TAILIEUCHUNG - Báo cáo khoa học: Trehalose synthase converts glycogen to trehalose

Trehalose (a,a-1,1-glucosyl-glucose) is essential for the growth of mycobac-teria, and these organisms have three different pathways that can produce trehalose. One pathway involves the enzyme described in the present study, trehalose synthase (TreS), which interconverts trehalose and maltose. | ễFEBS Journal Trehalose synthase converts glycogen to trehalose Yuan-Tseng Pan1 J. D. Carroll2 Naoki Asano3 Irena Pastuszak1 Vineetha K. Edavana1 and Alan D. Elbein1 1 Department of Biochemistry and Molecular Biology University of Arkansas for MedicalSciences Little Rock AR USA 2 Department of Microbiology and Immunology University of Arkansas for MedicalSciences Little Rock AR USA 3 Faculty of PharmaceuticalSciences Hokurika University Kanagawa-machi Kanazawa Japan Keywords amylase glycogen levels growth on trehalose trehalose mutants validoxylamine Correspondence A. D. Elbein Department of Biochemistry and Molecular Biology UAMS 4301 West Markham Street Slot 516 Little Rock AR 72205 USA Fax 1 501 686 8169 Tel 1 501 686 5176 E-mail elbeinaland@ Received 5 March 2008 revised 11 April 2008 accepted 30 April2008 doi Trehalose a a-1 1-glucosyl-glucose is essential for the growth of mycobacteria and these organisms have three different pathways that can produce trehalose. One pathway involves the enzyme described in the present study trehalose synthase TreS which interconverts trehalose and maltose. We show that TreS from Mycobacterium smegmatis as well as recombinant TreS produced in Escherichia coli has amylase activity in addition to the maltose M trehalose interconverting activity referred to as MTase . Both activities were present in the enzyme purified to apparent homogeneity from extracts of Mycobacterium smegmatis and also in the recombinant enzyme produced in E. coli from either the M. smegmatis or the Mycobacterium tuberculosis gene. Furthermore when either purified or recombinant TreS was chromatographed on a Sephacryl S-200 column both MTase and amylase activities were present in the same fractions across the peak and the ratio of these two activities remained constant in these fractions. In addition crystals of TreS also contained both amylase and MTase activities. TreS produced both radioactive maltose and .

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