Effects of glutathione on kinetics and structural properties of amphibian BbGSTP1-1.
Effects of glutathione on the kinetics and structural properties of BbGSTP1-1 were investigated. The liganded state BbGSTP1-1 acquires the capacity to bind the hydrophobic molecules more avidly. Thus, GSH-binding produces significant conformational changes on BbGSTP1-1 which are transmitted to the hydrophobic binding site. Fluorescent experiments carried out with glutathione-analog S-methylglutathione suggest that the -SH group of tripeptide is essential for triggering protein conformational changes. It is argued that the capacity of BbGSTP1-1 to be modulated by GSH concentration allows it to play an efficient detoxication action in both aquatic and terrestrial environments.
Pennelli
Alfonso
A
Dipartimento di Scienze Biomediche, Università G. D'Annunzio, Via dei Vestini, 31, I-66013, Chieti, Italy.
Sacchetta
Paolo
P
Catitti
Cesare
C
Amicarelli
Fernanda
F
Di Ilio
Carmine
C
D000818:Animals; D001665:Binding Sites; D002023:Bufo bufo / Q000196:embryology / Q000378:metabolism*; D002352:Carrier Proteins / Q000378:metabolism; D004625:Embryo, Nonmammalian / Q000201:enzymology; D005978:Glutathione / Q000378:metabolism*; D051549:Glutathione S-Transferase pi; D005982:Glutathione Transferase / Q000378:metabolism*; D015801:Helminth Proteins; D007527:Isoenzymes / Q000378:metabolism*; D007700:Kinetics; D008958:Models, Molecular
D002352:Carrier Proteins; D015801:Helminth Proteins; D007527:Isoenzymes; C419583:hydrophobic ligand binding protein, Hymenolepis diminuta; D051549:Glutathione S-Transferase pi; D005982:Glutathione Transferase; D005978:Glutathione