Boles E, Zimmermann F K
Institut für Mikrobiologie, Technische Hochschule Darmstadt, Federal Republic of Germany.
Curr Genet. 1993 Mar;23(3):187-91. doi: 10.1007/BF00351494.
Two glycolytic enzymes, phosphoglucose isomerase and fructose-1,6-bisphosphate aldolase, of Saccharomyces cerevisiae could be replaced by their heterologous counterparts from Escherichia coli and Drosophila melanogaster. Both heterologous enzymes, which show respectively little and no sequence homology to the corresponding yeast enzymes, fully restored wild-type properties when their genes were expressed in yeast deletion mutants. This result does not support notions of an obligatory formation of glycolytic multi-enzyme aggregates in yeast; nor does it support possible regulatory functions of yeast phosphoglucose isomerase.
酿酒酵母的两种糖酵解酶，磷酸葡萄糖异构酶和果糖-1,6-二磷酸醛缩酶，可以被来自大肠杆菌和黑腹果蝇的异源对应酶所取代。这两种异源酶与相应的酵母酶分别几乎没有和完全没有序列同源性，当它们的基因在酵母缺失突变体中表达时，完全恢复了野生型特性。这一结果不支持酵母中糖酵解多酶聚集体必然形成的观点；也不支持酵母磷酸葡萄糖异构酶可能的调节功能。
