Molecular cloning and characterization of scrB, the structural gene for the Streptococcus mutans phosphoenolpyruvate-dependent sucrose phosphotransferase system sucrose-6-phosphate hydrolase
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چکیده
منابع مشابه
Characterization of a phosphoenolpyruvate-dependent sucrose phosphotransferase system in Streptococcus mutans.
A phosphoenolpyruvate-dependent sucrose phosphotransferase system has been identified in Streptococcus mutans. Sucrose phosphotransferase activity was inducible by sucrose and had an apparent Km for sucrose of 70 microM. The product of the sucrose phosphotransferase reaction was isolated and identified as sucrose phosphate. Additional analysis revealed that the phosphate group was on the glucos...
متن کاملRegulation of sucrose-6-phosphate hydrolase activity in Streptococcus mutans: characterization of the scrR gene.
Previous results have implicated an important role for the enzyme IIScr, the sucrose-specific permease, in the transport of sucrose by cariogenic Streptococcus mutans. The product of the scrB gene, sucrose-6-phosphate hydrolase (Suc-6PH), is required for the metabolism of phosphorylated sucrose. The results from the utilization of scrB::lacZ fusions in S. mutans GS-5 have suggested that sucrose...
متن کاملPhosphoenolpyruvate-dependent sucrose phosphotransferase activity in five serotypes of Streptococcus mutans.
An inducible phosphoenolpyruvate-dependent sucrose phosphotransferase system has been demonstrated in decryptified cell suspensions of the various common serotypes of the cariogenic microorganism Streptococcus mutans.
متن کاملComprehensive mutational analysis of sucrose-metabolizing pathways in Streptococcus mutans reveals novel roles for the sucrose phosphotransferase system permease.
Sucrose is perhaps the most efficient carbohydrate for the promotion of dental caries in humans, and the primary caries pathogen Streptococcus mutans encodes multiple enzymes involved in the metabolism of this disaccharide. Here, we engineered a series of mutants lacking individual or combinations of sucrolytic pathways to understand the control of sucrose catabolism and to determine whether as...
متن کاملA phosphoenolpyruvate-dependent phosphotransferase system is the principal maltose transporter in Streptococcus mutans.
We report that a phosphoenolpyruvate-dependent phosphotransferase system, MalT, is the principal maltose transporter for Streptococcus mutans. MalT also contributes to maltotriose uptake. Since maltose and maltodextrins are products of starch degradation found in saliva, the ability to take up and ferment these carbohydrates may contribute to dental caries.
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ژورنال
عنوان ژورنال: Journal of Bacteriology
سال: 1986
ISSN: 0021-9193,1098-5530
DOI: 10.1128/jb.166.2.426-434.1986