6-glucosyltransferase

Various strains of oral streptococci produce D-glucosyltransferases which utilize sucrose as a o-glucosyl donor in the production of soluble and insoluble D-glucans. Consequently, it may be expected that some deoxyfluoro derivatives of sucrose function as competitive inhibitors for the dextransu-crases of tooth bacteria, thus preventing decay, or at least may be used as active-site probes for the enzymes. Another aim of these researches is to find non-metabolizable sweeteners. 

Vogt, T., Substrate specificity and sequence analysis define a polyphyletic origin of betanidin 5- and 6-0-glucosyltransferase from Dorotheanthus bellidiformis, Planta, 214, 492, 2002. 

Sasaki, N. et al.. Detection of UDP-glucose cyclo-DOPA 5-O-glucosyltransferase activity in four o clocks (Mirabilis jalapa L.), EEBS Lett, 568, 159, 2004. 

Sasaki, N. et al., Isolation and characterization of cDNAs encoding an enzyme with glucosyltransferase activity for cyc/o-dopa from four o clocks and feather cockscombs, Plant Cell Physiol., 46, 666, 2005. 

Mutans streptococci are the major pathogenic organisms of dental caries in humans. The pathogenicity is closely related to production of extracellular, water-insoluble glucans from sucrose by glucosyltransferase and acid release from various fermentable sugars. Poly(catechin) obtained by HRP catalyst in a phosphate buffer (pH 6) markedly inhibited glucosyltransferase from Streptococcus sorbrinus 6715, whereas the inhibitory effect of catechin for this enzyme was very low. 

Parry, A. D. and Edwards, R. (1994). Characterization of o-glucosyltransferases with activities toward phenolic substrates in alfalfa. Phytochemistry 37 655-661. Phamdelegue, M. H., Loublier, Y., Ducruet, V., Douault, P., Marilleau, R. and Etievant, P. (1994). Characterization of chemicals involved in honeybee-plant interactions. Grana 33 184-190. 

M. Remaud-Simeon, A. Lopez-Munguia, V. Pelenc, F. Paul, and P. Monsan, Production and use of glucosyltransferases from Leuconostoc mesenteroides NRRL B-1299 for the synthesis of oligosaccharides containing a-(l >2) linkages, Appl. Biochem. Biotechnol., 44 (1994) 101-117. 

J. J. Ferretti, M. L. Gilpin, and R. R. Russell, Nucleotide sequence of a glucosyltransferase gene from Streptococcus sobrinus MFe28, J. Bacteriol., 169 (1987) 4271 1278. 

S. Kralj, G. H. van Geel-Schutten, H. Rahaoui, R. J. Leer, E. J. Faber, M. J. van der Maarel, and L. Dijkhuizen, Molecular characterization of a novel glucosyltransferase from Lactobacillus reuteri strain 121 synthesizing a unique, highly branched glucan with a-(l —>4) and a-(l —>6) glucosidic bonds, Appl. Environ. Microbiol, 68 (2002) 4283 1291. 

T. Fujiwara, T. Hoshino, T. Ooshima, S. Sobue, and S. Hamada, Purification, characterization, and molecular analysis of the gene encoding glucosyltransferase from Streptococcus oralis, Infect. Immun., 68 (2000) 2475-2483. 

Figure 5.4. Abbreviated scheme for biosynthesis of major flavonoid subclasses, showing the primary enzymes and substrates leading to different subclasses. Bold-faced, uppercase abbreviations refer to enzyme names, whereas substrate names are presented in lowercase letters. PAL, phenylalanine ammonia lyase C4H, cinnamate 4-hydroxylase 4CL, 4-coumarate CoA ligase CHS, chalcone synthase CHI, chalcone isomerase CHR, chalcone reductase IPS, isoflavone synthase F3H, flavonone 3-hydroxylase F3 H, flavonoid 3 -hydroxylase F3 5 H, flavonoid 3 5 -hydroxylase FNSI/II, flavone synthase DFR, dihydroflavonol 4-reductase FLS, flavonol synthase ANS, anthocyanidin synthase LAR, leucoanthocyanidin reductase ANR, anthocyanidin reductase UFGT, UDP-glucose flavonoid 3-O-glucosyltransferase. R3 = H or OH. R5 = H or OH. Glc = glucose. Please refer to text for more information.

CL, 4-coumarate CoA ligase CHS, chalcone synthase CHI, chalcone isomerase F3H, flavanone 3-hydroxylase DFR, dihydroflavonol 4-reductase ANS, anthocyanidin synthase FGT, flavonoid 3-O-glucosyltransferase. 

REED, D.W., DAVIN, L JAIN, J.C., DELUCA, V., NELSON, L., UNDERHILL, E.W., Purification and properties of UDP-glucose thiohydroximate glucosyltransferase from Brassica napus L. seedlings, Arch. Biochem. Biophys., 1993,305,526-532. 

GUO, L., POULTON, J.E., Partial purification and characterization of Arabidopsis thaliana UDPG Thiohydroximate glucosyltransferase, Phytochemistry, 1994, 36, 1133-1138. 

JONES, P.R., M0LLER, B.L., H0J, P.B. The UDP-glucose p-Hydroxymandelonitrile-O-glucosyltransferase that catalyzes the last step in synthesis of the cyanogenic glucoside dhurrin in Sorghum bicolor, J. Biol. Chem., 1999, 274,35483-35491. 

Offen W, Martinez-Fleites C, Yang M, Kiat-Lim E, Davis BG, Tarling CA, Ford CM, Bowles DJ, Davies GJ (2006) Structure of a flavonoid glucosyltransferase reveals the basis for plant natural product modification. EMBO J 25 1396-1405... 

Me(3ner B, Thulke O, Schaffner AR (2003) Arabidopsis glucosyltransferases with activities toward both endogeneous and xenobiotic substrates. Planta 217 138-146... 

Brazier M, Cole DJ, Edwards R (2002) O-Glucosyltransferase activities toward phenolic natural products and xenobiotics in wheat and herbicide-resistant and herbicide-susceptible black-grass (Alopecurus myosuroides). Phytochemistry 59 149-156... 

Yue, C.-J., and Zhong, J.-J. (2005). Purification and characterisation of UDPG Ginsenoside Rd glucosyltransferase from suspended cells of Panax notoginseng. Process Biochem. 40, 3742-3748. 

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