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S-acetonyl-CoA. A nonreactive analog of acetyl-CoA
Journal article   Open access   Peer reviewed

S-acetonyl-CoA. A nonreactive analog of acetyl-CoA

P Rubenstein and R Dryer
The Journal of biological chemistry, Vol.255(16), pp.7858-7862
08/25/1980
DOI: 10.1016/S0021-9258(19)43913-6
PMID: 6995455
url
https://doi.org/10.1016/S0021-9258(19)43913-6View
Published (Version of record) Open Access

Abstract

We have synthesized S-acetonyl-CoA from CoASH and 1-bromoacetone. This thioether-containing structural analogue of acetyl-CoA is a potent competitive inhibitor, with respect to acetyl-CoA, of citrate synthase, phosphotransacetylase, and carnitine acetyltransferase. This analog will not activate Escherichia coli phosphoenolpyruvate carboxylase or rat liver pyruvate carboxylase, two enzymes which require acetyl-CoA as an obligate activator. Furthermore, acetonyl-CoA will not compete with acetyl-CoA for binding to these enzymes showing the apparent absolute requirement of these two enzymes for a thioester group on the activating ligand. S-Acetonyl-CoA should be a useful reagent in the investigation of acetyl-CoA-requiring processes.
 Animals Carnitine O-Acetyltransferase - antagonists & inhibitors Citrate (si)-Synthase - antagonists & inhibitors Coenzyme A - analogs & derivatives Coenzyme A - chemical synthesis Coenzyme A - pharmacology Enzyme Activation - drug effects Escherichia coli - enzymology Liver - enzymology Phosphate Acetyltransferase - antagonists & inhibitors Phosphoenolpyruvate Carboxylase - antagonists & inhibitors Pyruvate Carboxylase - antagonists & inhibitors Rats

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