Paschoalin V M, Silva J T, Panek A D
Departamento de Bioquimica, Universidade Federal do Rio de Janeiro, Brazil.
Curr Genet. 1989 Aug;16(2):81-7. doi: 10.1007/BF00393399.
Uridine diphosphoglucose is not the sole donor for trehalose synthesis in yeast cells: an ADPG-dependent trehalose synthase, has been identified in mutant strains with undetectable UDPG-dependent trehalose-6-P synthase activity. Genetic and chromatographic studies indicate that the two activities correspond to different proteins. The apparent Km for the nucleotide is similar for both enzymes, and Mg2+ is also required for both activities; however, a striking difference was observed with respect to ATP.Mg activation. This newly determined enzymatic activity in Saccharomyces clarifies previous contradictory results with mutant strains that are able to accumulate trehalose during growth yet whose UDPG-dependent trehalose synthase activity is undetectable in vitro.
在UDPG依赖性海藻糖-6-P合酶活性无法检测到的突变菌株中,已鉴定出一种依赖ADPG的海藻糖合酶。遗传学和色谱研究表明,这两种活性对应于不同的蛋白质。两种酶对核苷酸的表观Km相似,且两种活性都需要Mg2+;然而,在ATP·Mg激活方面观察到了显著差异。酿酒酵母中这种新确定的酶活性澄清了先前与突变菌株相关的矛盾结果,这些突变菌株在生长过程中能够积累海藻糖,但在体外其UDPG依赖性海藻糖合酶活性无法检测到。