doi.org/10.1021/bc034192+
    56. Richard Svensson,, Johan Alander,, Richard N. Armstrong, and, Ralf Morgenstern. Kinetic Characterization of Thiolate Anion Formation and Chemical Catalysis of Activated Microsomal Glutathione Transferase 1. Biochemistry 2004, 43 (27) , 8869-8877. https://doi.org/10.1021/bi0492511
    57. Yiping Zhan and, Gordon S. Rule. Glutathione Induces Helical Formation in the Carboxy Terminus of Human Glutathione Transferase A1-1. Biochemistry 2004, 43 (23) , 7244-7254. https://doi.org/10.1021/bi0363329
    58. Melissa A. Vargo,, Lucia Nguyen, and, Roberta F. Colman. Subunit Interface Residues of Glutathione S-Transferase A1-1 that Are Important in the Monomer−Dimer Equilibrium. Biochemistry 2004, 43 (12) , 3327-3335. https://doi.org/10.1021/bi030245z
    59. Jane E. Ladner,, James F. Parsons,, Chris L. Rife,, Gary L. Gilliland, and, Richard N. Armstrong. Parallel Evolutionary Pathways for Glutathione Transferases:  Structure and Mechanism of the Mitochondrial Class Kappa Enzyme rGSTK1-1. Biochemistry 2004, 43 (2) , 352-361. https://doi.org/10.1021/bi035832z
    60. Salerwe Mosebi,, Yasien Sayed,, Jonathan Burke, and, Heini W. Dirr. Residue 219 Impacts on the Dynamics of the C-Terminal Region in Glutathione Transferase A1-1:  Implications for Stability and Catalytic and Ligandin Functions. Biochemistry 2003, 42 (51) , 15326-15332. https://doi.org/10.1021/bi035671z
    61. Diana S. Hamilton,, Xiyun Zhang,, Zhebo Ding,, Ina Hubatsch,, Bengt Mannervik,, K. N. Houk,, Bruce Ganem, and, Donald J. Creighton. Mechanism of the Glutathione Transferase-Catalyzed Conversion of Antitumor 2-Crotonyloxymethyl-2-cycloalkenones to GSH Adducts. Journal of the American Chemical Society 2003, 125 (49) , 15049-15058. https://doi.org/10.1021/ja030396p
    62. Sofia Håkansson,, Johan Viljanen, and, Kerstin S. Broo. Programmed Delivery of Novel Functional Groups to the Alpha Class Glutathione Transferases. Biochemistry 2003, 42 (34) , 10260-10268. https://doi.org/10.1021/bi0343525
    63. Kenneth A. Johnson,, Francesco Angelucci,, Andrea Bellelli,, Maxime Hervé,, Josette Fontaine,, Demetrious Tsernoglou,, André Capron,, François Trottein, and, Maurizio Brunori. Crystal Structure of the 28 kDa Glutathione S-Transferase from Schistosoma haematobium. Biochemistry 2003, 42 (34) , 10084-10094. https://doi.org/10.1021/bi034449r
    64. Yijun Gu,, Bing Xiao,, Heather L. Wargo,, Matthew H. Bucher,, Shivendra V. Singh, and, Xinhua Ji. Residues 207, 216, and 221 and the Catalytic Activity of mGSTA1-1 and mGSTA2-2 toward Benzo[a]pyrene-(7R,8S)-diol-(9S,10R)-epoxide,. Biochemistry 2003, 42 (4) , 917-921. https://doi.org/10.1021/bi026778+
    65. Judith A. T. Hornby,, Simona G. Codreanu,, Richard N. Armstrong, and, Heini W. Dirr. Molecular Recognition at the Dimer Interface of a Class Mu Glutathione Transferase:  Role of a Hydrophobic Interaction Motif in Dimer Stability and Protein Function. Biochemistry 2002, 41 (48) , 14238-14247. https://doi.org/10.1021/bi020548d
    66. Simona G. Codreanu,, Jane E. Ladner,, Gaoyi Xiao,, Nina V. Stourman,, David L. Hachey,, Gary L. Gilliland, and, Richard N. Armstrong. Local Protein Dynamics and Catalysis:  Detection of Segmental Motion Associated with Rate-Limiting Product Release by a Glutathione Transferase. Biochemistry 2002, 41 (51) , 15161-15172. https://doi.org/10.1021/bi026776p
    67. Wayne B. Anderson,, Daniel C. Liebler,, Philip G. Board, and, M. W. Anders. Mass Spectral Characterization of Dichloroacetic Acid-Modified Human Glutathione Transferase Zeta. Chemical Research in Toxicology 2002, 15 (11) , 1387-1397. https://doi.org/10.1021/tx025553x
    68. Robert P. Lyon and, William M. Atkins. Kinetic Characterization of Native and Cysteine 112-Modified Glutathione S-Transferase A1-1:  Reassessment of Nonsubstrate Ligand Binding. Biochemistry 2002, 41 (36) , 10920-10927. https://doi.org/10.1021/bi0262810
    69. Lars Ridder,, Ivonne M. C. M. Rietjens,, Jacques Vervoort, and, Adrian J. Mulholland. Quantum Mechanical/Molecular Mechanical Free Energy Simulations of the Glutathione S-Transferase (M1-1) Reaction with Phenanthrene 9,10-Oxide. Journal of the American Chemical Society 2002, 124 (33) , 9926-9936. https://doi.org/10.1021/ja0256360
    70. Hoffman B. M. Lantum,, Philip G. Board, and, M. W. Anders. Kinetics of the Biotransformation of Maleylacetone and Chlorofluoroacetic Acid by Polymorphic Variants of Human Glutathione Transferase Zeta (hGSTZ1-1). Chemical Research in Toxicology 2002, 15 (7) , 957-963. https://doi.org/10.1021/tx010095y
    71. Jiaqin Yao,, Minsun Chang,, Yan Li,, Emily Pisha,, Xuemei Liu,, Dan Yao,, Ebrahim C. Elguindi,, Sylvie Y. Blond, and, Judy L. Bolton. Inhibition of Cellular Enzymes by Equine Catechol Estrogens in Human Breast Cancer Cells:  Specificity for Glutathione S-Transferase P1-1. Chemical Research in Toxicology 2002, 15 (7) , 935-942. https://doi.org/10.1021/tx020018i
    72. Hoffman B. M. Lantum,, Daniel C. Liebler,, Philip G. Board, and, M. W. Anders. Alkylation and Inactivation of Human Glutathione Transferase Zeta (hGSTZ1-1) by Maleylacetone and Fumarylacetone. Chemical Research in Toxicology 2002, 15 (5) , 707-716. https://doi.org/10.1021/tx025503s
    73. Anna Maria Caccuri,, Giovanni Antonini,, Nerino Allocati,, Carmine Di Ilio,, Federica Innocenti,, Francesca De Maria,, Michael W. Parker,, Michele Masulli,, Francesca Polizio,, Giorgio Federici, and, Giorgio Ricci. Properties and Utility of the Peculiar Mixed Disulfide in the Bacterial Glutathione Transferase B1-1. Biochemistry 2002, 41 (14) , 4686-4693. https://doi.org/10.1021/bi0158425
    74. Jonathan G. Krum,, Heather Ellsworth,, Ryan R. Sargeant,, Gregory Rich, and, Scott A. Ensign. Kinetic and Microcalorimetric Analysis of Substrate and Cofactor Interactions in Epoxyalkane:CoM Transferase, a Zinc-Dependent Epoxidase. Biochemistry 2002, 41 (15) , 5005-5014. https://doi.org/10.1021/bi0255221
    75. Ann Gustafsson,, Pär L. Pettersson,, Leif Grehn,, Per Jemth, and, Bengt Mannervik. Role of the Glutamyl α-Carboxylate of the Substrate Glutathione in the Catalytic Mechanism of Human Glutathione Transferase A1-1. Biochemistry 2001, 40 (51) , 15835-15845. https://doi.org/10.1021/bi010429i
    76. Luc Bousset,, Hassan Belrhali,, Ronald Melki, and, Solange Morera. Crystal Structures of the Yeast Prion Ure2p Functional Region in Complex with Glutathione and Related Compounds,. Biochemistry 2001, 40 (45) , 13564-13573. https://doi.org/10.1021/bi011007b
    77. T. Kevin Hitchens,, Bengt Mannervik, and, Gordon S. Rule. Disorder-to-Order Transition of the Active Site of Human Class Pi Glutathione Transferase, GST P1-1. Biochemistry 2001, 40 (39) , 11660-11669. https://doi.org/10.1021/bi010909+
    78. Bryan A. Bernat and, Richard N. Armstrong. Elementary Steps in the Acquisition of Mn2+ by the Fosfomycin Resistance Protein (FosA). Biochemistry 2001, 40 (42) , 12712-12718. https://doi.org/10.1021/bi0114832
    79. Donald E. Nerland,, Jian Cai,, William M. Pierce, Jr., and, Frederick W. Benz. Covalent Binding of Acrylonitrile to Specific Rat Liver Glutathione S-Transferases in Vivo. Chemical Research in Toxicology 2001, 14 (7) , 799-806. https://doi.org/10.1021/tx010002c
    80. Nicole E. Pettigrew,, Edward J. Brush, and, Roberta F. Colman. 3-Methyleneoxindole:  An Affinity Label of Glutathione S-Transferase pi Which Targets Tryptophan 38. Biochemistry 2001, 40 (25) , 7549-7558. https://doi.org/10.1021/bi002840w
    81. Scott A. Ensign. Microbial Metabolism of Aliphatic Alkenes. Biochemistry 2001, 40 (20) , 5845-5853. https://doi.org/10.1021/bi015523d
    82. Minsun Chang,, Young Geun Shin,, Richard B. van Breemen,, Sylvie Y. Blond, and, Judy L. Bolton. Structural and Functional Consequences of Inactivation of Human Glutathione S-Transferase P1-1 Mediated by the Catechol Metabolite of Equine Estrogens, 4-Hydroxyequilenin. Biochemistry 2001, 40 (15) , 4811-4820. https://doi.org/10.1021/bi002513o
    83. Ralf Morgenstern,, Richard Svensson,, Bryan A. Bernat, and, Richard N. Armstrong. Kinetic Analysis of the Slow Ionization of Glutathione by Microsomal Glutathione Transferase MGST1. Biochemistry 2001, 40 (11) , 3378-3384. https://doi.org/10.1021/bi0023394
    84. Galina Polekhina,, Philip G. Board,, Anneke C. Blackburn, and, Michael W. Parker. Crystal Structure of Maleylacetoacetate Isomerase/Glutathione Transferase Zeta Reveals the Molecular Basis for Its Remarkable Catalytic Promiscuity,. Biochemistry 2001, 40 (6) , 1567-1576. https://doi.org/10.1021/bi002249z
    85. Chiara Micaloni,, Anna P. Mazzetti,, Marzia Nuccetelli,, Jamie Rossjohn,, William J. McKinstry,, Giovanni Antonini,, Anna M. Caccuri,, Aaron J. Oakley,, Giorgio Federici,, Giorgio Ricci,, Michael W. Parker, and, Mario Lo Bello. Valine 10 May Act as a Driver for Product Release from the Active Site of Human Glutathione Transferase P1-1,. Biochemistry 2000, 39 (51) , 15961-15970. https://doi.org/10.1021/bi0007122
    86. Richard Svensson,, Rosanna Rinaldi,, Stellan Swedmark, and, Ralf Morgenstern. Reactivity of Cysteine-49 and Its Influence on the Activation of Microsomal Glutathione Transferase 1:  Evidence for Subunit Interaction. Biochemistry 2000, 39 (49) , 15144-15149. https://doi.org/10.1021/bi001764u
    87. Judith A. T. Hornby,, Jiann-Kae Luo,, Julie M. Stevens,, Louise A. Wallace,, Warren Kaplan,, Richard N. Armstrong, and, Heini W. Dirr. Equilibrium Folding of Dimeric Class μ Glutathione Transferases Involves a Stable Monomeric Intermediate. Biochemistry 2000, 39 (40) , 12336-12344. https://doi.org/10.1021/bi000176d
    88. Yijun Gu,, Shivendra V. Singh, and, Xinhua Ji. Residue R216 and Catalytic Efficiency of a Murine Class Alpha Glutathione S-Transferase toward Benzo[a]pyrene 7(R),8(S)-Diol 9(S),10(R)-Epoxide,. Biochemistry 2000, 39 (41) , 12552-12557. https://doi.org/10.1021/bi001396u
    89. Scott A. McCallum,, T. Kevin Hitchens,, Christine Torborg, and, Gordon S. Rule. Ligand-Induced Changes in the Structure and Dynamics of a Human Class Mu Glutathione S-Transferase. Biochemistry 2000, 39 (25) , 7343-7356. https://doi.org/10.1021/bi992767d
    90. Kandiah Anandarajah,, Philip M. Kiefer, Jr.,, Bryon S. Donohoe, and, Shelley D. Copley. Recruitment of a Double Bond Isomerase To Serve as a Reductive Dehalogenase during Biodegradation of Pentachlorophenol. Biochemistry 2000, 39 (18) , 5303-5311. https://doi.org/10.1021/bi9923813
    91. Yury V. Patskovsky,, Larysa N. Patskovska, and, Irving Listowsky. An Asparagine-Phenylalanine Substitution Accounts for Catalytic Differences between hGSTM3-3 and Other Human Class Mu Glutathione S-Transferases,. Biochemistry 1999, 38 (49) , 16187-16194. https://doi.org/10.1021/bi991714t
    92. Heini W. Dirr and, Louise A. Wallace. Role of the C-Terminal Helix 9 in the Stability and Ligandin Function of Class α Glutathione Transferase A1-1. Biochemistry 1999, 38 (47) , 15631-15640. https://doi.org/10.1021/bi991179x
    93. Bing Xiao,, Sharda P. Singh,, Bindu Nanduri,, Yogesh C. Awasthi,, Piotr Zimniak, and, Xinhua Ji. Crystal Structure of a Murine Glutathione S-Transferase in Complex with a Glutathione Conjugate of 4-Hydroxynon-2-enal in One Subunit and Glutathione in the Other:  Evidence of Signaling across the Dimer Interface,. Biochemistry 1999, 38 (37) , 11887-11894. https://doi.org/10.1021/bi990468i
    94. Per Jemth and, Bengt Mannervik. Fast Product Formation and Slow Product Release Are Important Features in a Hysteretic Reaction Mechanism of Glutathione Transferase T2-2. Biochemistry 1999, 38 (31) , 9982-9991. https://doi.org/10.1021/bi983065b
    95. Xinhua Ji,, Jaroslaw Blaszczyk,, Bing Xiao,, Rosemary O'Donnell,, Xun Hu,, Christian Herzog,, Shivendra V. Singh, and, Piotr Zimniak. Structure and Function of Residue 104 and Water Molecules in the Xenobiotic Substrate-Binding Site in Human Glutathione S-Transferase P1-1,. Biochemistry 1999, 38 (32) , 10231-10238. https://doi.org/10.1021/bi990668u
    96. Yury V. Patskovsky,, Larysa N. Patskovska, and, Irving Listowsky. Functions of His107 in the Catalytic Mechanism of Human Glutathione S-Transferase hGSTM1a-1a,. Biochemistry 1999, 38 (4) , 1193-1202. https://doi.org/10.1021/bi982164m
    97. Jibo Wang,, Susanne Bauman, and, Roberta F. Colman. Photoaffinity Labeling of Rat Liver Glutathione S-Transferase, 4-4, by Glutathionyl S-[4-(Succinimidyl)-benzophenone]. Biochemistry 1998, 37 (45) , 15671-15679. https://doi.org/10.1021/bi981381k
    98. Kendra E. Hightower,, Chih-chin Huang,, Patrick J. Casey, and, Carol A. Fierke. H-Ras Peptide and Protein Substrates Bind Protein Farnesyltransferase as an Ionized Thiolate. Biochemistry 1998, 37 (44) , 15555-15562. https://doi.org/10.1021/bi981525v
    99. Eric C. Dietze,, Mark P. Grillo,, Thomas Kalhorn,, Brenda S. Nieslanik,, Claudia M. Jochheim, and, William M. Atkins. Thiol Ester Hydrolysis Catalyzed by Glutathione S-Transferase A1-1. Biochemistry 1998, 37 (42) , 14948-14957. https://doi.org/10.1021/bi981284r
    100. Aaron J. Oakley,, Mario Lo Bello,, Giorgio Ricci,, Giorgio Federici, and, Michael W. Parker. Evidence for an Induced-Fit Mechanism Operating in Pi Class Glutathione Transferases,. Biochemistry 1998, 37 (28) , 9912-9917. https://doi.org/10.1021/bi980323w
    Load more citations

    Pair your accounts.

    Export articles to Mendeley

    Get article recommendations from ACS based on references in your Mendeley library.

    Pair your accounts.

    Export articles to Mendeley

    Get article recommendations from ACS based on references in your Mendeley library.

    You’ve supercharged your research process with ACS and Mendeley!

    STEP 1:
    Click to create an ACS ID

    Please note: If you switch to a different device, you may be asked to login again with only your ACS ID.

    Please note: If you switch to a different device, you may be asked to login again with only your ACS ID.

    Please note: If you switch to a different device, you may be asked to login again with only your ACS ID.

    MENDELEY PAIRING EXPIRED
    Your Mendeley pairing has expired. Please reconnect