ArticleThe Biochemical journal1999
The role of tyrosine-9 and the C-terminal helix in the catalytic mechanism of Alpha-class glutathione S-transferases.
Article in The Biochemical journal, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed.
- Structural insights into sigma class glutathione transferase from Taenia solium: Analysis and functional implications.PLoS neglected tropical diseases · 2025Article
- Article
- Investigation of the active site of an unclassified glutathione transferase inJournal of pesticide science · 2020Article
- ESR Resolves the C Terminus Structure of the Ligand-free Human Glutathione S-Transferase A1-1.Biophysical journal · 2018Article
- Regioselective covalent immobilization of catalytically active glutathione S-transferase on glass slides.Bioconjugate chemistry · 2013Article
- Article
- The intersubunit lock-and-key motif in human glutathione transferase A1-1: role of the key residues Met51 and Phe52 in function and dimer stability.The Biochemical journal · 2006Article
- Reciprocal regulation of glutathione S-transferase spliceforms and the Drosophila c-Jun N-terminal kinase pathway components.The Biochemical journal · 2004Article
- Catalytic and structural contributions for glutathione-binding residues in a Delta class glutathione S-transferase.The Biochemical journal · 2004Article
- The anomalous pKa of Tyr-9 in glutathione S-transferase A1-1 catalyzes product release.The Journal of biological chemistry · 2003Article
- Microsomal glutathione S-transferase A1-1 with glutathione peroxidase activity from sheep liver: molecular cloning, expression and characterization.The Biochemical journal · 2001Article
- Contribution of aromatic-aromatic interactions to the anomalous pK(a) of tyrosine-9 and the C-terminal dynamics of glutathione S-transferase A1-1.Biochemistry · 2001Article
- Functional and structural roles of the glutathione-binding residues in maize (Zea mays) glutathione S-transferase I.The Biochemical journal · 2001Article
- The C-terminus of glutathione S-transferase A1-1 is required for entropically-driven ligand binding.Biochemistry · 2001Article
- Lysine: N6-hydroxylase: stability and interaction with ligands.Journal of protein chemistry · 1999Article
Corrections and comments
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Authors and funding
5 authors.
Funding
Abstract
Glutathione S-transferases (GSTs) play a key role in the metabolism of drugs and xenobiotics. To investigate the catalytic mechanism, substrate binding and catalysis by the wild-type and two mutants of GST A1-1 have been studied. Substitution of the 'essential' Tyr(9) by phenylalanine leads to a marked decrease in the k(cat) for 1-chloro-2,4-dinitrobenzene (CDNB), but has no affect on k(cat) for ethacrynic acid. Similarly, removal of the C-terminal helix by truncation of the enzyme at residue 209 leads to a decrease in k(cat) for CDNB, but an increase in k(cat) for ethacrynic acid. The binding of a GSH analogue increases the affinity of the wild-type enzyme for CDNB, and increases the rate of the enzyme-catalysed conjugation of this substrate with the small thiols 2-mercaptoethanol and dithiothreitol. This suggests that GSH binding produces a conformational change which is transmitted to the binding site for the hydrophobic substrate, where it alters both the affinity for the substrate and the catalytic-centre activity ('turnover number') for conjugation, perhaps by increasing the proportion of the substrate bound productively. Neither of these two effects of GSH analogues are seen in the C-terminally truncated enzyme, indicating a role for the C-terminal helix in the GSH-induced conformational change.
Indexed as
Identifiers
10527929PMC1220582What OpenQuestion holds
Registered trials
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