Characterization of the hydrophobic substrate-binding site of the bacterial beta class glutathione transferase from Proteus mirabilis.

doi:10.1093/protein/gzq048

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Article

Characterization of the hydrophobic substrate-binding site of the bacterial beta class glutathione transferase from Proteus mirabilis.

Protein engineering, design & selection : PEDS - 1 Sept 2010

Federici Luca, Masulli Michele, Di Ilio Carmine, Allocati Nerino

Abstract excerpt

Since their discovery, bacterial glutathione (GSH)transferases have been characterized in terms of their ability to catalyse a variety of different reactions on a large set of toxic molecules of xenobiotic or endobiotic origin. Furthermore the contribution of different residues in the GSH-binding site to GSH activation has been extensively investigated. Little is known, however, about the contribution to...

Topics

Bacterial Proteins
Benzene Derivatives
Binding Sites
Circular Dichroism
Enzyme Stability
Glutathione
Glutathione Transferase
Hydrogen-Ion Concentration
Hydrophobic and Hydrophilic Interactions
Kinetics

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Models, Molecular

Mutagenesis, Site-Directed

Mutation

Protein Folding

Proteus mirabilis

Temperature

Source

Open in PubMed

Identifiers

PMID: 20663851
DOI: 10.1093/protein/gzq048

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-20663851-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

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