Matches in SemOpenAlex for { <https://semopenalex.org/work/W4233291509> ?p ?o ?g. }
Showing items 1 to 77 of
77
with 100 items per page.
- W4233291509 endingPage "419" @default.
- W4233291509 startingPage "419" @default.
- W4233291509 abstract "Potentiometric, spectroscopic and stopped-flow experiments have been performed to dissect the binding mechanism of GSH to selected glutathione S-transferases (GSTs), A1-1, M2-2 and Lucilia cuprina GST, belonging to Alpha, Mu and Delta classes respectively. Both Alpha and Mu isoenzymes quantitatively release the thiol proton of the substrate when the binary complex is formed. Proton extrusion, quenching of intrinsic fluorescence and thiolate formation, diagnostic of different steps along the binding pathway, have been monitored by stopped-flow analysis. Kinetic data are consistent with a multi-step binding mechanism: the substrate is initially bound to form an un-ionized pre-complex [k1⩾ (2-5)×106 M-1˙s-1], which is slowly converted into the final Michaelis complex (k2 = 1100-1200 s-1). Ionization of GSH, fluorescence quenching and proton extrusion are fast events that occur either synchronously or rapidly after the final complex formation. The Delta isoenzyme shows an interesting difference: proton extrusion is almost stoichiometric with thiolate formed at the active site only up to pH 7.0. Above this pH, at least one protein residue acts as internal base to neutralize the thiol proton. These results suggest that the Alpha and Mu enzymes retain not only a similar catalytic outcome and overall three-dimensional structure but also share a similar kinetic mechanism for GSH binding. The Delta GST, which is closely related to the mammalian Theta class enzymes and is distantly related to Alpha and Mu GSTs in the evolutionary pathway, might display a different activation mechanism for GSH." @default.
- W4233291509 created "2022-05-12" @default.
- W4233291509 creator A5000877030 @default.
- W4233291509 creator A5009225717 @default.
- W4233291509 creator A5013714055 @default.
- W4233291509 creator A5014130762 @default.
- W4233291509 creator A5050377002 @default.
- W4233291509 creator A5061601818 @default.
- W4233291509 creator A5066343783 @default.
- W4233291509 creator A5087504067 @default.
- W4233291509 date "1999-12-01" @default.
- W4233291509 modified "2023-09-27" @default.
- W4233291509 title "Proton release on binding of glutathione to Alpha, Mu and Delta class glutathione transferases" @default.
- W4233291509 doi "https://doi.org/10.1042/0264-6021:3440419" @default.
- W4233291509 hasPublicationYear "1999" @default.
- W4233291509 type Work @default.
- W4233291509 citedByCount "10" @default.
- W4233291509 countsByYear W42332915092012 @default.
- W4233291509 crossrefType "journal-article" @default.
- W4233291509 hasAuthorship W4233291509A5000877030 @default.
- W4233291509 hasAuthorship W4233291509A5009225717 @default.
- W4233291509 hasAuthorship W4233291509A5013714055 @default.
- W4233291509 hasAuthorship W4233291509A5014130762 @default.
- W4233291509 hasAuthorship W4233291509A5050377002 @default.
- W4233291509 hasAuthorship W4233291509A5061601818 @default.
- W4233291509 hasAuthorship W4233291509A5066343783 @default.
- W4233291509 hasAuthorship W4233291509A5087504067 @default.
- W4233291509 hasBestOaLocation W42332915092 @default.
- W4233291509 hasConcept C107824862 @default.
- W4233291509 hasConcept C121332964 @default.
- W4233291509 hasConcept C121745418 @default.
- W4233291509 hasConcept C12554922 @default.
- W4233291509 hasConcept C181199279 @default.
- W4233291509 hasConcept C185592680 @default.
- W4233291509 hasConcept C18903297 @default.
- W4233291509 hasConcept C2777289219 @default.
- W4233291509 hasConcept C538909803 @default.
- W4233291509 hasConcept C55493867 @default.
- W4233291509 hasConcept C62520636 @default.
- W4233291509 hasConcept C71240020 @default.
- W4233291509 hasConcept C86803240 @default.
- W4233291509 hasConcept C91881484 @default.
- W4233291509 hasConceptScore W4233291509C107824862 @default.
- W4233291509 hasConceptScore W4233291509C121332964 @default.
- W4233291509 hasConceptScore W4233291509C121745418 @default.
- W4233291509 hasConceptScore W4233291509C12554922 @default.
- W4233291509 hasConceptScore W4233291509C181199279 @default.
- W4233291509 hasConceptScore W4233291509C185592680 @default.
- W4233291509 hasConceptScore W4233291509C18903297 @default.
- W4233291509 hasConceptScore W4233291509C2777289219 @default.
- W4233291509 hasConceptScore W4233291509C538909803 @default.
- W4233291509 hasConceptScore W4233291509C55493867 @default.
- W4233291509 hasConceptScore W4233291509C62520636 @default.
- W4233291509 hasConceptScore W4233291509C71240020 @default.
- W4233291509 hasConceptScore W4233291509C86803240 @default.
- W4233291509 hasConceptScore W4233291509C91881484 @default.
- W4233291509 hasIssue "2" @default.
- W4233291509 hasLocation W42332915091 @default.
- W4233291509 hasLocation W42332915092 @default.
- W4233291509 hasOpenAccess W4233291509 @default.
- W4233291509 hasPrimaryLocation W42332915091 @default.
- W4233291509 hasRelatedWork W1550154378 @default.
- W4233291509 hasRelatedWork W1739571172 @default.
- W4233291509 hasRelatedWork W2007545289 @default.
- W4233291509 hasRelatedWork W2018038343 @default.
- W4233291509 hasRelatedWork W2058609585 @default.
- W4233291509 hasRelatedWork W2064273003 @default.
- W4233291509 hasRelatedWork W2073859835 @default.
- W4233291509 hasRelatedWork W2159702810 @default.
- W4233291509 hasRelatedWork W2165378040 @default.
- W4233291509 hasRelatedWork W2171854397 @default.
- W4233291509 hasVolume "344" @default.
- W4233291509 isParatext "false" @default.
- W4233291509 isRetracted "false" @default.
- W4233291509 workType "article" @default.