嗜热链球菌中的半乳糖激酶活性。
Galactokinase activity in Streptococcus thermophilus.
作者信息
Hutkins R, Morris H A, McKay L L
出版信息
Appl Environ Microbiol. 1985 Oct;50(4):777-80. doi: 10.1128/aem.50.4.777-780.1985.
Abstract
ATP-dependent phosphorylation of [14C]galactose by 11 strains of Streptococcus thermophilus indicated that these organisms possessed the Leloir enzyme, galactokinase (galK). Activities were 10 times higher in fully induced, galactose-fermenting (Gal+) strains than in galactose-nonfermenting (Gal-) strains. Lactose-grown, Gal- cells released free galactose into the medium and were unable to utilize residual galactose or to induce galK above basal levels. Gal+ S. thermophilus 19258 also released galactose into the medium, but when lactose was depleted growth on galactose commenced, and galK increased from 0.025 to 0.22 micromol of galactose phosphorylated per min per mg of protein. When lactose was added to galactose-grown cells of S. thermophilus 19258, galK activity rapidly decreased. These results suggest that galK in Gal+ S. thermophilus is subject to an induction-repression mechanism, but that galK cannot be induced in Gal- strains.
摘要
11株嗜热链球菌对[14C]半乳糖的ATP依赖性磷酸化作用表明，这些微生物含有Leloir酶——半乳糖激酶（galK）。在完全诱导的半乳糖发酵（Gal+）菌株中，其活性比半乳糖非发酵（Gal-）菌株高10倍。以乳糖为生长底物的Gal-细胞将游离半乳糖释放到培养基中，并且无法利用残留的半乳糖或将galK诱导至基础水平以上。Gal+嗜热链球菌19258也将半乳糖释放到培养基中，但当乳糖耗尽时，开始利用半乳糖生长，galK活性从每分钟每毫克蛋白质磷酸化0.025微摩尔半乳糖增加到0.22微摩尔。当向以半乳糖为生长底物的嗜热链球菌19258细胞中添加乳糖时，galK活性迅速下降。这些结果表明，Gal+嗜热链球菌中的galK受诱导-阻遏机制的调控，但galK在Gal-菌株中无法被诱导。
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