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Volumn 34, Issue 2, 2016, Pages 88-111

Sucrose synthase: A unique glycosyltransferase for biocatalytic glycosylation process development

Author keywords

Glycobiotechnology; Glycosides; Glycosylation; Glycosyltransferase; Natural products; Nucleoside diphosphate recycling; Nucleotide activated sugars; Sucrose synthase

Indexed keywords

BIOCATALYSTS; BIOMOLECULES; CATALYSIS; COST EFFECTIVENESS; ENZYMES; FRUCTOSE; GLUCOSE; GLYCOSIDES; GLYCOSYLATION; REACTION INTERMEDIATES; SUGARS; SYNTHESIS (CHEMICAL);

EID: 84958111998     PISSN: 07349750     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.biotechadv.2015.11.003     Document Type: Review
Times cited : (170)

References (189)
  • 1
    • 84863787892 scopus 로고    scopus 로고
    • No evidence for the occurrence of substrate inhibition of Arabidopsis thaliana sucrose synthase-(AtSUS1) by fructose and UDP-glucose
    • Almagro G., Baroja-Fernández E., Muñoz F.J., Bahaji A., Etxeberria E., Li J., et al. No evidence for the occurrence of substrate inhibition of Arabidopsis thaliana sucrose synthase-(AtSUS1) by fructose and UDP-glucose. Plant Signal. Behav. 2012, 7:799-802.
    • (2012) Plant Signal. Behav. , vol.7 , pp. 799-802
    • Almagro, G.1    Baroja-Fernández, E.2    Muñoz, F.J.3    Bahaji, A.4    Etxeberria, E.5    Li, J.6
  • 2
    • 0033134235 scopus 로고    scopus 로고
    • Purification of tomato sucrose synthase phosphorylated isoforms by Fe(III)-immobilized metal affinity chromatography
    • Anguenot R., Yelle S., Nguyen-Quoc B. Purification of tomato sucrose synthase phosphorylated isoforms by Fe(III)-immobilized metal affinity chromatography. Arch. Biochem. Biophys. 1999, 365:163-169.
    • (1999) Arch. Biochem. Biophys. , vol.365 , pp. 163-169
    • Anguenot, R.1    Yelle, S.2    Nguyen-Quoc, B.3
  • 3
    • 84933073715 scopus 로고    scopus 로고
    • Reaction mechanisms in carbohydrate-active enzymes: glycoside hydrolases and glycosyltransferases. Insights from ab initio quantum mechanics/molecular mechanics dynamic simulations
    • Ardevol A., Rovira C. Reaction mechanisms in carbohydrate-active enzymes: glycoside hydrolases and glycosyltransferases. Insights from ab initio quantum mechanics/molecular mechanics dynamic simulations. J. Am. Chem. Soc. 2015, 137:7528-7547.
    • (2015) J. Am. Chem. Soc. , vol.137 , pp. 7528-7547
    • Ardevol, A.1    Rovira, C.2
  • 4
    • 0036009917 scopus 로고    scopus 로고
    • Rice SPK, a calmodulin-like domain protein kinase, is required for storage product accumulation during seed development. Phosphorylation of sucrose synthase is a possible factor
    • Asano T., Kunieda N., Omura Y., Ibe H., Kawasaki T., Takano M., et al. Rice SPK, a calmodulin-like domain protein kinase, is required for storage product accumulation during seed development. Phosphorylation of sucrose synthase is a possible factor. Plant Cell 2002, 14:619-628.
    • (2002) Plant Cell , vol.14 , pp. 619-628
    • Asano, T.1    Kunieda, N.2    Omura, Y.3    Ibe, H.4    Kawasaki, T.5    Takano, M.6
  • 5
    • 0343726476 scopus 로고
    • Sucrose-uridine diphosphate glucosyltransferase from Jerusalem artichoke tubers
    • Avigad G. Sucrose-uridine diphosphate glucosyltransferase from Jerusalem artichoke tubers. J. Biol. Chem. 1964, 239:3613-3618.
    • (1964) J. Biol. Chem. , vol.239 , pp. 3613-3618
    • Avigad, G.1
  • 6
    • 0012645246 scopus 로고
    • UDP-glucose: fructose transglucosylase from sugar beet roots
    • Avigad G., Milner Y. UDP-glucose: fructose transglucosylase from sugar beet roots. Methods Enzymol. 1966, 8:341-345.
    • (1966) Methods Enzymol. , vol.8 , pp. 341-345
    • Avigad, G.1    Milner, Y.2
  • 8
    • 84862907757 scopus 로고    scopus 로고
    • Sucrose synthase activity in the sus1/sus2/sus3/sus4 Arabidopsis mutant is sufficient to support normal cellulose and starch production
    • Baroja-Fernández E., Muñoz F.J., Li J., Bahaji A., Almagro G., Montero M., et al. Sucrose synthase activity in the sus1/sus2/sus3/sus4 Arabidopsis mutant is sufficient to support normal cellulose and starch production. Proc. Natl. Acad. Sci. 2012, 109:321-326.
    • (2012) Proc. Natl. Acad. Sci. , vol.109 , pp. 321-326
    • Baroja-Fernández, E.1    Muñoz, F.J.2    Li, J.3    Bahaji, A.4    Almagro, G.5    Montero, M.6
  • 11
    • 0242549961 scopus 로고
    • Synthesis of disaccharides with pea preparations
    • Bean R.C., Hassid W.Z. Synthesis of disaccharides with pea preparations. J. Am. Chem. Soc. 1955, 77:5737-5738.
    • (1955) J. Am. Chem. Soc. , vol.77 , pp. 5737-5738
    • Bean, R.C.1    Hassid, W.Z.2
  • 13
    • 0035903833 scopus 로고    scopus 로고
    • Chemo-enzymatic synthesis of the Galili epitope Galα(→ 3)Galβ(→ 4)GlcNAc on a homogeneously soluble PEG polymer by a multi-enzyme system
    • Brinkmann N., Malissard M., Ramuz M., Römer U., Schumacher T., Berger E.G., et al. Chemo-enzymatic synthesis of the Galili epitope Galα(→ 3)Galβ(→ 4)GlcNAc on a homogeneously soluble PEG polymer by a multi-enzyme system. Bioorg. Med. Chem. Lett. 2001, 11:2503-2506.
    • (2001) Bioorg. Med. Chem. Lett. , vol.11 , pp. 2503-2506
    • Brinkmann, N.1    Malissard, M.2    Ramuz, M.3    Römer, U.4    Schumacher, T.5    Berger, E.G.6
  • 14
    • 84943338897 scopus 로고    scopus 로고
    • Comparison of broad-scope assays of nucleotide sugar-dependent glycosyltransferases
    • Bubner P., Czabany T., Luley-Goedl C., Nidetzky B. Comparison of broad-scope assays of nucleotide sugar-dependent glycosyltransferases. Anal. Biochem. 2015, 490:46-51.
    • (2015) Anal. Biochem. , vol.490 , pp. 46-51
    • Bubner, P.1    Czabany, T.2    Luley-Goedl, C.3    Nidetzky, B.4
  • 15
    • 0032821706 scopus 로고    scopus 로고
    • Enzymatic synthesis of nucleotide sugars
    • Bülter T., Elling L. Enzymatic synthesis of nucleotide sugars. Glycoconj. J. 1999, 16:147-159.
    • (1999) Glycoconj. J. , vol.16 , pp. 147-159
    • Bülter, T.1    Elling, L.2
  • 16
    • 0344110509 scopus 로고    scopus 로고
    • Chemoenzymatic synthesis of UDP-N-acetyl-α-d-galactosamine
    • Bülter T., Wandrey C., Elling L. Chemoenzymatic synthesis of UDP-N-acetyl-α-d-galactosamine. Carbohydr. Res. 1997, 305:469-473.
    • (1997) Carbohydr. Res. , vol.305 , pp. 469-473
    • Bülter, T.1    Wandrey, C.2    Elling, L.3
  • 17
    • 84895115352 scopus 로고    scopus 로고
    • Leloir glycosyltransferases and natural product glycosylation: biocatalytic synthesis of the C-glucoside nothofagin, a major antioxidant of redbush herbal tea
    • Bungaruang L., Gutmann A., Nidetzky B. Leloir glycosyltransferases and natural product glycosylation: biocatalytic synthesis of the C-glucoside nothofagin, a major antioxidant of redbush herbal tea. Adv. Synth. Catal. 2013, 355:2757-2763.
    • (2013) Adv. Synth. Catal. , vol.355 , pp. 2757-2763
    • Bungaruang, L.1    Gutmann, A.2    Nidetzky, B.3
  • 18
    • 4444373841 scopus 로고    scopus 로고
    • Crystal structure of glycogen synthase: homologous enzymes catalyze glycogen synthesis and degradation
    • Buschiazzo A., Ugalde J.E., Guerin M.E., Shepard W., Ugalde R.A., Alzari P.M. Crystal structure of glycogen synthase: homologous enzymes catalyze glycogen synthesis and degradation. EMBO J. 2004, 23:3196-3205.
    • (2004) EMBO J. , vol.23 , pp. 3196-3205
    • Buschiazzo, A.1    Ugalde, J.E.2    Guerin, M.E.3    Shepard, W.4    Ugalde, R.A.5    Alzari, P.M.6
  • 19
    • 84865982932 scopus 로고    scopus 로고
    • Recent progress in enzymatic synthesis of sugar nucleotides
    • Cai L. Recent progress in enzymatic synthesis of sugar nucleotides. J. Carbohydr. Chem. 2012, 31:535-552.
    • (2012) J. Carbohydr. Chem. , vol.31 , pp. 535-552
    • Cai, L.1
  • 20
    • 0021178780 scopus 로고
    • Synthesis of 1'-deoxy-1'-fluorosucrose via sucrose synthetase mediated coupling of 1-deoxy-1-fluorofructose with uridine diphosphate glucose
    • Card P.J., Hitz W.D. Synthesis of 1'-deoxy-1'-fluorosucrose via sucrose synthetase mediated coupling of 1-deoxy-1-fluorofructose with uridine diphosphate glucose. J. Am. Chem. Soc. 1984, 106:5348-5350.
    • (1984) J. Am. Chem. Soc. , vol.106 , pp. 5348-5350
    • Card, P.J.1    Hitz, W.D.2
  • 21
    • 0007234471 scopus 로고
    • Chemoenzymic syntheses of fructose-modified sucroses via multienzyme systems. Some topographical aspects of the binding of sucrose to a sucrose carrier protein
    • Card P.J., Hitz W.D., Ripp K.G. Chemoenzymic syntheses of fructose-modified sucroses via multienzyme systems. Some topographical aspects of the binding of sucrose to a sucrose carrier protein. J. Am. Chem. Soc. 1986, 108:158-161.
    • (1986) J. Am. Chem. Soc. , vol.108 , pp. 158-161
    • Card, P.J.1    Hitz, W.D.2    Ripp, K.G.3
  • 22
    • 0242466471 scopus 로고
    • Specificity of nuceloside diphosphate sugars in sucrose biosynthesis
    • Cardini C.E., Recondo E. Specificity of nuceloside diphosphate sugars in sucrose biosynthesis. Plant Cell Physiol. 1962, 3:313-318.
    • (1962) Plant Cell Physiol. , vol.3 , pp. 313-318
    • Cardini, C.E.1    Recondo, E.2
  • 24
    • 0034644746 scopus 로고    scopus 로고
    • Changing the donor cofactor of bovine α1,3-galactosyltransferase by fusion with UDP-galactose 4-epimerase: more efficient biocatalysis for synthesis of α-Gal epitopes
    • Chen X., Liu Z., Wang J., Fang J., Fan H., Wang P.G. Changing the donor cofactor of bovine α1,3-galactosyltransferase by fusion with UDP-galactose 4-epimerase: more efficient biocatalysis for synthesis of α-Gal epitopes. J. Biol. Chem. 2000, 275:31594-31600.
    • (2000) J. Biol. Chem. , vol.275 , pp. 31594-31600
    • Chen, X.1    Liu, Z.2    Wang, J.3    Fang, J.4    Fan, H.5    Wang, P.G.6
  • 25
    • 0035819944 scopus 로고    scopus 로고
    • Sugar nucleotide regeneration beads (superbeads): a versatile tool for the practical synthesis of oligosaccharides
    • Chen X., Fang J., Zhang J., Liu Z., Shao J., Kowal P., et al. Sugar nucleotide regeneration beads (superbeads): a versatile tool for the practical synthesis of oligosaccharides. J. Am. Chem. Soc. 2001, 123:2081-2082.
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 2081-2082
    • Chen, X.1    Fang, J.2    Zhang, J.3    Liu, Z.4    Shao, J.5    Kowal, P.6
  • 26
    • 0035850540 scopus 로고    scopus 로고
    • Transferring a biosynthetic cycle into a productive Escherichia coli strain: large-scale synthesis of galactosides
    • Chen X., Zhang J., Kowal P., Liu Z., Andreana P.R., Lu Y., et al. Transferring a biosynthetic cycle into a productive Escherichia coli strain: large-scale synthesis of galactosides. J. Am. Chem. Soc. 2001, 123:8866-8867.
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 8866-8867
    • Chen, X.1    Zhang, J.2    Kowal, P.3    Liu, Z.4    Andreana, P.R.5    Lu, Y.6
  • 27
    • 0035142035 scopus 로고    scopus 로고
    • Two novel genes encoding SNF1-related protein kinases from Arabidopsis thaliana: differential accumulation of AtSR1 and AtSR2 transcripts in response to cytokinins and sugars, and phosphorylation of sucrose synthase by AtSR2
    • Chikano H., Ogawa M., Ikeda Y., Koizumi N., Kusano T., Sano H. Two novel genes encoding SNF1-related protein kinases from Arabidopsis thaliana: differential accumulation of AtSR1 and AtSR2 transcripts in response to cytokinins and sugars, and phosphorylation of sucrose synthase by AtSR2. Mol. Gen. Genet. 2001, 264:674-681.
    • (2001) Mol. Gen. Genet. , vol.264 , pp. 674-681
    • Chikano, H.1    Ogawa, M.2    Ikeda, Y.3    Koizumi, N.4    Kusano, T.5    Sano, H.6
  • 28
    • 33644645201 scopus 로고    scopus 로고
    • Molecular characterization and expression of four cDNAs encoding sucrose synthase from green bamboo Bambusa oldhamii
    • Chiu W.-B., Lin C.-H., Chang C.-J., Hsieh M.-H., Wang A.-Y. Molecular characterization and expression of four cDNAs encoding sucrose synthase from green bamboo Bambusa oldhamii. New Phytol. 2006, 170:53-63.
    • (2006) New Phytol. , vol.170 , pp. 53-63
    • Chiu, W.-B.1    Lin, C.-H.2    Chang, C.-J.3    Hsieh, M.-H.4    Wang, A.-Y.5
  • 29
    • 0037466315 scopus 로고    scopus 로고
    • An evolving hierarchical family classification for glycosyltransferases
    • Coutinho P.M., Deleury E., Davies G.J., Henrissat B. An evolving hierarchical family classification for glycosyltransferases. J. Mol. Biol. 2003, 328:307-317.
    • (2003) J. Mol. Biol. , vol.328 , pp. 307-317
    • Coutinho, P.M.1    Deleury, E.2    Davies, G.J.3    Henrissat, B.4
  • 30
    • 78249271725 scopus 로고    scopus 로고
    • The proteins involved in sucrose synthesis in the marine cyanobacterium Synechococcus sp. PCC 7002 are encoded by two genes transcribed from a gene cluster
    • Cumino A.C., Perez-Cenci M., Giarrocco L.E., Salerno G.L. The proteins involved in sucrose synthesis in the marine cyanobacterium Synechococcus sp. PCC 7002 are encoded by two genes transcribed from a gene cluster. FEBS Lett. 2010, 584:4655-4660.
    • (2010) FEBS Lett. , vol.584 , pp. 4655-4660
    • Cumino, A.C.1    Perez-Cenci, M.2    Giarrocco, L.E.3    Salerno, G.L.4
  • 31
    • 0033793487 scopus 로고    scopus 로고
    • A prokaryotic sucrose synthase gene (susA) isolated from a filamentous nitrogen-fixing cyanobacterium encodes a protein similar to those of plants
    • Curatti L., Porchia A.C., Herrera-Estrella L., Salerno G.L. A prokaryotic sucrose synthase gene (susA) isolated from a filamentous nitrogen-fixing cyanobacterium encodes a protein similar to those of plants. Planta 2000, 211:729-735.
    • (2000) Planta , vol.211 , pp. 729-735
    • Curatti, L.1    Porchia, A.C.2    Herrera-Estrella, L.3    Salerno, G.L.4
  • 32
    • 48749110373 scopus 로고    scopus 로고
    • Sucrose synthase is involved in the conversion of sucrose to polysaccharides in filamentous nitrogen-fixing cyanobacteria
    • Curatti L., Giarrocco L.E., Cumino A.C., Salerno G.L. Sucrose synthase is involved in the conversion of sucrose to polysaccharides in filamentous nitrogen-fixing cyanobacteria. Planta 2008, 228:617-625.
    • (2008) Planta , vol.228 , pp. 617-625
    • Curatti, L.1    Giarrocco, L.E.2    Cumino, A.C.3    Salerno, G.L.4
  • 33
    • 84865041566 scopus 로고    scopus 로고
    • Sucrose analogs: an attractive (bio)source for glycodiversification
    • Daude D., Remaud-Simeon M., Andre I. Sucrose analogs: an attractive (bio)source for glycodiversification. Nat. Prod. Rep. 2012, 29:945-960.
    • (2012) Nat. Prod. Rep. , vol.29 , pp. 945-960
    • Daude, D.1    Remaud-Simeon, M.2    Andre, I.3
  • 34
    • 84932195219 scopus 로고    scopus 로고
    • Development of an in vivo glucosylation platform by coupling production to growth: production of phenolic glucosides by a glycosyltransferase of Vitis vinifera
    • De Bruyn F., De Paepe B., Maertens J., Beauprez J., De Cocker P., Mincke S., et al. Development of an in vivo glucosylation platform by coupling production to growth: production of phenolic glucosides by a glycosyltransferase of Vitis vinifera. Biotechnol. Bioeng. 2015, 112:1594-1603.
    • (2015) Biotechnol. Bioeng. , vol.112 , pp. 1594-1603
    • De Bruyn, F.1    De Paepe, B.2    Maertens, J.3    Beauprez, J.4    De Cocker, P.5    Mincke, S.6
  • 35
    • 84924521776 scopus 로고    scopus 로고
    • Biotechnological advances in UDP-sugar based glycosylation of small molecules
    • De Bruyn F., Maertens J., Beauprez J., Soetaert W., De Mey M. Biotechnological advances in UDP-sugar based glycosylation of small molecules. Biotechnol. Adv. 2015, 33:288-302.
    • (2015) Biotechnol. Adv. , vol.33 , pp. 288-302
    • De Bruyn, F.1    Maertens, J.2    Beauprez, J.3    Soetaert, W.4    De Mey, M.5
  • 36
    • 0015523211 scopus 로고
    • The purification and properties of sucrose synthetase from etiolated Phaseolus aureus seedlings
    • Delmer D.P. The purification and properties of sucrose synthetase from etiolated Phaseolus aureus seedlings. J. Biol. Chem. 1972, 247:3822-3828.
    • (1972) J. Biol. Chem. , vol.247 , pp. 3822-3828
    • Delmer, D.P.1
  • 37
    • 2942534432 scopus 로고    scopus 로고
    • A pH-sensitive assay for galactosyltransferase
    • Deng C., Chen R.R. A pH-sensitive assay for galactosyltransferase. Anal. Biochem. 2004, 330:219-226.
    • (2004) Anal. Biochem. , vol.330 , pp. 219-226
    • Deng, C.1    Chen, R.R.2
  • 38
    • 84865272107 scopus 로고    scopus 로고
    • Enzymatic glycosylation of small molecules: challenging substrates require tailored catalysts
    • Desmet T., Soetaert W., Bojarová P., Křen V., Dijkhuizen L., Eastwick-Field V., et al. Enzymatic glycosylation of small molecules: challenging substrates require tailored catalysts. Chem. Eur. J. 2012, 18:10786-10801.
    • (2012) Chem. Eur. J. , vol.18 , pp. 10786-10801
    • Desmet, T.1    Soetaert, W.2    Bojarová, P.3    Křen, V.4    Dijkhuizen, L.5    Eastwick-Field, V.6
  • 39
    • 84941993790 scopus 로고    scopus 로고
    • Identification of sucrose synthase in nonphotosynthetic bacteria and characterization of the recombinant enzymes
    • Diricks M., De Bruyn F., Van Daele P., Walmagh M., Desmet T. Identification of sucrose synthase in nonphotosynthetic bacteria and characterization of the recombinant enzymes. Appl. Microbiol. Biotechnol. 2015, 99:8465-8474.
    • (2015) Appl. Microbiol. Biotechnol. , vol.99 , pp. 8465-8474
    • Diricks, M.1    De Bruyn, F.2    Van Daele, P.3    Walmagh, M.4    Desmet, T.5
  • 40
    • 0003104388 scopus 로고
    • Substrate inhibition of maize endosperm sucrose synthase by fructose and its interaction with glucose inhibition
    • Doehlert D.C. Substrate inhibition of maize endosperm sucrose synthase by fructose and its interaction with glucose inhibition. Plant Sci. 1987, 52:153-157.
    • (1987) Plant Sci. , vol.52 , pp. 153-157
    • Doehlert, D.C.1
  • 41
    • 84943160206 scopus 로고    scopus 로고
    • One assay for all: exploring small molecule phosphorylation using amylose-polyiodide complexes
    • Duan X.C., Chen H., Liu F.F., Conway L., Wei S., Cai Z.P., et al. One assay for all: exploring small molecule phosphorylation using amylose-polyiodide complexes. Anal. Chem. 2015, 87:9546-9550.
    • (2015) Anal. Chem. , vol.87 , pp. 9546-9550
    • Duan, X.C.1    Chen, H.2    Liu, F.F.3    Conway, L.4    Wei, S.5    Cai, Z.P.6
  • 42
    • 0027330393 scopus 로고
    • 13C spin coupling constants to assess furanose ring and glycosidic bond conformations in aqueous solution
    • 13C spin coupling constants to assess furanose ring and glycosidic bond conformations in aqueous solution. Carbohydr. Res. 1993, 249:281-303.
    • (1993) Carbohydr. Res. , vol.249 , pp. 281-303
    • Duker, J.M.1    Serianni, A.S.2
  • 43
    • 3543149006 scopus 로고    scopus 로고
    • The toxicity of recombinant proteins in Escherichia coli: a comparison of overexpression in BL21(DE3), C41(DE3), and C43(DE3)
    • Dumon-Seignovert L., Cariot G., Vuillard L. The toxicity of recombinant proteins in Escherichia coli: a comparison of overexpression in BL21(DE3), C41(DE3), and C43(DE3). Protein Expr. Purif. 2004, 37:203-206.
    • (2004) Protein Expr. Purif. , vol.37 , pp. 203-206
    • Dumon-Seignovert, L.1    Cariot, G.2    Vuillard, L.3
  • 44
    • 33747851344 scopus 로고    scopus 로고
    • The three maize sucrose synthase isoforms differ in distribution, localization, and phosphorylation
    • Duncan K.A., Hardin S.C., Huber S.C. The three maize sucrose synthase isoforms differ in distribution, localization, and phosphorylation. Plant Cell Physiol. 2006, 47:959-971.
    • (2006) Plant Cell Physiol. , vol.47 , pp. 959-971
    • Duncan, K.A.1    Hardin, S.C.2    Huber, S.C.3
  • 45
    • 0033230289 scopus 로고    scopus 로고
    • Flavanone-7-O-glucosyltransferase activity from Petunia hybrida
    • Durren R.L., McIntosh C.A. Flavanone-7-O-glucosyltransferase activity from Petunia hybrida. Phytochemistry 1999, 52:793-798.
    • (1999) Phytochemistry , vol.52 , pp. 793-798
    • Durren, R.L.1    McIntosh, C.A.2
  • 46
    • 0001036645 scopus 로고
    • A comparison of two sucrose synthetase isozymes from normal and shrunken-maize
    • Echt C.S., Chourey P.S. A comparison of two sucrose synthetase isozymes from normal and shrunken-maize. Plant Physiol. 1985, 79:530-536.
    • (1985) Plant Physiol. , vol.79 , pp. 530-536
    • Echt, C.S.1    Chourey, P.S.2
  • 47
    • 0033565384 scopus 로고    scopus 로고
    • Characterization of trehalose phosphorylase from Schizophyllum commune
    • Eis C., Nidetzky B. Characterization of trehalose phosphorylase from Schizophyllum commune. Biochem. J. 1999, 341:385-393.
    • (1999) Biochem. J. , vol.341 , pp. 385-393
    • Eis, C.1    Nidetzky, B.2
  • 48
    • 0028927674 scopus 로고
    • Effect of metal ions on sucrose synthase from rice grains - a study on enzyme inhibition and enzyme topography
    • Elling L. Effect of metal ions on sucrose synthase from rice grains - a study on enzyme inhibition and enzyme topography. Glycobiology 1995, 5:201-206.
    • (1995) Glycobiology , vol.5 , pp. 201-206
    • Elling, L.1
  • 49
    • 0030634217 scopus 로고    scopus 로고
    • Glycobiotechnology: enzymes for the synthesis of nucleotide sugars
    • Springer, Berlin, T. Scheper (Ed.)
    • Elling L. Glycobiotechnology: enzymes for the synthesis of nucleotide sugars. Advances in Biochemical Engineering/Biotechnology 1997, 89-144. Springer, Berlin. T. Scheper (Ed.).
    • (1997) Advances in Biochemical Engineering/Biotechnology , pp. 89-144
    • Elling, L.1
  • 50
    • 0027231227 scopus 로고
    • Purification of sucrose synthase from rice and its protein-chemical characterization
    • Elling L., Kula M.-R. Purification of sucrose synthase from rice and its protein-chemical characterization. J. Biotechnol. 1993, 29:277-286.
    • (1993) J. Biotechnol. , vol.29 , pp. 277-286
    • Elling, L.1    Kula, M.-R.2
  • 52
    • 0028825708 scopus 로고
    • Characterization of sucrose synthase from rice grains for the enzymatic synthesis of UDP and TDP glucose
    • Elling L., Kula M.-R. Characterization of sucrose synthase from rice grains for the enzymatic synthesis of UDP and TDP glucose. Enzym. Microb. Technol. 1995, 17:929-934.
    • (1995) Enzym. Microb. Technol. , vol.17 , pp. 929-934
    • Elling, L.1    Kula, M.-R.2
  • 54
    • 0027268549 scopus 로고
    • Investigation of sucrose synthase from rice for the synthesis of various nucleotide sugars and saccharides
    • Elling L., Grothus M., Kula M.-R. Investigation of sucrose synthase from rice for the synthesis of various nucleotide sugars and saccharides. Glycobiology 1993, 3:349-355.
    • (1993) Glycobiology , vol.3 , pp. 349-355
    • Elling, L.1    Grothus, M.2    Kula, M.-R.3
  • 55
    • 0028796199 scopus 로고
    • Isolation of sucrose synthase from rice (Oryza sativa) grains in pilot scale for application in carbohydrate synthesis
    • Elling L., Guldenberg B., Grothus M., Zervosen A., Peus M., Helfer A., et al. Isolation of sucrose synthase from rice (Oryza sativa) grains in pilot scale for application in carbohydrate synthesis. Biotechnol. Appl. Biochem. 1995, 21:29-37.
    • (1995) Biotechnol. Appl. Biochem. , vol.21 , pp. 29-37
    • Elling, L.1    Guldenberg, B.2    Grothus, M.3    Zervosen, A.4    Peus, M.5    Helfer, A.6
  • 56
    • 23644432034 scopus 로고    scopus 로고
    • An enzyme module system for the synthesis of dTDP-activated deoxysugars from dTMP and sucrose
    • Elling L., Rupprath C., Gunther N., Römer U., Verseck S., Weingarten P., et al. An enzyme module system for the synthesis of dTDP-activated deoxysugars from dTMP and sucrose. ChemBioChem 2005, 6:1423-1430.
    • (2005) ChemBioChem , vol.6 , pp. 1423-1430
    • Elling, L.1    Rupprath, C.2    Gunther, N.3    Römer, U.4    Verseck, S.5    Weingarten, P.6
  • 57
    • 0033792972 scopus 로고    scopus 로고
    • Large-scale production of oligosaccharides using engineered bacteria
    • Endo T., Koizumi S. Large-scale production of oligosaccharides using engineered bacteria. Curr. Opin. Struct. Biol. 2000, 10:536-541.
    • (2000) Curr. Opin. Struct. Biol. , vol.10 , pp. 536-541
    • Endo, T.1    Koizumi, S.2
  • 58
    • 0033032743 scopus 로고    scopus 로고
    • Large-scale production of N-acetyllactosamine through bacterial coupling
    • Endo T., Koizumi S., Tabata K., Kakita S., Ozaki A. Large-scale production of N-acetyllactosamine through bacterial coupling. Carbohydr. Res. 1999, 316:179-183.
    • (1999) Carbohydr. Res. , vol.316 , pp. 179-183
    • Endo, T.1    Koizumi, S.2    Tabata, K.3    Kakita, S.4    Ozaki, A.5
  • 59
    • 0034069205 scopus 로고    scopus 로고
    • Large-scale production of CMP-NeuAc and sialylated oligosaccharides through bacterial coupling
    • Endo T., Koizumi S., Tabata K., Ozaki A. Large-scale production of CMP-NeuAc and sialylated oligosaccharides through bacterial coupling. Appl. Microbiol. Biotechnol. 2000, 53:257-261.
    • (2000) Appl. Microbiol. Biotechnol. , vol.53 , pp. 257-261
    • Endo, T.1    Koizumi, S.2    Tabata, K.3    Ozaki, A.4
  • 60
    • 85027916679 scopus 로고    scopus 로고
    • Enzyme module systems for the synthesis of uridine 5'-diphospho-α-d-glucuronic acid and non-sulfated human natural killer cell-(HNK-1) epitope
    • Engels L., Henze M., Hummel W., Elling L. Enzyme module systems for the synthesis of uridine 5'-diphospho-α-d-glucuronic acid and non-sulfated human natural killer cell-(HNK-1) epitope. Adv. Synth. Catal. 2015, 357:1751-1762.
    • (2015) Adv. Synth. Catal. , vol.357 , pp. 1751-1762
    • Engels, L.1    Henze, M.2    Hummel, W.3    Elling, L.4
  • 61
    • 84913582173 scopus 로고    scopus 로고
    • Biochemical and molecular characterization of RcSUS1, a cytosolic sucrose synthase phosphorylated in vivo at serine 11 in developing castor oil seeds
    • Fedosejevs E.T., Ying S., Park J., Anderson E.M., Mullen R.T., She Y.-M., et al. Biochemical and molecular characterization of RcSUS1, a cytosolic sucrose synthase phosphorylated in vivo at serine 11 in developing castor oil seeds. J. Biol. Chem. 2014, 289:33412-33424.
    • (2014) J. Biol. Chem. , vol.289 , pp. 33412-33424
    • Fedosejevs, E.T.1    Ying, S.2    Park, J.3    Anderson, E.M.4    Mullen, R.T.5    She, Y.-M.6
  • 64
    • 80055000805 scopus 로고    scopus 로고
    • Enzymatic methods for glyco(diversification/randomization) of drugs and small molecules
    • Gantt R.W., Peltier-Pain P., Thorson J.S. Enzymatic methods for glyco(diversification/randomization) of drugs and small molecules. Nat. Prod. Rep. 2011, 28:1811-1853.
    • (2011) Nat. Prod. Rep. , vol.28 , pp. 1811-1853
    • Gantt, R.W.1    Peltier-Pain, P.2    Thorson, J.S.3
  • 65
    • 0031879563 scopus 로고    scopus 로고
    • The synthesis of sialylated oligosaccharides using a CMP-Neu5Ac synthetase/sialyltransferase fusion
    • Gilbert M., Bayer R., Cunningham A.-M., DeFrees S., Gao Y., Watson D.C., et al. The synthesis of sialylated oligosaccharides using a CMP-Neu5Ac synthetase/sialyltransferase fusion. Nat. Biotechnol. 1998, 16:769-772.
    • (1998) Nat. Biotechnol. , vol.16 , pp. 769-772
    • Gilbert, M.1    Bayer, R.2    Cunningham, A.-M.3    DeFrees, S.4    Gao, Y.5    Watson, D.C.6
  • 66
    • 33746882419 scopus 로고    scopus 로고
    • Structure-function relationships for Schizophyllum commune trehalose phosphorylase and their implications for the catalytic mechanism of family GT-glycosyltransferases
    • Goedl C., Griessler R., Schwarz A., Nidetzky B. Structure-function relationships for Schizophyllum commune trehalose phosphorylase and their implications for the catalytic mechanism of family GT-glycosyltransferases. Biochem. J. 2006, 397:491-500.
    • (2006) Biochem. J. , vol.397 , pp. 491-500
    • Goedl, C.1    Griessler, R.2    Schwarz, A.3    Nidetzky, B.4
  • 67
    • 0025063332 scopus 로고
    • Chemical synthesis of GDP-fucose analogs and their utilization by the Lewis *α(→ 4) fucosyltransferase
    • Gokhale U.B., Hindsgaul O., Palcic M.M. Chemical synthesis of GDP-fucose analogs and their utilization by the Lewis *α(→ 4) fucosyltransferase. Can. J. Chem. 1990, 68:1063-1071.
    • (1990) Can. J. Chem. , vol.68 , pp. 1063-1071
    • Gokhale, U.B.1    Hindsgaul, O.2    Palcic, M.M.3
  • 68
    • 0034830711 scopus 로고    scopus 로고
    • Characterization of PknC, a Ser/Thr kinase with broad substrate specificity from the cyanobacterium Anabaena sp. strain PCC 7120
    • Gonzalez L., Phalip V., Zhang C.-C. Characterization of PknC, a Ser/Thr kinase with broad substrate specificity from the cyanobacterium Anabaena sp. strain PCC 7120. Eur. J. Biochem. 2001, 268:1869-1875.
    • (2001) Eur. J. Biochem. , vol.268 , pp. 1869-1875
    • Gonzalez, L.1    Phalip, V.2    Zhang, C.-C.3
  • 69
    • 0014938667 scopus 로고
    • Sucrose synthetase from Phaseolus aureus seedlings
    • Grimes W.J., Jones B.L., Albersheim P. Sucrose synthetase from Phaseolus aureus seedlings. J. Biol. Chem. 1970, 245:188-197.
    • (1970) J. Biol. Chem. , vol.245 , pp. 188-197
    • Grimes, W.J.1    Jones, B.L.2    Albersheim, P.3
  • 70
    • 0346768386 scopus 로고
    • Enzymatic synthesis of α-d-glucopyranosyl-α -d-lyxopyranoside and α -d-glucopyranosyl-β-D-xylulofuranoside
    • Grothus M., Steigel A., Kula M.-R., Elling L. Enzymatic synthesis of α-d-glucopyranosyl-α -d-lyxopyranoside and α -d-glucopyranosyl-β-D-xylulofuranoside. Carbohydr. Lett. 1994, 1:83-88.
    • (1994) Carbohydr. Lett. , vol.1 , pp. 83-88
    • Grothus, M.1    Steigel, A.2    Kula, M.-R.3    Elling, L.4
  • 71
    • 84906226811 scopus 로고    scopus 로고
    • Towards the synthesis of glycosylated dihydrochalcone natural products using glycosyltransferase-catalysed cascade reactions
    • Gutmann A., Bungaruang L., Weber H., Leypold M., Breinbauer R., Nidetzky B. Towards the synthesis of glycosylated dihydrochalcone natural products using glycosyltransferase-catalysed cascade reactions. Green Chem. 2014, 16:4417-4425.
    • (2014) Green Chem. , vol.16 , pp. 4417-4425
    • Gutmann, A.1    Bungaruang, L.2    Weber, H.3    Leypold, M.4    Breinbauer, R.5    Nidetzky, B.6
  • 72
    • 84899521788 scopus 로고    scopus 로고
    • A two-step O- to C-glycosidic bond rearrangement using complementary glycosyltransferase activities
    • Gutmann A., Krump C., Bungaruang L., Nidetzky B. A two-step O- to C-glycosidic bond rearrangement using complementary glycosyltransferase activities. Chem. Commun. 2014, 50:5465-5468.
    • (2014) Chem. Commun. , vol.50 , pp. 5465-5468
    • Gutmann, A.1    Krump, C.2    Bungaruang, L.3    Nidetzky, B.4
  • 74
    • 84867731329 scopus 로고    scopus 로고
    • Biotechnological production of human milk oligosaccharides
    • Han N.S., Kim T.-J., Park Y.-C., Kim J., Seo J.-H. Biotechnological production of human milk oligosaccharides. Biotechnol. Adv. 2012, 30:1268-1278.
    • (2012) Biotechnol. Adv. , vol.30 , pp. 1268-1278
    • Han, N.S.1    Kim, T.-J.2    Park, Y.-C.3    Kim, J.4    Seo, J.-H.5
  • 75
    • 0141792977 scopus 로고    scopus 로고
    • Phosphorylation of sucrose synthase at serine 170: occurrence and possible role as a signal for proteolysis
    • Hardin S.C., Tang G.-Q., Scholz A., Holtgraewe D., Winter H., Huber S.C. Phosphorylation of sucrose synthase at serine 170: occurrence and possible role as a signal for proteolysis. Plant J. 2003, 35:588-603.
    • (2003) Plant J. , vol.35 , pp. 588-603
    • Hardin, S.C.1    Tang, G.-Q.2    Scholz, A.3    Holtgraewe, D.4    Winter, H.5    Huber, S.C.6
  • 76
    • 1942437647 scopus 로고    scopus 로고
    • Phosphorylation of the amino terminus of maize sucrose synthase in relation to membrane association and enzyme activity
    • Hardin S.C., Winter H., Huber S.C. Phosphorylation of the amino terminus of maize sucrose synthase in relation to membrane association and enzyme activity. Plant Physiol. 2004, 134:1427-1438.
    • (2004) Plant Physiol. , vol.134 , pp. 1427-1438
    • Hardin, S.C.1    Winter, H.2    Huber, S.C.3
  • 77
    • 84861094604 scopus 로고    scopus 로고
    • Synthesis of β-d-fructofuranosyl-(→ 1)-2-acetamido-2-deoxy-α-d-glucopyranoside (N-acetylsucrosamine) using β-fructofuranosidase-containing Aspergillus oryzae mycelia as a whole-cell catalyst
    • Hirano T., Wada T., Iwai S., Sato H., Noda M., Juami M., et al. Synthesis of β-d-fructofuranosyl-(→ 1)-2-acetamido-2-deoxy-α-d-glucopyranoside (N-acetylsucrosamine) using β-fructofuranosidase-containing Aspergillus oryzae mycelia as a whole-cell catalyst. Carbohydr. Res. 2012, 353:27-32.
    • (2012) Carbohydr. Res. , vol.353 , pp. 27-32
    • Hirano, T.1    Wada, T.2    Iwai, S.3    Sato, H.4    Noda, M.5    Juami, M.6
  • 78
    • 0029783026 scopus 로고    scopus 로고
    • One-pot enzymatic synthesis of the Galα1 → 3Galβ1 → 4GlcNAc sequence with in situ UDP-Gal regeneration
    • Hokke C., Zervosen A., Elling L., Joziasse D.H., van den Eijnden D.H. One-pot enzymatic synthesis of the Galα1 → 3Galβ1 → 4GlcNAc sequence with in situ UDP-Gal regeneration. Glycoconj. J. 1996, 13:687-692.
    • (1996) Glycoconj. J. , vol.13 , pp. 687-692
    • Hokke, C.1    Zervosen, A.2    Elling, L.3    Joziasse, D.H.4    van den Eijnden, D.H.5
  • 82
    • 0031715259 scopus 로고    scopus 로고
    • Purification and characterization of sucrose synthase isozymes from etiolated rice seedlings
    • Huang D.-Y., Wang A.-Y. Purification and characterization of sucrose synthase isozymes from etiolated rice seedlings. IUBMB Life 1998, 46:107-113.
    • (1998) IUBMB Life , vol.46 , pp. 107-113
    • Huang, D.-Y.1    Wang, A.-Y.2
  • 83
    • 0030267085 scopus 로고    scopus 로고
    • Phosphorylation of serine-15 of maize leaf sucrose synthase (occurrence in vivo and possible regulatory significance)
    • Huber S.C., Huber J.L., Liao P.-C., Gage D.A., McMichael R.W., Chourey P.S., et al. Phosphorylation of serine-15 of maize leaf sucrose synthase (occurrence in vivo and possible regulatory significance). Plant Physiol. 1996, 112:793-802.
    • (1996) Plant Physiol. , vol.112 , pp. 793-802
    • Huber, S.C.1    Huber, J.L.2    Liao, P.-C.3    Gage, D.A.4    McMichael, R.W.5    Chourey, P.S.6
  • 84
    • 0028672815 scopus 로고
    • Regeneration of sugar nucleotide for enzymatic oligosaccharide synthesis
    • Ichikawa Y., Wang R., Wong C.-H. Regeneration of sugar nucleotide for enzymatic oligosaccharide synthesis. Methods Enzymol. 1994, 247:107-127.
    • (1994) Methods Enzymol. , vol.247 , pp. 107-127
    • Ichikawa, Y.1    Wang, R.2    Wong, C.-H.3
  • 85
    • 0028847233 scopus 로고
    • Application of sucrose phosphorylase reaction in one-pot enzymatic galactosylation - scavenger of phosphate and generation of glucose 1-phosphate in situ
    • Ichikawa M., Schnaar R.L., Ichikawa Y. Application of sucrose phosphorylase reaction in one-pot enzymatic galactosylation - scavenger of phosphate and generation of glucose 1-phosphate in situ. Tetrahedron Lett. 1995, 36:8731-8732.
    • (1995) Tetrahedron Lett. , vol.36 , pp. 8731-8732
    • Ichikawa, M.1    Schnaar, R.L.2    Ichikawa, Y.3
  • 86
    • 0037302496 scopus 로고    scopus 로고
    • Characterization of two sucrose synthase isoforms in sugarbeet root
    • Klotz K.L., Finger F.L., Shelver W.L. Characterization of two sucrose synthase isoforms in sugarbeet root. Plant Physiol. Biochem. 2003, 41:107-115.
    • (2003) Plant Physiol. Biochem. , vol.41 , pp. 107-115
    • Klotz, K.L.1    Finger, F.L.2    Shelver, W.L.3
  • 87
    • 2442459991 scopus 로고    scopus 로고
    • Sucrose metabolism: regulatory mechanisms and pivotal roles in sugar sensing and plant development
    • Koch K. Sucrose metabolism: regulatory mechanisms and pivotal roles in sugar sensing and plant development. Curr. Opin. Plant Biol. 2004, 7:235-246.
    • (2004) Curr. Opin. Plant Biol. , vol.7 , pp. 235-246
    • Koch, K.1
  • 88
    • 0034505430 scopus 로고    scopus 로고
    • Synthesis of complex carbohydrates and glycoconjugates: enzyme-based and programmable one-pot strategies
    • Koeller K.M., Wong C.-H. Synthesis of complex carbohydrates and glycoconjugates: enzyme-based and programmable one-pot strategies. Chem. Rev. 2000, 100:4465-4494.
    • (2000) Chem. Rev. , vol.100 , pp. 4465-4494
    • Koeller, K.M.1    Wong, C.-H.2
  • 89
    • 0031754396 scopus 로고    scopus 로고
    • Large-scale production of UDP-galactose and globotriose by coupling metabolically engineered bacteria
    • Koizumi S., Endo T., Tabata K., Ozaki A. Large-scale production of UDP-galactose and globotriose by coupling metabolically engineered bacteria. Nat. Biotechnol. 1998, 16:847-850.
    • (1998) Nat. Biotechnol. , vol.16 , pp. 847-850
    • Koizumi, S.1    Endo, T.2    Tabata, K.3    Ozaki, A.4
  • 91
    • 8544237035 scopus 로고    scopus 로고
    • UDP-sugar pyrophosphorylase with broad substrate specificity toward various monosaccharide 1-phosphates from pea sprouts
    • Kotake T., Yamaguchi D., Ohzono H., Hojo S., Kaneko S., Ishida H.-k., et al. UDP-sugar pyrophosphorylase with broad substrate specificity toward various monosaccharide 1-phosphates from pea sprouts. J. Biol. Chem. 2004, 279:45728-45736.
    • (2004) J. Biol. Chem. , vol.279 , pp. 45728-45736
    • Kotake, T.1    Yamaguchi, D.2    Ohzono, H.3    Hojo, S.4    Kaneko, S.5    Ishida, H.-K.6
  • 92
    • 50549100880 scopus 로고    scopus 로고
    • Fructansucrase enzymes and sucrose analogues: a new approach for the synthesis of unique fructo-oligosaccharides
    • Kralj S., Buchholz K., Dijkhuizen L., Seibel J. Fructansucrase enzymes and sucrose analogues: a new approach for the synthesis of unique fructo-oligosaccharides. Biocatal. Biotransform. 2008, 26:32-41.
    • (2008) Biocatal. Biotransform. , vol.26 , pp. 32-41
    • Kralj, S.1    Buchholz, K.2    Dijkhuizen, L.3    Seibel, J.4
  • 93
    • 49749126041 scopus 로고    scopus 로고
    • Sweet antibiotics - the role of glycosidic residues in antibiotic and antitumor activity and their randomization
    • Křen V., Řezanka T. Sweet antibiotics - the role of glycosidic residues in antibiotic and antitumor activity and their randomization. FEMS Microbiol. Rev. 2008, 32:858-889.
    • (2008) FEMS Microbiol. Rev. , vol.32 , pp. 858-889
    • Křen, V.1    Řezanka, T.2
  • 96
    • 84940044108 scopus 로고    scopus 로고
    • Creating a water-soluble resveratrol-based antioxidant through site-selective enzymatic glucosylation
    • Lepak A., Gutmann A., Kulmer S.T., Nidetzky B. Creating a water-soluble resveratrol-based antioxidant through site-selective enzymatic glucosylation. ChemBioChem 2015, 16:1870-1874.
    • (2015) ChemBioChem , vol.16 , pp. 1870-1874
    • Lepak, A.1    Gutmann, A.2    Kulmer, S.T.3    Nidetzky, B.4
  • 97
    • 0037971696 scopus 로고    scopus 로고
    • Cloning, characterization and expression analysis of a sucrose synthase gene from tropical epiphytic orchid Oncidium Goldiana
    • Li C.R., Zhang X.B., Hew C.S. Cloning, characterization and expression analysis of a sucrose synthase gene from tropical epiphytic orchid Oncidium Goldiana. Physiol. Plant. 2003, 118:352-360.
    • (2003) Physiol. Plant. , vol.118 , pp. 352-360
    • Li, C.R.1    Zhang, X.B.2    Hew, C.S.3
  • 98
    • 1242321415 scopus 로고    scopus 로고
    • Cloning, characterization and tissue specific expression of a sucrose synthase gene from tropical epiphytic CAM orchid Mokara Yellow
    • Li C.R., Zhang X.B., Huang C.H., Hew C.S. Cloning, characterization and tissue specific expression of a sucrose synthase gene from tropical epiphytic CAM orchid Mokara Yellow. J. Plant Physiol. 2004, 161:87-94.
    • (2004) J. Plant Physiol. , vol.161 , pp. 87-94
    • Li, C.R.1    Zhang, X.B.2    Huang, C.H.3    Hew, C.S.4
  • 99
    • 84988109762 scopus 로고
    • Molecular modeling of saccharides, 8. Selective 2-O-benzylation of sucrose: a facile entry to its 2-deoxy- and 2-keto-derivatives and to sucrosamine
    • Lichtenthaler F.W., Immel S., Pokinskyj P. Molecular modeling of saccharides, 8. Selective 2-O-benzylation of sucrose: a facile entry to its 2-deoxy- and 2-keto-derivatives and to sucrosamine. Liebigs Ann. 1995, 1995:1939-1947.
    • (1995) Liebigs Ann. , vol.1995 , pp. 1939-1947
    • Lichtenthaler, F.W.1    Immel, S.2    Pokinskyj, P.3
  • 100
    • 25444442036 scopus 로고    scopus 로고
    • Plant glycosyltransferases - their potential as novel biocatalysts
    • Lim E.K. Plant glycosyltransferases - their potential as novel biocatalysts. Chem. Eur. J. 2005, 11:5486-5494.
    • (2005) Chem. Eur. J. , vol.11 , pp. 5486-5494
    • Lim, E.K.1
  • 101
    • 0037393072 scopus 로고    scopus 로고
    • P1 trisaccharide (Galα1,4Galβ1,4GlcNAc) synthesis by enzyme glycosylation reactions using recombinant Escherichia coli
    • Liu Z., Lu Y., Zhang J., Pardee K., Wang P.G. P1 trisaccharide (Galα1,4Galβ1,4GlcNAc) synthesis by enzyme glycosylation reactions using recombinant Escherichia coli. Appl. Environ. Microbiol. 2003, 69:2110-2115.
    • (2003) Appl. Environ. Microbiol. , vol.69 , pp. 2110-2115
    • Liu, Z.1    Lu, Y.2    Zhang, J.3    Pardee, K.4    Wang, P.G.5
  • 102
    • 84910126096 scopus 로고    scopus 로고
    • Facile enzymatic synthesis of sugar 1-phosphates as substrates for phosphorylases using anomeric kinases
    • Liu Y., Nishimoto M., Kitaoka M. Facile enzymatic synthesis of sugar 1-phosphates as substrates for phosphorylases using anomeric kinases. Carbohydr. Res. 2015, 401:1-4.
    • (2015) Carbohydr. Res. , vol.401 , pp. 1-4
    • Liu, Y.1    Nishimoto, M.2    Kitaoka, M.3
  • 104
    • 78650090993 scopus 로고    scopus 로고
    • Carbohydrate synthesis by disaccharide phosphorylases: reactions, catalytic mechanisms and application in the glycosciences
    • Luley-Goedl C., Nidetzky B. Carbohydrate synthesis by disaccharide phosphorylases: reactions, catalytic mechanisms and application in the glycosciences. Biotechnol. J. 2010, 5:1324-1338.
    • (2010) Biotechnol. J. , vol.5 , pp. 1324-1338
    • Luley-Goedl, C.1    Nidetzky, B.2
  • 105
    • 79954994761 scopus 로고    scopus 로고
    • Glycosides as compatible solutes: biosynthesis and applications
    • Luley-Goedl C., Nidetzky B. Glycosides as compatible solutes: biosynthesis and applications. Nat. Prod. Rep. 2011, 28:875-896.
    • (2011) Nat. Prod. Rep. , vol.28 , pp. 875-896
    • Luley-Goedl, C.1    Nidetzky, B.2
  • 106
    • 0035800104 scopus 로고    scopus 로고
    • High yielding one-pot enzyme-catalyzed synthesis of UDP-glucose in gram scales
    • Ma X., Stöckigt J. High yielding one-pot enzyme-catalyzed synthesis of UDP-glucose in gram scales. Carbohydr. Res. 2001, 333:159-163.
    • (2001) Carbohydr. Res. , vol.333 , pp. 159-163
    • Ma, X.1    Stöckigt, J.2
  • 107
    • 0028601326 scopus 로고
    • Protein phosphorylation in cyanobacteria
    • Mann N.H. Protein phosphorylation in cyanobacteria. Microbiology 1994, 140:3207-3215.
    • (1994) Microbiology , vol.140 , pp. 3207-3215
    • Mann, N.H.1
  • 109
    • 0026527703 scopus 로고
    • Enzymatic synthesis and isolation of thymidine diphosphate-6-deoxy-d-xylo-4-hexulose and thymidine diphosphate-l-rhamnose
    • Marumo K., Lindqvist L., Verma N., Weintraub A., Reeves P.R., Lindberg A.A. Enzymatic synthesis and isolation of thymidine diphosphate-6-deoxy-d-xylo-4-hexulose and thymidine diphosphate-l-rhamnose. Eur. J. Biochem. 1992, 204:539-545.
    • (1992) Eur. J. Biochem. , vol.204 , pp. 539-545
    • Marumo, K.1    Lindqvist, L.2    Verma, N.3    Weintraub, A.4    Reeves, P.R.5    Lindberg, A.A.6
  • 110
    • 34248581665 scopus 로고    scopus 로고
    • An efficient chemoenzymatic production of small molecule glucosides with in situ UDP-glucose recycling
    • Masada S., Kawase Y., Nagatoshi M., Oguchi Y., Terasaka K., Mizukami H. An efficient chemoenzymatic production of small molecule glucosides with in situ UDP-glucose recycling. FEBS Lett. 2007, 581:2562-2566.
    • (2007) FEBS Lett. , vol.581 , pp. 2562-2566
    • Masada, S.1    Kawase, Y.2    Nagatoshi, M.3    Oguchi, Y.4    Terasaka, K.5    Mizukami, H.6
  • 111
    • 50849133566 scopus 로고    scopus 로고
    • Enzymatic preparation of 1-O-hydroxycinnamoyl-β-D-glucoses and their application to the study of 1-O-hydroxycinnamoyl-β-D-glucose-dependent acyltransferase in anthocyanin-producing cultured cells of Daucus carota and Glehnia littoralis
    • Matsuba Y., Okuda Y., Abe Y., Kitamura Y., Terasaka K., Mizukami H., et al. Enzymatic preparation of 1-O-hydroxycinnamoyl-β-D-glucoses and their application to the study of 1-O-hydroxycinnamoyl-β-D-glucose-dependent acyltransferase in anthocyanin-producing cultured cells of Daucus carota and Glehnia littoralis. Plant Biol. 2008, 25:369-375.
    • (2008) Plant Biol. , vol.25 , pp. 369-375
    • Matsuba, Y.1    Okuda, Y.2    Abe, Y.3    Kitamura, Y.4    Terasaka, K.5    Mizukami, H.6
  • 112
    • 84938152152 scopus 로고    scopus 로고
    • Biochemical characterization of a recombinant UDP-glucosyltransferase from rice and enzymatic production of deoxynivalenol-3-O-β-D-glucoside
    • Michlmayr H., Malachova A., Varga E., Kleinova J., Lemmens M., Newmister S., et al. Biochemical characterization of a recombinant UDP-glucosyltransferase from rice and enzymatic production of deoxynivalenol-3-O-β-D-glucoside. Toxins 2015, 7:2685-2700.
    • (2015) Toxins , vol.7 , pp. 2685-2700
    • Michlmayr, H.1    Malachova, A.2    Varga, E.3    Kleinova, J.4    Lemmens, M.5    Newmister, S.6
  • 113
    • 0030593468 scopus 로고    scopus 로고
    • Over-production of proteins in Escherichia coli: mutant hosts that allow synthesis of some membrane proteins and globular proteins at high levels
    • Miroux B., Walker J.E. Over-production of proteins in Escherichia coli: mutant hosts that allow synthesis of some membrane proteins and globular proteins at high levels. J. Mol. Biol. 1996, 260:289-298.
    • (1996) J. Mol. Biol. , vol.260 , pp. 289-298
    • Miroux, B.1    Walker, J.E.2
  • 114
    • 0000769546 scopus 로고
    • Sucrose synthase of soybean nodules
    • Morell M., Copeland L. Sucrose synthase of soybean nodules. Plant Physiol. 1985, 78:149-154.
    • (1985) Plant Physiol. , vol.78 , pp. 149-154
    • Morell, M.1    Copeland, L.2
  • 115
    • 0001178549 scopus 로고
    • Purification and characterization of sucrose synthase from peach (Prunus persica) fruit
    • Moriguchi T., Yamaki S. Purification and characterization of sucrose synthase from peach (Prunus persica) fruit. Plant Cell Physiol. 1988, 29:1361-1366.
    • (1988) Plant Cell Physiol. , vol.29 , pp. 1361-1366
    • Moriguchi, T.1    Yamaki, S.2
  • 116
    • 0001601942 scopus 로고
    • Sucrose synthetase of sweet potato roots. Part II: a kinetic study
    • Murata T. Sucrose synthetase of sweet potato roots. Part II: a kinetic study. Agric. Biol. Chem. 1971, 35:1441-1448.
    • (1971) Agric. Biol. Chem. , vol.35 , pp. 1441-1448
    • Murata, T.1
  • 117
    • 0012718460 scopus 로고
    • Sucrose synthetase of rice grains and potato tubers
    • Murata T. Sucrose synthetase of rice grains and potato tubers. Agric. Biol. Chem. 1972, 36:1815-1818.
    • (1972) Agric. Biol. Chem. , vol.36 , pp. 1815-1818
    • Murata, T.1
  • 118
    • 0031218655 scopus 로고    scopus 로고
    • Expression and characterization of sucrose synthase from mung bean seedlings in Escherichia coli
    • Nakai T., Tonouchi N., Tsuchida T., Mori H., Sakai F., Hayashi T. Expression and characterization of sucrose synthase from mung bean seedlings in Escherichia coli. Biosci. Biotechnol. Biochem. 1997, 61:1500-1503.
    • (1997) Biosci. Biotechnol. Biochem. , vol.61 , pp. 1500-1503
    • Nakai, T.1    Tonouchi, N.2    Tsuchida, T.3    Mori, H.4    Sakai, F.5    Hayashi, T.6
  • 121
    • 77956968010 scopus 로고
    • Biosynthesis of saccharides from glycopyranosyl esters of nucleotides ("sugar nucleotides")
    • Neufeld E.F., Hassid W.Z. Biosynthesis of saccharides from glycopyranosyl esters of nucleotides ("sugar nucleotides"). Adv. Carbohydr. Chem. 1963, 18:309-356.
    • (1963) Adv. Carbohydr. Chem. , vol.18 , pp. 309-356
    • Neufeld, E.F.1    Hassid, W.Z.2
  • 122
    • 35548975958 scopus 로고    scopus 로고
    • Practical preparation of lacto-N-biose I, a candidate for the bifidus factor in human milk
    • Nishimoto M., Kitaoka M. Practical preparation of lacto-N-biose I, a candidate for the bifidus factor in human milk. Biosci. Biotechnol. Biochem. 2007, 71:2101-2104.
    • (2007) Biosci. Biotechnol. Biochem. , vol.71 , pp. 2101-2104
    • Nishimoto, M.1    Kitaoka, M.2
  • 123
    • 0015880795 scopus 로고
    • Enzymic mechanism of starch synthesis in ripening rice grains: VII. Purification and enzymic properties of sucrose synthetase
    • Nomura T., Akazawa T. Enzymic mechanism of starch synthesis in ripening rice grains: VII. Purification and enzymic properties of sucrose synthetase. Arch. Biochem. Biophys. 1973, 156:644-652.
    • (1973) Arch. Biochem. Biophys. , vol.156 , pp. 644-652
    • Nomura, T.1    Akazawa, T.2
  • 124
    • 0017125142 scopus 로고
    • The metal ion catalyzed decomposition of nucleoside diphosphate sugars
    • Nunez H.A., Barker R. The metal ion catalyzed decomposition of nucleoside diphosphate sugars. Biochemistry 1976, 15:3843-3847.
    • (1976) Biochemistry , vol.15 , pp. 3843-3847
    • Nunez, H.A.1    Barker, R.2
  • 125
    • 33646131401 scopus 로고    scopus 로고
    • Preparation of UDP-galacturonic acid using UDP-sugar pyrophosphorylase
    • Ohashi T., Cramer N., Ishimizu T., Hase S. Preparation of UDP-galacturonic acid using UDP-sugar pyrophosphorylase. Anal. Biochem. 2006, 352:182-187.
    • (2006) Anal. Biochem. , vol.352 , pp. 182-187
    • Ohashi, T.1    Cramer, N.2    Ishimizu, T.3    Hase, S.4
  • 126
    • 70349318377 scopus 로고    scopus 로고
    • Identification, recombinant expression, and biochemical characterization of a flavonol 3-O-glucosyltransferase clone from Citrus paradisi
    • Owens D.K., McIntosh C.A. Identification, recombinant expression, and biochemical characterization of a flavonol 3-O-glucosyltransferase clone from Citrus paradisi. Phytochemistry 2009, 70:1382-1391.
    • (2009) Phytochemistry , vol.70 , pp. 1382-1391
    • Owens, D.K.1    McIntosh, C.A.2
  • 127
    • 79953328716 scopus 로고    scopus 로고
    • Glycosyltransferases as biocatalysts
    • Palcic M.M. Glycosyltransferases as biocatalysts. Curr. Opin. Chem. Biol. 2011, 15:226-233.
    • (2011) Curr. Opin. Chem. Biol. , vol.15 , pp. 226-233
    • Palcic, M.M.1
  • 128
    • 43849103990 scopus 로고    scopus 로고
    • A high-throughput pH indicator assay for screening glycosyltransferase saturation mutagenesis libraries
    • Persson M., Palcic M.M. A high-throughput pH indicator assay for screening glycosyltransferase saturation mutagenesis libraries. Anal. Biochem. 2008, 378:1-7.
    • (2008) Anal. Biochem. , vol.378 , pp. 1-7
    • Persson, M.1    Palcic, M.M.2
  • 129
    • 0035151023 scopus 로고    scopus 로고
    • Crystal structure of the retaining galactosyltransferase LgtC from Neisseria meningitidis in complex with donor and acceptor sugar analogs
    • Persson K., Ly H.D., Dieckelmann M., Wakarchuk W.W., Withers S.G., Strynadka N.C.J. Crystal structure of the retaining galactosyltransferase LgtC from Neisseria meningitidis in complex with donor and acceptor sugar analogs. Nat. Struct. Biol. 2001, 8:166-175.
    • (2001) Nat. Struct. Biol. , vol.8 , pp. 166-175
    • Persson, K.1    Ly, H.D.2    Dieckelmann, M.3    Wakarchuk, W.W.4    Withers, S.G.5    Strynadka, N.C.J.6
  • 131
    • 33846197938 scopus 로고    scopus 로고
    • Biocatalysis for pharmaceutical intermediates: the future is now
    • Pollard D.J., Woodley J.M. Biocatalysis for pharmaceutical intermediates: the future is now. Trends Biotechnol. 2007, 25:66-73.
    • (2007) Trends Biotechnol. , vol.25 , pp. 66-73
    • Pollard, D.J.1    Woodley, J.M.2
  • 132
    • 0030459822 scopus 로고    scopus 로고
    • Sucrose biosynthesis in a prokaryotic organism: presence of two sucrose-phosphate synthases in Anabaena with remarkable differences compared with the plant enzymes
    • Porchia A.C., Salerno G.L. Sucrose biosynthesis in a prokaryotic organism: presence of two sucrose-phosphate synthases in Anabaena with remarkable differences compared with the plant enzymes. Proc. Natl. Acad. Sci. 1996, 93:13600-13604.
    • (1996) Proc. Natl. Acad. Sci. , vol.93 , pp. 13600-13604
    • Porchia, A.C.1    Salerno, G.L.2
  • 133
    • 0033228193 scopus 로고    scopus 로고
    • Sucrose metabolism in cyanobacteria: sucrose synthase from Anabaena sp. strain PCC 7119 is remarkably different from the plant enzymes with respect to substrate affinity and amino-terminal sequence
    • Porchia A.C., Curatti L., Salerno G.L. Sucrose metabolism in cyanobacteria: sucrose synthase from Anabaena sp. strain PCC 7119 is remarkably different from the plant enzymes with respect to substrate affinity and amino-terminal sequence. Planta 1999, 210:34-40.
    • (1999) Planta , vol.210 , pp. 34-40
    • Porchia, A.C.1    Curatti, L.2    Salerno, G.L.3
  • 134
    • 9144221530 scopus 로고    scopus 로고
    • TreT, a novel trehalose glycosyltransferring synthase of the hyperthermophilic archaeon Thermococcus litoralis
    • Qu Q., Lee S.-J., Boos W. TreT, a novel trehalose glycosyltransferring synthase of the hyperthermophilic archaeon Thermococcus litoralis. J. Biol. Chem. 2004, 279:47890-47897.
    • (2004) J. Biol. Chem. , vol.279 , pp. 47890-47897
    • Qu, Q.1    Lee, S.-J.2    Boos, W.3
  • 135
    • 0346125214 scopus 로고    scopus 로고
    • Characterization of recombinant sucrose synthase 1 from potato for the synthesis of sucrose analogues
    • Römer U., Nettelstroth N., Köckenberger W., Elling L. Characterization of recombinant sucrose synthase 1 from potato for the synthesis of sucrose analogues. Adv. Synth. Catal. 2001, 343:655-661.
    • (2001) Adv. Synth. Catal. , vol.343 , pp. 655-661
    • Römer, U.1    Nettelstroth, N.2    Köckenberger, W.3    Elling, L.4
  • 136
    • 0242522877 scopus 로고    scopus 로고
    • The donor substrate spectrum of recombinant sucrose synthase 1 from potato for the synthesis of sucrose analogues
    • Römer U., Rupprath C., Elling L. The donor substrate spectrum of recombinant sucrose synthase 1 from potato for the synthesis of sucrose analogues. Adv. Synth. Catal. 2003, 345:684-686.
    • (2003) Adv. Synth. Catal. , vol.345 , pp. 684-686
    • Römer, U.1    Rupprath, C.2    Elling, L.3
  • 137
    • 0346094305 scopus 로고    scopus 로고
    • Expression, purification and characterization of recombinant sucrose synthase 1 from Solanum tuberosum L. for carbohydrate engineering
    • Römer U., Schrader H., Günther N., Nettelstroth N., Frommer W.B., Elling L. Expression, purification and characterization of recombinant sucrose synthase 1 from Solanum tuberosum L. for carbohydrate engineering. J. Biotechnol. 2004, 107:135-149.
    • (2004) J. Biotechnol. , vol.107 , pp. 135-149
    • Römer, U.1    Schrader, H.2    Günther, N.3    Nettelstroth, N.4    Frommer, W.B.5    Elling, L.6
  • 138
    • 0001052544 scopus 로고
    • Purification and characterization of sucrose synthase from the cotyledons of Vicia faba L
    • Ross H.A., Davies H.V. Purification and characterization of sucrose synthase from the cotyledons of Vicia faba L. Plant Physiol. 1992, 100:1008-1013.
    • (1992) Plant Physiol. , vol.100 , pp. 1008-1013
    • Ross, H.A.1    Davies, H.V.2
  • 139
    • 21244483529 scopus 로고    scopus 로고
    • Nucleotide deoxysugars: essential tools for the glycosylation engineering of novel bioactive compounds
    • Rupprath C., Schumacher T., Elling L. Nucleotide deoxysugars: essential tools for the glycosylation engineering of novel bioactive compounds. Curr. Med. Chem. 2005, 12:1637-1675.
    • (2005) Curr. Med. Chem. , vol.12 , pp. 1637-1675
    • Rupprath, C.1    Schumacher, T.2    Elling, L.3
  • 140
    • 34547215445 scopus 로고    scopus 로고
    • An enzyme module system for in situ regeneration of deoxythymidine 5'-diphosphate (dTDP)-activated deoxy sugars
    • Rupprath C., Kopp M., Hirtz D., Müller R., Elling L. An enzyme module system for in situ regeneration of deoxythymidine 5'-diphosphate (dTDP)-activated deoxy sugars. Adv. Synth. Catal. 2007, 349:1489-1496.
    • (2007) Adv. Synth. Catal. , vol.349 , pp. 1489-1496
    • Rupprath, C.1    Kopp, M.2    Hirtz, D.3    Müller, R.4    Elling, L.5
  • 141
    • 84883764639 scopus 로고    scopus 로고
    • Synthesis of nucleotide sugars and α-galacto-oligosaccharides by recombinant Escherichia coli cells with trehalose substrate
    • Ryu S.-I., Lee S.-B. Synthesis of nucleotide sugars and α-galacto-oligosaccharides by recombinant Escherichia coli cells with trehalose substrate. Enzym. Microb. Technol. 2013, 53:359-363.
    • (2013) Enzym. Microb. Technol. , vol.53 , pp. 359-363
    • Ryu, S.-I.1    Lee, S.-B.2
  • 142
    • 78650252130 scopus 로고    scopus 로고
    • Catalytic reversibility of Pyrococcus horikoshii trehalose synthase: efficient synthesis of several nucleoside diphosphate glucoses with enzyme recycling
    • Ryu S.-I., Kim J.-E., Kim E.-J., Chung S.-K., Lee S.-B. Catalytic reversibility of Pyrococcus horikoshii trehalose synthase: efficient synthesis of several nucleoside diphosphate glucoses with enzyme recycling. Process Biochem. 2011, 46:128-134.
    • (2011) Process Biochem. , vol.46 , pp. 128-134
    • Ryu, S.-I.1    Kim, J.-E.2    Kim, E.-J.3    Chung, S.-K.4    Lee, S.-B.5
  • 143
    • 0037937490 scopus 로고    scopus 로고
    • Origin of sucrose metabolism in higher plants: when, how and why?
    • Salerno G.L., Curatti L. Origin of sucrose metabolism in higher plants: when, how and why?. Trends Plant Sci. 2003, 8:63-69.
    • (2003) Trends Plant Sci. , vol.8 , pp. 63-69
    • Salerno, G.L.1    Curatti, L.2
  • 144
    • 84918773143 scopus 로고    scopus 로고
    • Identification of the glucosyltransferase that mediates direct flavone C-glucosylation in Gentiana triflora
    • Sasaki N., Nishizaki Y., Yamada E., Tatsuzawa F., Nakatsuka T., Takahashi H., et al. Identification of the glucosyltransferase that mediates direct flavone C-glucosylation in Gentiana triflora. FEBS Lett. 2015, 589:182-187.
    • (2015) FEBS Lett. , vol.589 , pp. 182-187
    • Sasaki, N.1    Nishizaki, Y.2    Yamada, E.3    Tatsuzawa, F.4    Nakatsuka, T.5    Takahashi, H.6
  • 145
    • 84888132121 scopus 로고    scopus 로고
    • Continuous production of β-d-fructofuranosyl-(→ 1)-2-acetamido-2-deoxy-α-d-glucopyranoside (N-acetylsucrosamine) using a column reactor packed with β-fructofuranosidase-containing mycelia of Aspergillus oryzae immobilized on a porous carrier
    • Sato H., Yokochi S., Kasama T., Hirano T., Hakamata W., Nishio T. Continuous production of β-d-fructofuranosyl-(→ 1)-2-acetamido-2-deoxy-α-d-glucopyranoside (N-acetylsucrosamine) using a column reactor packed with β-fructofuranosidase-containing mycelia of Aspergillus oryzae immobilized on a porous carrier. J. Appl. Glycosci. 2012, 59:153-160.
    • (2012) J. Appl. Glycosci. , vol.59 , pp. 153-160
    • Sato, H.1    Yokochi, S.2    Kasama, T.3    Hirano, T.4    Hakamata, W.5    Nishio, T.6
  • 146
    • 46449118775 scopus 로고    scopus 로고
    • Broadening the biocatalytic properties of recombinant sucrose synthase 1 from potato (Solanum tuberosum L.) by expression in Escherichia coli and Saccharomyces cerevisiae
    • Sauerzapfe B., Engels L., Elling L. Broadening the biocatalytic properties of recombinant sucrose synthase 1 from potato (Solanum tuberosum L.) by expression in Escherichia coli and Saccharomyces cerevisiae. Enzym. Microb. Technol. 2008, 43:289-296.
    • (2008) Enzym. Microb. Technol. , vol.43 , pp. 289-296
    • Sauerzapfe, B.1    Engels, L.2    Elling, L.3
  • 147
    • 60449095770 scopus 로고    scopus 로고
    • Chemo-enzymatic synthesis of poly-N-acetyllactosamine (poly-LacNAc) structures and their characterization for CGL2-galectin-mediated binding of ECM glycoproteins to biomaterial surfaces
    • Sauerzapfe B., Křenek K., Schmiedel J., Wakarchuk W.W., Pelantová H., Křen V., et al. Chemo-enzymatic synthesis of poly-N-acetyllactosamine (poly-LacNAc) structures and their characterization for CGL2-galectin-mediated binding of ECM glycoproteins to biomaterial surfaces. Glycoconj. J. 2009, 26:141-159.
    • (2009) Glycoconj. J. , vol.26 , pp. 141-159
    • Sauerzapfe, B.1    Křenek, K.2    Schmiedel, J.3    Wakarchuk, W.W.4    Pelantová, H.5    Křen, V.6
  • 148
    • 7044228166 scopus 로고    scopus 로고
    • A kinetic study of sugarcane sucrose synthase
    • Schäfer W.E., Rohwer J.M., Botha F.C. A kinetic study of sugarcane sucrose synthase. Eur. J. Biochem. 2004, 271:3971-3977.
    • (2004) Eur. J. Biochem. , vol.271 , pp. 3971-3977
    • Schäfer, W.E.1    Rohwer, J.M.2    Botha, F.C.3
  • 150
    • 0029294661 scopus 로고
    • Biochemical, physiological, and molecular characterization of sucrose synthase from Daucus carota
    • Sebkova V., Unger C., Hardegger M., Sturm A. Biochemical, physiological, and molecular characterization of sucrose synthase from Daucus carota. Plant Physiol. 1995, 108:75-83.
    • (1995) Plant Physiol. , vol.108 , pp. 75-83
    • Sebkova, V.1    Unger, C.2    Hardegger, M.3    Sturm, A.4
  • 151
    • 33750298166 scopus 로고    scopus 로고
    • Glycosylation with activated sugars using glycosyltransferases and transglycosidases
    • Seibel J., Jördening H.-J., Buchholz K. Glycosylation with activated sugars using glycosyltransferases and transglycosidases. Biocatal. Biotransform. 2006, 24:311-342.
    • (2006) Biocatal. Biotransform. , vol.24 , pp. 311-342
    • Seibel, J.1    Jördening, H.-J.2    Buchholz, K.3
  • 152
    • 0141482140 scopus 로고    scopus 로고
    • Enhanced production of α-galactosyl epitopes by metabolically engineered Pichia pastoris
    • Shao J., Hayashi T., Wang P.G. Enhanced production of α-galactosyl epitopes by metabolically engineered Pichia pastoris. Appl. Environ. Microbiol. 2003, 69:5238-5242.
    • (2003) Appl. Environ. Microbiol. , vol.69 , pp. 5238-5242
    • Shao, J.1    Hayashi, T.2    Wang, P.G.3
  • 153
    • 67650516761 scopus 로고    scopus 로고
    • The crystal structures of the open and catalytically competent closed conformation of Escherichia coli glycogen synthase
    • Sheng F., Jia X., Yep A., Preiss J., Geiger J.H. The crystal structures of the open and catalytically competent closed conformation of Escherichia coli glycogen synthase. J. Biol. Chem. 2009, 284:17796-17807.
    • (2009) J. Biol. Chem. , vol.284 , pp. 17796-17807
    • Sheng, F.1    Jia, X.2    Yep, A.3    Preiss, J.4    Geiger, J.H.5
  • 154
    • 0014980545 scopus 로고
    • Studies on UDP-glucose: d-fructose 2-glucosyltransferase from tapioca tuber
    • Shukla R.N., Sanwal G.G. Studies on UDP-glucose: d-fructose 2-glucosyltransferase from tapioca tuber. Arch. Biochem. Biophys. 1971, 142:303-309.
    • (1971) Arch. Biochem. Biophys. , vol.142 , pp. 303-309
    • Shukla, R.N.1    Sanwal, G.G.2
  • 155
    • 0036010672 scopus 로고    scopus 로고
    • Metabolizable and non-metabolizable sugars activate different signal transduction pathways in tomato
    • Sinha A.K., Hofmann M.G., Römer U., Köckenberger W., Elling L., Roitsch T. Metabolizable and non-metabolizable sugars activate different signal transduction pathways in tomato. Plant Physiol. 2002, 128:1480-1489.
    • (2002) Plant Physiol. , vol.128 , pp. 1480-1489
    • Sinha, A.K.1    Hofmann, M.G.2    Römer, U.3    Köckenberger, W.4    Elling, L.5    Roitsch, T.6
  • 156
    • 70849089731 scopus 로고    scopus 로고
    • Production of flavonoid O-glucoside using sucrose synthase and flavonoid O-glucosyltransferase fusion protein
    • Son M.H., Kim B.G., Kim D.H., Jin M., Kim K., Ahn J.H. Production of flavonoid O-glucoside using sucrose synthase and flavonoid O-glucosyltransferase fusion protein. J. Microbiol. Biotechnol. 2009, 19:709-712.
    • (2009) J. Microbiol. Biotechnol. , vol.19 , pp. 709-712
    • Son, M.H.1    Kim, B.G.2    Kim, D.H.3    Jin, M.4    Kim, K.5    Ahn, J.H.6
  • 157
    • 33748235492 scopus 로고
    • Synthesis of dTDP-6-deoxy-4-ketoglucose and analogues with native and recombinant dTDP-glucose-4,6-dehydratase
    • Stein A., Kula M.-R., Elling L., Verseck S., Klaffke W. Synthesis of dTDP-6-deoxy-4-ketoglucose and analogues with native and recombinant dTDP-glucose-4,6-dehydratase. Angew. Chem. Int. Ed. 1995, 34:1748-1749.
    • (1995) Angew. Chem. Int. Ed. , vol.34 , pp. 1748-1749
    • Stein, A.1    Kula, M.-R.2    Elling, L.3    Verseck, S.4    Klaffke, W.5
  • 158
    • 0031809937 scopus 로고    scopus 로고
    • Combined preparative enzymatic synthesis of dTDP-6-deoxy-4-keto-d-glucose from dTDP and sucrose
    • Stein A., Kula M.-R., Elling L. Combined preparative enzymatic synthesis of dTDP-6-deoxy-4-keto-d-glucose from dTDP and sucrose. Glycoconj. J. 1998, 15:139-145.
    • (1998) Glycoconj. J. , vol.15 , pp. 139-145
    • Stein, A.1    Kula, M.-R.2    Elling, L.3
  • 160
    • 0345255484 scopus 로고
    • Sucrose synthase in wild tomato, Lycopersicon chmielewskii, and tomato fruit sink strength
    • Sun J., Loboda T., Sung S.-J.S., Black C.C. Sucrose synthase in wild tomato, Lycopersicon chmielewskii, and tomato fruit sink strength. Plant Physiol. 1992, 98:1163-1169.
    • (1992) Plant Physiol. , vol.98 , pp. 1163-1169
    • Sun, J.1    Loboda, T.2    Sung, S.-J.S.3    Black, C.C.4
  • 161
    • 0030469927 scopus 로고    scopus 로고
    • Occurrence of two sucrose synthase isozymes during maturation of Japanese pear fruit
    • Suzuki A., Kanayama Y., Yamaki S. Occurrence of two sucrose synthase isozymes during maturation of Japanese pear fruit. J. Am. Soc. Hortic. Sci. 1996, 121:943-947.
    • (1996) J. Am. Soc. Hortic. Sci. , vol.121 , pp. 943-947
    • Suzuki, A.1    Kanayama, Y.2    Yamaki, S.3
  • 162
    • 0034028935 scopus 로고    scopus 로고
    • Purification and characterization of two sucrose synthase isoforms from Japanese pear fruit
    • Tanase K., Yamaki S. Purification and characterization of two sucrose synthase isoforms from Japanese pear fruit. Plant Cell Physiol. 2000, 41:408-414.
    • (2000) Plant Cell Physiol. , vol.41 , pp. 408-414
    • Tanase, K.1    Yamaki, S.2
  • 163
    • 0036097484 scopus 로고    scopus 로고
    • Changes in the phosphorylation state of sucrose synthase during development of Japanese pear fruit
    • Tanase K., Shiratake K., Mori H., Yamaki S. Changes in the phosphorylation state of sucrose synthase during development of Japanese pear fruit. Physiol. Plant. 2002, 114:21-26.
    • (2002) Physiol. Plant. , vol.114 , pp. 21-26
    • Tanase, K.1    Shiratake, K.2    Mori, H.3    Yamaki, S.4
  • 164
    • 84904807319 scopus 로고    scopus 로고
    • A practical glycosyltransferase assay for the identification of new inhibitor chemotypes
    • Tedaldi L., Evitt A., Göös N., Jiang J., Wagner G.K. A practical glycosyltransferase assay for the identification of new inhibitor chemotypes. MedChemComm 2014, 5:1193-1201.
    • (2014) MedChemComm , vol.5 , pp. 1193-1201
    • Tedaldi, L.1    Evitt, A.2    Göös, N.3    Jiang, J.4    Wagner, G.K.5
  • 165
    • 84870499885 scopus 로고    scopus 로고
    • In situ UDP-glucose regeneration unravels diverse functions of plant secondary product glycosyltransferases
    • Terasaka K., Mizutani Y., Nagatsu A., Mizukami H. In situ UDP-glucose regeneration unravels diverse functions of plant secondary product glycosyltransferases. FEBS Lett. 2012, 586:4344-4350.
    • (2012) FEBS Lett. , vol.586 , pp. 4344-4350
    • Terasaka, K.1    Mizutani, Y.2    Nagatsu, A.3    Mizukami, H.4
  • 166
    • 0037617267 scopus 로고
    • Sucrose-UDP glucosyltransferase of Zea mays endosperm
    • Tsai C.-Y. Sucrose-UDP glucosyltransferase of Zea mays endosperm. Phytochemistry 1974, 13:885-891.
    • (1974) Phytochemistry , vol.13 , pp. 885-891
    • Tsai, C.-Y.1
  • 167
    • 0038356588 scopus 로고    scopus 로고
    • Identification of rice manganese-dependent protein kinases that phosphorylate sucrose synthase at multiple serine residues
    • Tsai Z.-C., Wang A.-Y. Identification of rice manganese-dependent protein kinases that phosphorylate sucrose synthase at multiple serine residues. Bot. Bull. Acad. Sin. 2003, 44:141-150.
    • (2003) Bot. Bull. Acad. Sin. , vol.44 , pp. 141-150
    • Tsai, Z.-C.1    Wang, A.-Y.2
  • 168
  • 169
    • 77956534307 scopus 로고    scopus 로고
    • A framework for classification of prokaryotic protein kinases
    • Tyagi N., Anamika K., Srinivasan N. A framework for classification of prokaryotic protein kinases. PLoS One 2010, 5.
    • (2010) PLoS One , vol.5
    • Tyagi, N.1    Anamika, K.2    Srinivasan, N.3
  • 170
    • 0025630354 scopus 로고
    • High-efficiency synthesis of sialyloligosaccharides and sialoglycopeptides
    • Unverzagt C., Kunz H., Paulson J.C. High-efficiency synthesis of sialyloligosaccharides and sialoglycopeptides. J. Am. Chem. Soc. 1990, 112:9308-9309.
    • (1990) J. Am. Chem. Soc. , vol.112 , pp. 9308-9309
    • Unverzagt, C.1    Kunz, H.2    Paulson, J.C.3
  • 171
    • 54249164978 scopus 로고    scopus 로고
    • Thermostable variants constructed via the structure-guided consensus method also show increased stability in salts solutions and homogeneous aqueous-organic media
    • Vazquez-Figueroa E., Yeh V., Broering J.M., Chaparro-Riggers J.F., Bommarius A.S. Thermostable variants constructed via the structure-guided consensus method also show increased stability in salts solutions and homogeneous aqueous-organic media. Protein Eng. Des. Sel. 2008, 21:673-680.
    • (2008) Protein Eng. Des. Sel. , vol.21 , pp. 673-680
    • Vazquez-Figueroa, E.1    Yeh, V.2    Broering, J.M.3    Chaparro-Riggers, J.F.4    Bommarius, A.S.5
  • 172
    • 47049105152 scopus 로고    scopus 로고
    • Structural and enzymatic analysis of MshA from Corynebacterium glutamicum: substrate-assisted catalysis
    • Vetting M.W., Frantom P.A., Blanchard J.S. Structural and enzymatic analysis of MshA from Corynebacterium glutamicum: substrate-assisted catalysis. J. Biol. Chem. 2008, 283:15834-15844.
    • (2008) J. Biol. Chem. , vol.283 , pp. 15834-15844
    • Vetting, M.W.1    Frantom, P.A.2    Blanchard, J.S.3
  • 175
    • 33644816557 scopus 로고    scopus 로고
    • In vitro galactosylation of human IgG at 1 kg scale using recombinant galactosyltransferase
    • Warnock D., Bai X., Autote K., Gonzales J., Kinealy K., Yan B., et al. In vitro galactosylation of human IgG at 1 kg scale using recombinant galactosyltransferase. Biotechnol. Bioeng. 2005, 92:831-842.
    • (2005) Biotechnol. Bioeng. , vol.92 , pp. 831-842
    • Warnock, D.1    Bai, X.2    Autote, K.3    Gonzales, J.4    Kinealy, K.5    Yan, B.6
  • 176
    • 46849095162 scopus 로고    scopus 로고
    • Glycosyltransferase-catalyzed synthesis of bioactive oligosaccharides
    • Weijers C.A.G.M., Franssen M.C.R., Visser G.M. Glycosyltransferase-catalyzed synthesis of bioactive oligosaccharides. Biotechnol. Adv. 2008, 26:436-456.
    • (2008) Biotechnol. Adv. , vol.26 , pp. 436-456
    • Weijers, C.A.G.M.1    Franssen, M.C.R.2    Visser, G.M.3
  • 178
    • 0016335313 scopus 로고
    • Studies on sucrose synthetase: kinetic mechanism
    • Wolosiuk R.A., Pontis H.G. Studies on sucrose synthetase: kinetic mechanism. Arch. Biochem. Biophys. 1974, 165:140-145.
    • (1974) Arch. Biochem. Biophys. , vol.165 , pp. 140-145
    • Wolosiuk, R.A.1    Pontis, H.G.2
  • 179
    • 84938878456 scopus 로고    scopus 로고
    • The crystal structure of Nitrosomonas europaea sucrose synthase reveals critical conformational changes and insights into the sucrose metabolism in prokaryotes
    • Wu R., Asención Diez M.D., Figueroa C.M., Machtey M., Iglesias A.A., Ballicora M.A., et al. The crystal structure of Nitrosomonas europaea sucrose synthase reveals critical conformational changes and insights into the sucrose metabolism in prokaryotes. J. Bacteriol. 2015, 197:2734-2746.
    • (2015) J. Bacteriol. , vol.197 , pp. 2734-2746
    • Wu, R.1    Asención Diez, M.D.2    Figueroa, C.M.3    Machtey, M.4    Iglesias, A.A.5    Ballicora, M.A.6
  • 180
    • 84922649036 scopus 로고    scopus 로고
    • Advances in the biotechnological glycosylation of valuable flavonoids
    • Xiao J., Muzashvili T.S., Georgiev M.I. Advances in the biotechnological glycosylation of valuable flavonoids. Biotechnol. Adv. 2014, 32:1145-1156.
    • (2014) Biotechnol. Adv. , vol.32 , pp. 1145-1156
    • Xiao, J.1    Muzashvili, T.S.2    Georgiev, M.I.3
  • 181
    • 0029878026 scopus 로고    scopus 로고
    • A novel three-enzyme reaction cycle for the synthesis of N-acetyllactosamine with in situ regeneration of uridine 5'-diphosphate glucose and uridine 5'-diphosphate galactose
    • Zervosen A., Elling L. A novel three-enzyme reaction cycle for the synthesis of N-acetyllactosamine with in situ regeneration of uridine 5'-diphosphate glucose and uridine 5'-diphosphate galactose. J. Am. Chem. Soc. 1996, 118:1836-1840.
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 1836-1840
    • Zervosen, A.1    Elling, L.2
  • 182
    • 33748216418 scopus 로고
    • Continuous enzymatic synthesis of 2'-deoxythymidine-5'-(α-D-glucopyranosyl)diphosphate
    • Zervosen A., Elling L., Kula M.-R. Continuous enzymatic synthesis of 2'-deoxythymidine-5'-(α-D-glucopyranosyl)diphosphate. Angew. Chem. Int. Ed. 1994, 33:571-572.
    • (1994) Angew. Chem. Int. Ed. , vol.33 , pp. 571-572
    • Zervosen, A.1    Elling, L.2    Kula, M.-R.3
  • 183
    • 0030025135 scopus 로고    scopus 로고
    • Combined enzymatic synthesis of nucleotide (deoxy) sugars from sucrose and nucleoside monophosphates
    • Zervosen A., Stein A., Adrian H., Elling L. Combined enzymatic synthesis of nucleotide (deoxy) sugars from sucrose and nucleoside monophosphates. Tetrahedron 1996, 52:2395-2404.
    • (1996) Tetrahedron , vol.52 , pp. 2395-2404
    • Zervosen, A.1    Stein, A.2    Adrian, H.3    Elling, L.4
  • 184
    • 0032530911 scopus 로고    scopus 로고
    • Application of recombinant sucrose synthase-large scale synthesis of ADP-glucose
    • Zervosen A., Römer U., Elling L. Application of recombinant sucrose synthase-large scale synthesis of ADP-glucose. J. Mol. Catal. B Enzym. 1998, 5:25-28.
    • (1998) J. Mol. Catal. B Enzym. , vol.5 , pp. 25-28
    • Zervosen, A.1    Römer, U.2    Elling, L.3
  • 185
  • 186
    • 0033230767 scopus 로고    scopus 로고
    • Soybean nodule sucrose synthase (nodulin-100): further analysis of its phosphorylation using recombinant and authentic root-nodule enzymes
    • Zhang X.Q., Lund A.A., Sarath G., Cerny R.L., Roberts D.M., Chollet R. Soybean nodule sucrose synthase (nodulin-100): further analysis of its phosphorylation using recombinant and authentic root-nodule enzymes. Arch. Biochem. Biophys. 1999, 371:70-82.
    • (1999) Arch. Biochem. Biophys. , vol.371 , pp. 70-82
    • Zhang, X.Q.1    Lund, A.A.2    Sarath, G.3    Cerny, R.L.4    Roberts, D.M.5    Chollet, R.6
  • 187
    • 30744463252 scopus 로고    scopus 로고
    • Protein phosphorylation on Ser, Thr and Tyr residues in cyanobacteria
    • Zhang C.C., Jang J., Sakr S., Wang L. Protein phosphorylation on Ser, Thr and Tyr residues in cyanobacteria. J. Mol. Microbiol. Biotechnol. 2005, 9:154-166.
    • (2005) J. Mol. Microbiol. Biotechnol. , vol.9 , pp. 154-166
    • Zhang, C.C.1    Jang, J.2    Sakr, S.3    Wang, L.4
  • 188
    • 33748302743 scopus 로고    scopus 로고
    • Exploiting the reversibility of natural product glycosyltransferase-catalyzed reactions
    • Zhang C., Griffith B.R., Fu Q., Albermann C., Fu X., Lee I.-K., et al. Exploiting the reversibility of natural product glycosyltransferase-catalyzed reactions. Science 2006, 313:1291-1294.
    • (2006) Science , vol.313 , pp. 1291-1294
    • Zhang, C.1    Griffith, B.R.2    Fu, Q.3    Albermann, C.4    Fu, X.5    Lee, I.-K.6
  • 189
    • 80053917641 scopus 로고    scopus 로고
    • The structure of sucrose synthase-from Arabidopsis thaliana and its functional implications
    • Zheng Y., Anderson S., Zhang Y., Garavito R.M. The structure of sucrose synthase-from Arabidopsis thaliana and its functional implications. J. Biol. Chem. 2011, 286:36108-36118.
    • (2011) J. Biol. Chem. , vol.286 , pp. 36108-36118
    • Zheng, Y.1    Anderson, S.2    Zhang, Y.3    Garavito, R.M.4


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