Jagusztyn-Krynicka E K, Hansen J B, Crow V L, Thomas T D, Honeyman A L, Curtiss R
Department of Microbiology, University of Alabama, Birmingham 35294.
J Bacteriol. 1992 Oct;174(19):6152-8. doi: 10.1128/jb.174.19.6152-6158.1992.
DNA cloned into Escherichia coli K-12 from a serotype c strain of Streptococcus mutans encodes three enzyme activities for galactose utilization via the tagatose 6-phosphate pathway: galactose 6-phosphate isomerase, tagatose 6-phosphate kinase, and tagatose-1,6-bisphosphate aldolase. The genes coding for the tagatose 6-phosphate pathway were located on a 3.28-kb HindIII DNA fragment. Analysis of the tagatose proteins expressed by recombinant plasmids in minicells was used to determine the sizes of the various gene products. Mutagenesis of these plasmids with transposon Tn5 was used to determine the order of the tagatose genes. Tagatose 6-phosphate isomerase appears to be composed of 14- and 19-kDa subunits. The sizes of the kinase and aldolase were found to be 34 and 36 kDa, respectively. These values correspond to those reported previously for the tagatose pathway enzymes in Staphylococcus aureus and Lactococcus lactis.
从变形链球菌血清型c菌株克隆到大肠杆菌K-12中的DNA编码了三种通过磷酸塔格糖途径利用半乳糖的酶活性:6-磷酸半乳糖异构酶、磷酸塔格糖激酶和1,6-二磷酸塔格糖醛缩酶。编码磷酸塔格糖途径的基因位于一个3.28kb的HindIII DNA片段上。通过分析重组质粒在小细胞中表达的塔格糖蛋白来确定各种基因产物的大小。用转座子Tn5对这些质粒进行诱变,以确定塔格糖基因的顺序。6-磷酸塔格糖异构酶似乎由14kDa和19kDa的亚基组成。发现激酶和醛缩酶的大小分别为34kDa和36kDa。这些值与先前报道的金黄色葡萄球菌和乳酸乳球菌中磷酸塔格糖途径酶的值一致。