Regulation of acetyl-CoA synthetase of Saccharomyces cerevisiae.
Acetyl-coenzyme A synthetase (EC 6.2.1.1) activity of Saccharomyces cerevisiae was determined by a radioactive assay procedure. The activity in vitro was inhibited significantly by NADPH, NADH, or AMP and to a lesser extent by NADP, NAD, or ADP. Glutamic acid and alpha-ketoglutaric acid were not inhibitory. The enzyme level was repressed when the cells were grown in a complex nutrient medium as opposed to the minimal medium. However, a glutamic acid auxotroph glul, when grown in excess glutamic acid, demonstrated a fivefold increase of acetyl-CoA synthetase.
D000106:Acetate-CoA Ligase / Q000037:antagonists & inhibitors / Q000096:biosynthesis* / Q000378:metabolism; D000244:Adenosine Diphosphate / Q000494:pharmacology; D000249:Adenosine Monophosphate / Q000494:pharmacology; D002474:Cell-Free System; D003066:Coenzyme A Ligases / Q000096:biosynthesis*; D004794:Enzyme Repression; D005947:Glucose / Q000378:metabolism; D005971:Glutamates / Q000378:metabolism; D009243:NAD / Q000494:pharmacology; D009249:NADP / Q000494:pharmacology; D012441:Saccharomyces cerevisiae / Q000378:metabolism*
D005971:Glutamates; D009243:NAD; D000249:Adenosine Monophosphate; D009249:NADP; D000244:Adenosine Diphosphate; D003066:Coenzyme A Ligases; D000106:Acetate-CoA Ligase; D005947:Glucose