raffinose and isomaltotriose

raffinose has been researched along with isomaltotriose* in 3 studies

Other Studies

3 other study(ies) available for raffinose and isomaltotriose

ArticleYear
The multiple-sugar metabolism (msm) gene cluster of Streptococcus mutans is transcribed as a single operon.
    FEMS microbiology letters, 1996, Jul-01, Volume: 140, Issue:2-3

    The multiple-sugar metabolism (msm) locus of Streptococcus mutans constitutes a non-PTS sugar uptake system responsible for the transport and utilization of raffinose, melibiose and isomaltotrioses. While previous studies have used polar mutations to suggest that these genes are co-transcribed, there has not been evidence to support this. In this report we present direct evidence that the msm genes can be transcribed as a single operon.

    Topics: Base Sequence; Biological Transport, Active; Carbohydrate Metabolism; Carbohydrates; DNA, Bacterial; DNA, Complementary; Genes, Bacterial; Melibiose; Molecular Sequence Data; Multigene Family; Operon; Polymerase Chain Reaction; Raffinose; RNA, Bacterial; Streptococcus mutans; Transcription, Genetic; Trisaccharides

1996
Transport of sugars, including sucrose, by the msm transport system of Streptococcus mutans.
    Journal of dental research, 1993, Volume: 72, Issue:10

    The range of substrates transported by the sugar-binding protein-dependent msm (multiple sugar metabolism) system of S. mutans was investigated. By determining the ability of unlabeled sugar to compete with radiolabeled melibiose transport, we have demonstrated that the transported sugars included a number of carbohydrates structurally related to raffinose. A model accommodating these results has been devised which accounts for the sugars transported by the msm transport system. Competition with radiolabeled melibiose transport indicated sucrose to be an msm substrate. This was confirmed by examination of uptake of radiolabeled sucrose in scrAB mutants lacking the sucrose-specific phosphotransferase system.

    Topics: Biological Transport; Carbohydrate Metabolism; Carbon Radioisotopes; Fructose; Gene Expression Regulation, Bacterial; Glucans; Glucose; Isomaltose; Melibiose; Operon; Raffinose; Streptococcus mutans; Sucrose; Trehalose; Trisaccharides

1993
A binding protein-dependent transport system in Streptococcus mutans responsible for multiple sugar metabolism.
    The Journal of biological chemistry, 1992, Mar-05, Volume: 267, Issue:7

    An 11-kilobase gene region of Streptococcus mutans has been identified which contains eight contiguous genes involved with the uptake and metabolism of multiple sugars (the msm system). Sequence analysis of this region indicates that several of these genes specify proteins with strong homology to components of periplasmic binding protein-dependent transport systems of Gram-negative bacteria. Additionally, this operon is controlled by a regulatory gene (msmR) that acts as a positive effector. The proteins specified by the structural genes of the msm operon include alpha-galactosidase (aga), a "periplasmic-like" sugar-binding protein (msmE), two membrane proteins (msmF, msmG), sucrose phosphorylase (gtfA), an ATP-binding protein (msmK), and dextran glucosidase (dexB). Insertional inactivation of each of these genes along with uptake data indicate that this system is responsible for the uptake of melibiose, raffinose, and isomaltotriose and the metabolism of melibiose, sucrose, and isomaltosaccharides.

    Topics: Amino Acid Sequence; Autoradiography; Bacterial Proteins; Base Sequence; Carbohydrate Metabolism; Chromosomes, Bacterial; Gene Expression; Genes, Bacterial; Genes, Regulator; Melibiose; Molecular Sequence Data; Multigene Family; Plasmids; Raffinose; Sequence Alignment; Streptococcus mutans; Trisaccharides

1992