ArticleThe Biochemical journal1995
Evidence for an essential serine residue in the active site of the Theta class glutathione transferases.
Article in The Biochemical journal, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed, 125 citations in OpenAlex.
- Identification and Characterization of the Detoxification Genes from the Transcriptome ofInsects · 2026Article
- A Novel GlutathioneToxins · 2021Article
- Functional Analysis of an Epsilon-Class Glutathione S-Transferase From Nilaparvata lugens (Hemiptera: Delphacidae).Journal of insect science (Online) · 2019Article
- Single-Nucleotide Polymorphisms (SNP) Mining and Their Effect on the Tridimensional Protein Structure Prediction in a Set of Immunity-Related Expressed Sequence Tags (EST) in Atlantic Salmon (Frontiers in genetics · 2019Article
- Dead-end complex, lipid interactions and catalytic mechanism of microsomal glutathione transferase 1, an electron crystallography and mutagenesis investigation.Scientific reports · 2017Article
- Biochemical characterization of an unclassified glutathioneJournal of pesticide science · 2016Article
- Inactivation of Anopheles gambiae Glutathione Transferase ε2 by Epiphyllocoumarin.Biochemistry research international · 2016Article
- Article
- Highlighting a π-π interaction: a protein modeling and molecular dynamics simulation study on Anopheles gambiae glutathione S-transferase 1-2.Journal of molecular modeling · 2013Article
- Structures of yeast glutathione-S-transferase Gtt2 reveal a new catalytic type of GST family.EMBO reports · 2009Article
- Glutathione transferases are structural and functional outliers in the thioredoxin fold.Biochemistry · 2009Article
- An atlas of the thioredoxin fold class reveals the complexity of function-enabling adaptations.PLoS computational biology · 2009Article
- A gene from Aspergillus nidulans with similarity to URE2 of Saccharomyces cerevisiae encodes a glutathione S-transferase which contributes to heavy metal and xenobiotic resistance.Applied and environmental microbiology · 2002Article
- Structure, function and evolution of glutathione transferases: implications for classification of non-mammalian members of an ancient enzyme superfamily.The Biochemical journal · 2001Review
- The crystal structure of the nitrogen regulation fragment of the yeast prion protein Ure2p.Proceedings of the National Academy of Sciences of the United States of America · 2001Article
- A genomics approach to the comprehensive analysis of the glutathione S-transferase gene family in soybean and maize.Plant physiology · 2000Article
- Characterization of the gene cluster involved in isoprene metabolism in Rhodococcus sp. strain AD45.Journal of bacteriology · 2000Article
- Proton release on binding of glutathione to alpha, Mu and Delta class glutathione transferases.The Biochemical journal · 1999Article
- Expression of two glutathione S-transferase genes in the yeast Issatchenkia orientalis is induced by o-dinitrobenzene during cell growth arrest.Journal of bacteriology · 1999Article
- Gene structure, expression and chromosomal localization of murine theta class glutathione transferase mGSTT1-1.The Biochemical journal · 1999Article
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A consistent feature of the Alpha-, Mu- and Pi-class glutathione transferases (GSTs) is the presence near the N-terminus of a tyrosine residue that contributes to the activation of glutathione. While this residue appears to be conserved in many Theta-class GSTs, its absence in some suggested that the Theta-class GSTs may have a significantly different structure or catalytic mechanism. The elucidation of the crystal structure of the Theta-class GST from the Australian sheep blowfly, Lucilia cuprina, has indicated that a serine residue rather than a tyrosine residue can form a hydrogen bond with the glutathionyl sulphur atom. The present studies show that mutation of Ser-9 to alanine substantially inactivates the L. cuprina GST, confirming its importance in the reaction mechanism. As this serine is conserved in all Theta-class enzymes reported so far, it seems that an active-site serine is a significant factor that distinguishes the Theta-class GSTs from members of the Alpha-, Mu- and Pi-class isoenzymes.
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