Insights into the Catalytic Mechanism of Glutathione S-Transferase: The Lesson from Schistosoma haematobium. (Articolo in rivista)

Type

• Prodotto della ricerca (Classe)
• Articolo in rivista (Classe)

Label

• Insights into the Catalytic Mechanism of Glutathione S-Transferase: The Lesson from Schistosoma haematobium. (Articolo in rivista) (literal)

Anno

• 2005-01-01T00:00:00+01:00 (literal)

Alternative label

• Angelucci F; Baiocco P; Brunori M; Gourlay L; Morea V; Bellelli A. (2005)
  Insights into the Catalytic Mechanism of Glutathione S-Transferase: The Lesson from Schistosoma haematobium.
  in Structure (Lond.)
  (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori

• Angelucci F; Baiocco P; Brunori M; Gourlay L; Morea V; Bellelli A. (literal)

Pagina inizio

• 1241 (literal)

Pagina fine

• 1246 (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume

• 13 (literal)

Rivista

• Structure (Rivista)

Note

• ISI Web of Science (WOS) (literal)
• PubMe (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni

• Department of Biochemical Sciences \"A. Rossi Fanelli\", University of Rome \"La Sapienza\", 00185 Rome, Italy; Istituto Pasteur-Fondazione Cenci-Bolognetti, University of Rome \"La Sapienza\", 00185 Rome, Italy; Istituto di Biologia e Patologia Molecolari del CNR, University of Rome \"La Sapienza\", 00185 Rome, Italy; (literal)

Titolo

• Insights into the Catalytic Mechanism of Glutathione S-Transferase: The Lesson from Schistosoma haematobium. (literal)

Abstract

• Glutathione S-transferases (GSTs) are involved in detoxification of xenobiotic compounds and in the biosynthesis of important metabolites. All GSTs activate glutathione (GSH) to GS-; in many GSTs, this is accomplished by a Tyr at H-bonding distance from the sulfur of GSH. The high-resolution structure of GST from Schistosoma haematobium revealed that the catalytic Tyr occupies two alternative positions, one external, involving a pi-cation interaction with the conserved Arg21, and the other inside the GSH binding site. The interaction with Arg21 lowers the pKa of the catalytic Tyr10, as required for catalysis. Examination of several other GST structures revealed the presence of an external pocket that may accommodate the catalytic Tyr, and suggested that the change in conformation and acidic properties of the catalytic Tyr may be shared by other GSTs. Arginine and two other residues of the external pocket constitute a conserved structural motif, clearly identified by sequence comparison. (literal)

Prodotto di

• Institute of molecular biology and pathology (IBPM) (Istituto)
• Analisi di famiglie proteiche e predizione strutturale di proteine modello (SV.P18.004.002) (Modulo)

Autore CNR

• MAURIZIO BRUNORI (Persona)
• VERONICA MOREA (Unità di personale interno)
• ANDREA BELLELLI (Unità di personale esterno)

Incoming links:

Prodotto

• Institute of molecular biology and pathology (IBPM) (Istituto)
• Analisi di famiglie proteiche e predizione strutturale di proteine modello (SV.P18.004.002) (Modulo)

Autore CNR di

• VERONICA MOREA (Unità di personale interno)
• MAURIZIO BRUNORI (Persona)
• ANDREA BELLELLI (Unità di personale esterno)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#rivistaDi

• Structure (Rivista)