Studies on Acetyl-coenzyme A Synthetase of Yeast: Inhibition by Long-chain Acyl-coenzyme A Esters
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Long-chain acyl-coenzyme A (CoA) compounds (palmityl, stearyl, and oleyl) were found to be potent inhibitors of acetyl-CoA synthetase (ACS) of Saccharomyces cerevisiae strain LK2G12 from aerobic, but not from nonaerobic, cells. The effectiveness of the inhibitors of the aerobic enzyme was in the following order: palmityl-CoA < stearyl-CoA < oleyl-CoA. Short-chain acyl-CoA compounds (propionyl, butyryl, and valeryl) and long-chain fatty acids had no effect on ACS from either source. The inhibition by oleyl-CoA was found to be dependent on enzyme concentration, whereas the inhibition by palmityl- and stearyl-CoA was independent of ACS concentration. Inhibition by palmityl-CoA was noncompetitive with respect to both acetate and CoA, and with increasing concentration of inhibitor the pattern was sigmoidal, with a Hill value of 3.24. At maximally inhibitory concentrations of palmityl-CoA, a small amount of enzyme activity remained. This noninhibitable enzyme in aerobic cells was shown not to be of nonaerobic origin.
Overexpression of acetyl-CoA synthetase in Saccharomyces cerevisiae increases acetic acid tolerance.
Ding J, Holzwarth G, Penner M, Patton-Vogt J, Bakalinsky A FEMS Microbiol Lett. 2015; 362(3):1-7.
PMID: 25673654 PMC: 4809976. DOI: 10.1093/femsle/fnu042.
Coordination of the dynamics of yeast sphingolipid metabolism during the diauxic shift.
Alvarez-Vasquez F, Sims K, Voit E, Hannun Y Theor Biol Med Model. 2007; 4:42.
PMID: 17974024 PMC: 2203994. DOI: 10.1186/1742-4682-4-42.
Rattray J, Schibeci A, Kidby D Bacteriol Rev. 1975; 39(3):197-231.
PMID: 240350 PMC: 413914. DOI: 10.1128/br.39.3.197-231.1975.
Arginine metabolism in Saccharomyces cerevisiae: subcellular localization of the enzymes.
Jauniaux J, Urrestarazu L, Wiame J J Bacteriol. 1978; 133(3):1096-1107.
PMID: 205532 PMC: 222139. DOI: 10.1128/jb.133.3.1096-1107.1978.
Klein H, JAHNKE L J Bacteriol. 1979; 137(1):179-84.
PMID: 33146 PMC: 218433. DOI: 10.1128/jb.137.1.179-184.1979.