de Jong-Gubbels P, van den Berg M A, Steensma H Y, van Dijken J P, Pronk J T
Department of Microbiology and Enzymology, Kluyver Laboratory of Biotechnology, Delft University of Technology, The Netherlands.
FEMS Microbiol Lett. 1997 Aug 1;153(1):75-81. doi: 10.1111/j.1574-6968.1997.tb10466.x.
In Saccharomyces cerevisiae, the structural genes ACS1 and ACS2 each encode an isoenzyme of acetyl-CoA synthetase (ACS; EC 6.2.1.1). Involvement of glucose catabolite repression in regulation of the two isoenzymes was investigated by following ACS activity after glucose pulses (100 mM) to ethanol-limited chemostat cultures. In wild-type S. cerevisiae and in an isogenic strain in which ACS2 had been disrupted, ACS activity decreased after a glucose pulse. No such inactivation was observed in a strain in which ACS1 was disrupted. Western blots demonstrated that the ACS1 product, but not the ACS2 product, was degraded after a glucose pulse. Inactivation kinetics of the ACS1 product resembled those of isocitrate lyase.
在酿酒酵母中,结构基因ACS1和ACS2各自编码一种乙酰辅酶A合成酶(ACS;EC 6.2.1.1)的同工酶。通过在乙醇限制的恒化器培养物中施加葡萄糖脉冲(100 mM)后跟踪ACS活性,研究了葡萄糖分解代谢物阻遏对这两种同工酶的调控作用。在野生型酿酒酵母和ACS2已被破坏的同基因菌株中,葡萄糖脉冲后ACS活性降低。在ACS1被破坏的菌株中未观察到这种失活现象。蛋白质免疫印迹表明,葡萄糖脉冲后ACS1的产物被降解,而ACS2的产物未被降解。ACS1产物的失活动力学与异柠檬酸裂解酶相似。