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- Title
Characterization of the hydrophobic substrate-binding site of the bacterial beta class glutathione transferase from Proteus mirabilis.
- Authors
Federici, Luca; Masulli, Michele; Di Ilio, Carmine; Allocati, Nerino
- Abstract
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 catalysis and overall stability of single residues shaping the hydrophobic co-substrate binding site (H-site). Here we tackle this problem by site-directed mutagenesis of residues facing the H-site in the bacterial beta class GSH transferase from Proteus mirabilis. We investigate the behaviour of these mutants under a variety of conditions and analyse their activity against several co-substrates, representative of the different reactions catalyzed by bacterial GSH transferases. Our work shows that mutations at the H-site can be used to modulate activity at the level of the different catalytic mechanisms operating on the chosen substrates, each mutation showing a different fingerprint. This work paves the way for future studies aimed at improving the catalytic properties of beta class GSH transferases against selected substrates for bioremediation purposes.
- Subjects
GLUTATHIONE transferase; DETOXIFICATION (Alternative medicine); BINDING sites; MOLECULES; MUTAGENESIS
- Publication
PEDS: Protein Engineering, Design & Selection, 2010, Vol 23, Issue 9, p743
- ISSN
1741-0126
- Publication type
Article
- DOI
10.1093/protein/gzq048