Levansucrase from Bacillus subtilis

P. Mantsala and M. Puntala, Comparison of levansucrase from Bacillus subtilis and from Bacillus amyloliquefaciens, FEMS Microbiol. Lett., 13 (1982) 395-399. 

Thiosucrose (98) was also a good inhibitor for the two enzymes which act on sucrose, the levansucrase from Bacillus subtilis and the yeast invertase [19]. 

Euzenat O, Guibert A, Combes D. Production of fructooligosaccharides by levansucrase from Bacillus subtilis C4. Process Biochem 1997 32 237-43. 

Levansucrases.—The levansucrase from Bacillus subtilis has an average molecular weight of 5.4 x 10. Estimates of the size and shape of the molecule were comparable with those obtained by electron microscopy. 

Levansucrase is a transfructosylase which converts sucrose to levan , a largely p(2 6)-linked fructofuranose polymer, and has been investigated because of its synthesis by oral bacteria. The levans and dextrans produced from dietary sucrose are sparingly water soluble and contribute to the build-up of dental plaque on the teeth. The enzyme from Bacillus subtilis was shown to have ping-pong kinetics,and the intermediacy of a covalent, fructosylated... 

Nagami, Y. and Tanaka, T., 1986, Molecular cloning and nucleotide sequence of a DNA fragment from Bacillus natto that enhances production of extracellular proteases and levansucrase in Bacillus subtilis, J. Bacteriol., 166 20... 

In Bacillus subtilis and Aerobacter levanicum, levans synthesized with levansucrase (EC 2.4.1.10) are highly branched.197-199 Levansu-crase catalyzes the synthesis from sucrose, as shown in equation 5. 

Bacillus subtilis levansucrase (sucrose 2,6-/8-D-fructan 6-)8-D-fructosyltrans-ferase, EC 2.4.1.10) catalyzes fructosyl transfer from sucrose to levan (154). In the absence of a fructosyl acceptor, the primary reaction is sucrose hydrolysis, although a limited amount of self-initiated levan synthesis occurs as well (155). As with sucrose phosphorylase, acceptor specificity is broad a number of saccharides and other nucleophiles are suitable fructosyl acceptors (154-158). The complete amino acid sequence of the approximately SO-kDa enzyme has been determined by both protein (159) and gene (160) sequence analyses. The three-dimensional structure at 3.8 A reveals a rod- or ellipsoid-shaped protein with a length some four times the diameter (161). 

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