FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W2005201301> ?p ?o ?g. }

• W2005201301 endingPage "108" @default.
• W2005201301 startingPage "101" @default.
• W2005201301 abstract "Steady-state kinetics, equilibrium binding, and primary substrate kinetic isotope effect studies revealed that the reduction of crotonyl-CoA by NADH, catalyzed by Haemophilus influenzae enoyl-ACP reductase (FabI), follows a rapid equilibrium random kinetic mechanism with negative interaction among the substrates. Two biphenyl inhibitors, triclosan and hexachlorophene, were studied in the context of the kinetic mechanism. IC50 values for triclosan in the presence and absence of NAD+ were 0.1 ± 0.02 and 2.4 ± 0.02 μM, respectively, confirming previous observations that the E–NAD+ complex binds triclosan more tightly than the free enzyme. Preincubation of the enzyme with triclosan and NADH suggested that the E–NADH complex is the active triclosan binding species as well. These results were reinforced by measurement of binding kinetic transients. Intrinsic protein fluorescence changes induced by binding of 20 μM triclosan to E, E–NADH, E–NAD+, and E–crotonyl-CoA occur at rates of 0.0124 ± 0.001, 0.0663 ± 0.002, 0.412 ± 0.01, and 0.0069 ± 0.0001 s−1, respectively. The rate of binding decreased with increasing crotonyl-CoA concentrations in the E-crotonyl-CoA complex, and the extrapolated rate at zero concentration of crotonyl-CoA corresponded to the rate observed for the binding to the free enzyme. This suggests that triclosan and the acyl substrate share a common binding site. Hexachlorophene inhibition, on the other hand, was NAD+- and time-independent; and the calculated IC50 value was 2.5 ± 0.4 μM. Steady-state inhibition patterns did not allow the mode of inhibition to be unambiguously determined, but binding kinetics suggested that free enzyme, E–NAD+, and E–crotonyl-CoA have similar affinity for hexachlorophene, since the kobss were in the same range of 20–24 s−1. When the E–NADH complex was mixed with hexachlorophene ligand, concentration-independent fluorescence quenching at 480 nm was observed, suggesting at least partial competition between NADH and hexachlorophene for the same binding site. Mutual exclusivity studies, together with the above-discussed results, indicate that triclosan and hexachlorophene bind at different sites of H. influenzae FabI." @default.
• W2005201301 created "2016-06-24" @default.
• W2005201301 creator A5001302659 @default.
• W2005201301 creator A5040723211 @default.
• W2005201301 creator A5067466789 @default.
• W2005201301 creator A5081758034 @default.
• W2005201301 creator A5083181975 @default.
• W2005201301 creator A5087417435 @default.
• W2005201301 date "2001-06-01" @default.
• W2005201301 modified "2023-10-14" @default.
• W2005201301 title "Enoyl-ACP Reductase (FabI) of Haemophilus influenzae: Steady-State Kinetic Mechanism and Inhibition by Triclosan and Hexachlorophene" @default.
• W2005201301 cites W1495055517 @default.
• W2005201301 cites W1501884416 @default.
• W2005201301 cites W1549181422 @default.
• W2005201301 cites W1549345480 @default.
• W2005201301 cites W1669810599 @default.
• W2005201301 cites W1973555080 @default.
• W2005201301 cites W1980648656 @default.
• W2005201301 cites W1983016574 @default.
• W2005201301 cites W2022931899 @default.
• W2005201301 cites W2029472817 @default.
• W2005201301 cites W2029967359 @default.
• W2005201301 cites W2046348365 @default.
• W2005201301 cites W2057120612 @default.
• W2005201301 cites W2065524541 @default.
• W2005201301 cites W2107851387 @default.
• W2005201301 cites W2115132031 @default.
• W2005201301 cites W2117202175 @default.
• W2005201301 cites W2117356421 @default.
• W2005201301 cites W2127229673 @default.
• W2005201301 cites W2128034051 @default.
• W2005201301 cites W2149075105 @default.
• W2005201301 cites W2160175061 @default.
• W2005201301 cites W2969273703 @default.
• W2005201301 doi "https://doi.org/10.1006/abbi.2001.2349" @default.
• W2005201301 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/11368521" @default.
• W2005201301 hasPublicationYear "2001" @default.
• W2005201301 type Work @default.
• W2005201301 sameAs 2005201301 @default.
• W2005201301 citedByCount "32" @default.
• W2005201301 countsByYear W20052013012012 @default.
• W2005201301 countsByYear W20052013012013 @default.
• W2005201301 countsByYear W20052013012015 @default.
• W2005201301 countsByYear W20052013012017 @default.
• W2005201301 countsByYear W20052013012019 @default.
• W2005201301 countsByYear W20052013012020 @default.
• W2005201301 countsByYear W20052013012021 @default.
• W2005201301 countsByYear W20052013012022 @default.
• W2005201301 crossrefType "journal-article" @default.
• W2005201301 hasAuthorship W2005201301A5001302659 @default.
• W2005201301 hasAuthorship W2005201301A5040723211 @default.
• W2005201301 hasAuthorship W2005201301A5067466789 @default.
• W2005201301 hasAuthorship W2005201301A5081758034 @default.
• W2005201301 hasAuthorship W2005201301A5083181975 @default.
• W2005201301 hasAuthorship W2005201301A5087417435 @default.
• W2005201301 hasConcept C134651460 @default.
• W2005201301 hasConcept C142724271 @default.
• W2005201301 hasConcept C178790620 @default.
• W2005201301 hasConcept C181199279 @default.
• W2005201301 hasConcept C185592680 @default.
• W2005201301 hasConcept C18903297 @default.
• W2005201301 hasConcept C2777289219 @default.
• W2005201301 hasConcept C2781289450 @default.
• W2005201301 hasConcept C55493867 @default.
• W2005201301 hasConcept C71240020 @default.
• W2005201301 hasConcept C71924100 @default.
• W2005201301 hasConcept C75520062 @default.
• W2005201301 hasConcept C8171440 @default.
• W2005201301 hasConcept C86803240 @default.
• W2005201301 hasConceptScore W2005201301C134651460 @default.
• W2005201301 hasConceptScore W2005201301C142724271 @default.
• W2005201301 hasConceptScore W2005201301C178790620 @default.
• W2005201301 hasConceptScore W2005201301C181199279 @default.
• W2005201301 hasConceptScore W2005201301C185592680 @default.
• W2005201301 hasConceptScore W2005201301C18903297 @default.
• W2005201301 hasConceptScore W2005201301C2777289219 @default.
• W2005201301 hasConceptScore W2005201301C2781289450 @default.
• W2005201301 hasConceptScore W2005201301C55493867 @default.
• W2005201301 hasConceptScore W2005201301C71240020 @default.
• W2005201301 hasConceptScore W2005201301C71924100 @default.
• W2005201301 hasConceptScore W2005201301C75520062 @default.
• W2005201301 hasConceptScore W2005201301C8171440 @default.
• W2005201301 hasConceptScore W2005201301C86803240 @default.
• W2005201301 hasIssue "1" @default.
• W2005201301 hasLocation W20052013011 @default.
• W2005201301 hasLocation W20052013012 @default.
• W2005201301 hasOpenAccess W2005201301 @default.
• W2005201301 hasPrimaryLocation W20052013011 @default.
• W2005201301 hasRelatedWork W2005201301 @default.
• W2005201301 hasRelatedWork W2012686105 @default.
• W2005201301 hasRelatedWork W2015676956 @default.
• W2005201301 hasRelatedWork W2035298123 @default.
• W2005201301 hasRelatedWork W2058609585 @default.
• W2005201301 hasRelatedWork W2071992344 @default.
• W2005201301 hasRelatedWork W2093331306 @default.
• W2005201301 hasRelatedWork W2975277321 @default.
• W2005201301 hasRelatedWork W2975588464 @default.
• W2005201301 hasRelatedWork W2978574435 @default.

• next