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• W1520718042 abstract "Acyl dithioesters of CoA have been synthesized by transesterification. The α-hydrogens have a spectrally determined pKa of 12.5 ± 0.14. The hydroxide catalyzed enolization rate is estimated to be 600 M−1·s−1. The absorbance of the dithioester, λmax = 306 nm, can be used to monitor both the condensation and transesterification reactions that use CoA-Ac as a substrate. For citrate synthase at pH 7.4 Vmax = (4.0 ± 0.4) · 10−4 s−1 and Km = 53 ± 7.5 μM, which are 2·10−6 and 3.3-times the Vmax and Km values observed for CoAS-Ac, while for Ac-CoA:choline O-acetyltransferase (EC 2.3.1.6) at pH 7.0 Vmax = (1.1 ± 0.2) · 10−2 μmol·s−1·(mg protein)−1 and Km = 83 ± 33 μM, which are 0.077 and 10-times the values observed with CoAS-Ac, respectively. The CoA dithioesters are stable at low pH, but hydrolyze with a second-order rate constant of 8.2·10−2 M−1·s−1 at pH 11.4. The spectral properties of these dithioesters should allow these analogs to be used as probes of the structure of enzyme bound intermediates." @default.
• W1520718042 created "2016-06-24" @default.
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• W1520718042 date "1988-01-01" @default.
• W1520718042 modified "2023-10-18" @default.
• W1520718042 title "Coenzyme A dithioesters: synthesis, characterization and reaction with citrate synthase and acetyl-CoA:choline" @default.
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• W1520718042 doi "https://doi.org/10.1016/0167-4838(88)90126-4" @default.
• W1520718042 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/3337828" @default.
• W1520718042 hasPublicationYear "1988" @default.
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