Interpreting the broad substrate specificities of glutathione S-transferases

Chemico-Biological Interactions

Volumn 133, Issue 1-3, 2001, Pages 170-172

  Tchaikovskaya, Tatyana ^a   Patskovsky, Yury V ^a   Federov, Alexander ^a   Almo, Steven C ^a   Girvin, Mark ^a   Listowsky, Irving ^a  

^a ALBERT EINSTEIN COLLEGE OF MEDICINE   (United States)

Author keywords

Catalysis; Glutathione transferase; Substrate reorientation; Thiolate anion

Indexed keywords

EID: 0003129131     PISSN: 00092797     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article

References (9)

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4. Y. Patskovsky, L. Patskovska, I. Listowsky, The enhanced affinity for thiolate anion and activation of enzyme-bound glutathione is governed by an arginine residue of human Mu class glutathione S-transferases, J. Biol. Chem. 272 (2000) 3296-3304.
5. Y. Patskovsky, L. Patskovska, I. Listowsky, Functions of His-107 in the catalytic mechanisms of human glutathione S-transferase hGSTM1a-1a, Biochemistry 38 (1999) 1193-1202.
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7. J.D. Rowe, T. Tchaikovskaya, N. Shintani, I. Listowsky, Selective expression of a glutathione S-transferase subclass during spermatogenesis, J. Androl. 19 (1998) 558-567.
8. Y. Patskovsky, M.Q. Huang, T. Takayama, I. Listowsky, W.R. Pearson, Distinctive structure of the human GSTM3 gene-inverted orientation relative to the Mu-class cluster, Arch. Biochem. Biophys. 361 (1999) 85-93.
9. Y. Patskovsky, L. Patskovska, I. Listowsky, An asparagine-phenylalanine substitution accounts for catalytic differences between hGSTM3-3 and other human class Mu glutathione S-transferases, Biochemistry 38 (1999) 16187-16194.