ArticleThe Biochemical journal1996
Molecular cloning and overexpression of a glutathione transferase gene from Proteus mirabilis.
Article in The Biochemical journal, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 50 citations in OpenAlex.
- Environmental resistome-guided development of resistance-tolerant antibiotics.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Dechlorination of polychlorobiphenyl degradation metabolites by a recombinant glutathioneFEBS open bio · 2019Article
- Sepsis: mechanisms of bacterial injury to the patient.Scandinavian journal of trauma, resuscitation and emergency medicine · 2019Review
- Reduced Glutathione Mediates Resistance to H2S Toxicity in Oral Streptococci.Applied and environmental microbiology · 2016Article
- Characterization of a Highly pH Stable Chi-Class Glutathione S-Transferase from Synechocystis PCC 6803.PloS one · 2015Article
- The still mysterious roles of cysteine-containing glutathione transferases in plants.Frontiers in pharmacology · 2014Review
- Crystallization and preliminary X-ray analysis of glutathione transferases from cyanobacteria.Acta crystallographica. Section F, Structural biology and crystallization communications · 2009Article
- Novel class of glutathione transferases from cyanobacteria exhibit high catalytic activities towards naturally occurring isothiocyanates.The Biochemical journal · 2007Article
- Role of Ser11 in the stabilization of the structure of Ochrobactrum anthropi glutathione transferase.The Biochemical journal · 2007Article
- Evolutionarily conserved structural motifs in bacterial GST (glutathione S-transferase) are involved in protein folding and stability.The Biochemical journal · 2006Article
- Contribution of the two conserved tryptophan residues to the catalytic and structural properties of Proteus mirabilis glutathione S-transferase B1-1.The Biochemical journal · 2005Article
- Proteus mirabilis glutathione S-transferase B1-1 is involved in protective mechanisms against oxidative and chemical stresses.The Biochemical journal · 2003Article
- Glutamic acid-65 is an essential residue for catalysis in Proteus mirabilis glutathione S-transferase B1-1.The Biochemical journal · 2002Article
- Evaluation of the role of two conserved active-site residues in beta class glutathione S-transferases.The Biochemical journal · 2000Article
- 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
- Molecular cloning, expression and site-directed mutagenesis of glutathione S-transferase from Ochrobactrum anthropi.The Biochemical journal · 1998Article
- Glutathione S-transferases of the yeast Yarrowia lipolytica have unusually large molecular mass.The Biochemical journal · 1998Article
- Glutathione S-transferase-encoding gene as a potential probe for environmental bacterial isolates capable of degrading polycyclic aromatic hydrocarbons.Applied and environmental microbiology · 1997Article
- Bacterial glutathione S-transferases: what are they good for?Journal of bacteriology · 1997Review
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The structural gene of the Proteus mirabilis glutathione transferase GSTB1-1 (gstB) has been isolated from genomic DNA. A nucleotide sequence determination of gstB predicted a translational product of 203 amino acid residues, perfectly matching the sequence of the previously purified protein [Mignogna, Allocati, Aceto, Piccolomini, Di Ilio, Barra and Martini (1993) Eur. J. Biochem. 211, 421-425]. The P. mirabilis GST sequence revealed 56% identity with the Escherichia coli GST at DNA level and 54% amino acid identity. Similarity has been revealed also with the translation products of the recently cloned gene bphH from Haemophilus influenzae (28% identity) and ORF3 of Burkholderia cepacia (27% identity). Putative promoter sequences with high similarity to the E. coli sigma 70 consensus promoter and to promoters of P. mirabilis cat and glnA genes preceded the ATG of the gstB open reading frame (ORF). gstB was brought under control of the tac promoter and overexpressed in E. coli by induction with isopropyl-beta-D-thiogalactopyranoside and growth at 37 degrees C. The physicochemical and catalytic properties of overexpressed protein were indistinguishable from those of the enzyme purified from P. mirabilis extract. Unlike the GST belonging to Mu and Theta classes, GSTB1-1 was unable to metabolize dichloromethane. The study of the interaction of cloned GSTB1-1 with a number of antibiotics indicates that this enzyme actively participates in the binding of tetracyclines and rifamycin.
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