Levansucrase

This reaction is often used to differentiate between dextransucrase and levansucrase in unknown microbial preparations. 

Jung, H.C., Lebeault, J.M. and Pan, J.G. (1998) Surface display of Zymomonas mobilis levansucrase by using the ice-nucleation protein of Pseudomonas syringae. Nature Biotechnology, 16, 576-580. 

Hestrin and Avineri-Shapiro98 have recently suggested a mechanism for levan production from sucrose and raffinose by levansucrase. The enzyme was used in the form of the autolyzate from A. levanicum (rendered sterile with chloroform and thymol9). This autolyzate was incubated for twenty-four hours at 37° with four volumes of 3% sucrose solution and one volume of phosphate buffer (pH 5.0). 

The specificity of levansucrase98 is dependent not only on the d-fructoside but also on the aldoside residue of the substrate. Neither inulin nor methyl D-fructofuranoside was hydrolyzed by levansucrase, and even when these two substrates were hydrolyzed by inulase (prepared from inulin-fermenting Torula yeast) or by yeast invertase respectively, no levan formation occurred with levansucrase. However, neither methyl D-fructofuranoside nor inulin inhibited levan formation from sucrose by levansucrase. No levan was formed from potassium D-glucose... 

The exact nature of levansucrase activity08 is not clear. It differs in certain respects from invertase, polymerase, fructosaccharase, and phosphorylase. Possibly the aldoside part of the substrate molecule is replaced by an enzyme-linked group, and partial decomposition of this levan precursor to aldose and ketose may furnish the energy necessary for levan synthesis. 

Kinetic Parameters for Sucrose Analogues as Substrates for Levansucrases (Wild-Type and Variant A5)... 

J. Seibel, R. Moraru, S. Gotze, K. Buchholz, S. Na amnieh, A. Pawlowski, and H. J. Hecht, Synthesis of sucrose analogues and the mechanism of action of Bacillus subtilis fructosyltransferase (levansucrase), Carbohydr. Res., 341 (2006) 2335-2349. 

S. Morales-Arrieta, M. E. Rodriguez, L. Segovia, A. Lopez-Munguia, and C. Olvera-Carranza, Identification and functional characterization of levS, a gene encoding for a levansucrase from Leuconostoc mesenteroides NRRL B-512 F, Gene, 376 (2006) 59-67. 

R. Chambert and G. Gonzy-Treboul, Levansucrase of Bacillus subtilis Kinetic and thermodynamic aspects of transfructosylation processes, Eur. J. Biochem., 62 (1976) 55-64. 

G. Meng and K. Fiitterer, Structural framework of lfuctosyl transfer in Bacillus subtilis levansucrase, Nat. Struct. Biol., 10 (2003) 935-941. 

C. Martinez-Fleites, M. Ortiz-Lombardia, T. Pons, N. Tarbouriech, E. J. Taylor, J. G. Arrieta, L. Hernandez, and G. J. Davies, Crystal structure of levansucrase from the Gram-negative bacterium Gluconacetobacter diazotrophicus, Biochem. J., 390 (2005) 19-27. 

A. Homann, R. Biedendieck, S. Gotze, D. Jahn, and J. Seibel, Insights into polymer versus oligosaccharide synthesis Mutagenesis and mechanistic studies of a novel levansucrase from Bacillus megaterium, Biochem. J., 407 (2007) 189-198. 

L. K. Ozimek, S. Kralj, M. J. van der Maarel, and L. Dijkhuizen, The levansucrase and inulosucrase enzymes of Lactobacillus reuteri 121 catalyse processive and non-processive transglycosylation reactions, Microbiology, 152 (2006) 1187-1196. 

L. Hernandez, J. Arrieta, C. Menendez, R. Vazquez, A. Coego, V. Suarez, G. Selman, M. F. Petit-Glatron, and R. Chambert, Isolation and enzymic properties of levansucrase secreted by Acetobacter diazotrophicus SRT4, a bacterium associated with sugar cane, Biochem. J., 309(Pt 1), (1995) 113-118. 

R. Chambert and M. F. Petit-Glatron, Polymerase and hydrolase activities of Bacillus subtilis levansucrase can be separately modulated by site-directed mutagenesis, Biochem. J., 279 (1991) 35—41. 

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

LEVANASE LEVANSUCRASE LEVELING EFFECT LEWIS ACID LEWIS ACIDITY LEWIS BASE LEWIS BASICITY ACIDITY... 

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]. 

Dijkhuizen and coworkers identified and characterized a Lactobacillus levansucrase (systematic name sucrose [6)-P-D-fructofuranosyl-(2 ]n a-D-glucopyranoside 6-P-D-fructosyltransferase EC 2.4.1.10) from L. reuteri strain 121, which could produce a high molecular weight levan polysaccharide from fructose [207]. 

In 1993, suicide by an E. colt containing the npt -sacFL-B suicide cassette (nptll gene encodes kanamycin resistance) was reported (Recorbet et al., 1993). In the absence of sucrose the sacK gene does not induce expression of the sacB gene. To induce cell death, sucrose was added to the soil in which the organism was released. This causes the cells to produce levansucrase (a sacB product), which in turn causes the periplasm of the cells to fill with levan. This leads to cell death by lysis. Sucrose... 

That the same enzyme might catalyze transfer and hydrolytic reactions was suspected early and ultimately shown (16) for levansucrase however, the first clear demonstrations of this capacity in 1950 involved two well known hydrolases, yeast invertase (17, 18) and / -glucosidase (19). 

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