Lobo Z
J Bacteriol. 1984 Oct;160(1):222-6. doi: 10.1128/jb.160.1.222-226.1984.
Six mutants lacking the glycolytic enzyme fructose 1,6-bisphosphate aldolase have been isolated in the yeast Saccharomyces cerevisiae by inositol starvation. The mutants grown on gluconeogenic substrates, such as glycerol or alcohol, and show growth inhibition by glucose and related sugars. The mutations are recessive, segregate as one gene in crosses, and fall in a single complementation group. All of the mutants synthesize an antigen cross-reacting to the antibody raised against yeast aldolase. The aldolase activity in various mutant alleles measured as fructose 1,6-bisphosphate cleavage is between 1 to 2% and as condensation of triose phosphates to fructose 1,6-bisphosphate is 2 to 5% that of the wild-type. The mutants accumulate fructose 1,6-bisphosphate from glucose during glycolysis and dihydroxyacetone phosphate during gluconeogenesis. This suggests that the aldolase activity is absent in vivo.
通过肌醇饥饿法，在酿酒酵母中分离出了六个缺乏糖酵解酶果糖1,6 -二磷酸醛缩酶的突变体。这些突变体在糖异生底物（如甘油或乙醇）上生长，并表现出对葡萄糖及相关糖类的生长抑制。这些突变是隐性的，在杂交中作为一个基因分离，且属于一个单一的互补群。所有突变体都能合成一种与针对酵母醛缩酶产生的抗体发生交叉反应的抗原。以果糖1,6 -二磷酸裂解来衡量，各种突变等位基因中的醛缩酶活性为野生型的1%至2%，而以磷酸丙糖缩合成果糖1,6 -二磷酸来衡量则为野生型的2%至5%。在糖酵解过程中，这些突变体从葡萄糖中积累果糖1,6 -二磷酸，在糖异生过程中积累磷酸二羟丙酮。这表明体内不存在醛缩酶活性。
