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Volumn 12, Issue 5, 2008, Pages 556-564

The impact of enzyme engineering upon natural product glycodiversification

Author keywords

[No Author keywords available]

Indexed keywords

GLYCOSYLTRANSFERASE; NATURAL PRODUCT;

EID: 54049149694     PISSN: 13675931     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cbpa.2008.07.013     Document Type: Review
Times cited : (87)

References (71)
  • 1
    • 58149163598 scopus 로고    scopus 로고
    • Williams GJ, Zhang C, Thorson JS: Natural product glycosyltransferases: Properties and applications. Adv Enzymol Relat Areas Mol Biol, 76, in press.
    • Williams GJ, Zhang C, Thorson JS: Natural product glycosyltransferases: Properties and applications. Adv Enzymol Relat Areas Mol Biol, 76, in press.
  • 2
    • 0031127564 scopus 로고    scopus 로고
    • The role of carbohydrates in biologically active natural products
    • Weymouth-Wilson A.C. The role of carbohydrates in biologically active natural products. Nat Prod Rep 14 (1997) 99-110
    • (1997) Nat Prod Rep , vol.14 , pp. 99-110
    • Weymouth-Wilson, A.C.1
  • 3
    • 49749126041 scopus 로고    scopus 로고
    • Sweet antibiotics - the role of glycosidic residues in antibiotic and antitumor activity and their randomization
    • Křen V., and Řezanka T. Sweet antibiotics - the role of glycosidic residues in antibiotic and antitumor activity and their randomization. FEMS Microbiol Rev 32 (2008) 858-889
    • (2008) FEMS Microbiol Rev , vol.32 , pp. 858-889
    • Křen, V.1    Řezanka, T.2
  • 6
    • 34247109045 scopus 로고    scopus 로고
    • Natural products as sources of new drugs over the last 25 years
    • Newman D.J., and Cragg G.M. Natural products as sources of new drugs over the last 25 years. J Nat Prod 70 (2007) 461-477
    • (2007) J Nat Prod , vol.70 , pp. 461-477
    • Newman, D.J.1    Cragg, G.M.2
  • 7
    • 42949160050 scopus 로고    scopus 로고
    • Natural products as leads to potential drugs: an old process or the new hope for drug discovery?
    • Newman D.J. Natural products as leads to potential drugs: an old process or the new hope for drug discovery?. J Med Chem 51 (2008) 2589-2599
    • (2008) J Med Chem , vol.51 , pp. 2589-2599
    • Newman, D.J.1
  • 8
    • 38449094992 scopus 로고    scopus 로고
    • Mother Nature's gifts to diseases of man: the impact of natural products on anti-infective, anticholestemics and anticancer drug discovery
    • Butler M.S., and Newman D.J. Mother Nature's gifts to diseases of man: the impact of natural products on anti-infective, anticholestemics and anticancer drug discovery. Prog Drug Res 65 1 (2008) 3-44
    • (2008) Prog Drug Res , vol.65 , Issue.1 , pp. 3-44
    • Butler, M.S.1    Newman, D.J.2
  • 9
    • 44249098800 scopus 로고    scopus 로고
    • Natural products to drugs: natural product-derived compounds in clinical trials
    • Butler M.S. Natural products to drugs: natural product-derived compounds in clinical trials. Nat Product Rep 25 (2008) 475-516
    • (2008) Nat Product Rep , vol.25 , pp. 475-516
    • Butler, M.S.1
  • 10
    • 33750921265 scopus 로고    scopus 로고
    • De novo asymmetric syntheses of SL0101 and its analogues via a palladium-catalyzed glycosylation
    • Shan M., and O'Doherty G.A. De novo asymmetric syntheses of SL0101 and its analogues via a palladium-catalyzed glycosylation. Org Lett 8 (2006) 5149-5152
    • (2006) Org Lett , vol.8 , pp. 5149-5152
    • Shan, M.1    O'Doherty, G.A.2
  • 11
    • 34447313701 scopus 로고    scopus 로고
    • De novo asymmetric synthesis of the anthrax tetrasaccharide by a palladium-catalyzed glycosylation reaction
    • Guo H., and O'Doherty G.A. De novo asymmetric synthesis of the anthrax tetrasaccharide by a palladium-catalyzed glycosylation reaction. Angew Chem Int Ed Engl 46 (2007) 5206-5208
    • (2007) Angew Chem Int Ed Engl , vol.46 , pp. 5206-5208
    • Guo, H.1    O'Doherty, G.A.2
  • 12
    • 34047220599 scopus 로고    scopus 로고
    • De novo approach to 2-deoxy-β-glycosides: asymmetric syntheses of digoxose and digitoxin
    • Zhou M., and O'Doherty G.A. De novo approach to 2-deoxy-β-glycosides: asymmetric syntheses of digoxose and digitoxin. J Org Chem 72 (2007) 2485-2493
    • (2007) J Org Chem , vol.72 , pp. 2485-2493
    • Zhou, M.1    O'Doherty, G.A.2
  • 13
    • 29044436566 scopus 로고    scopus 로고
    • Neoglycorandomization and chemoenzymatic glycorandomization: two complementary tools for natural product diversification
    • Langenhan J.M., Griffith B.R., and Thorson J.S. Neoglycorandomization and chemoenzymatic glycorandomization: two complementary tools for natural product diversification. J Nat Prod 68 (2005) 1696-1711
    • (2005) J Nat Prod , vol.68 , pp. 1696-1711
    • Langenhan, J.M.1    Griffith, B.R.2    Thorson, J.S.3
  • 14
    • 34447255199 scopus 로고    scopus 로고
    • Model for antibiotic optimization via neoglycosylation: Synthesis of liponeoglycopeptides active against VRE
    • This paper describes the installation of all possible N-decanoylglucopyranose and N-biphenoylglucopyranose regioisomers onto the vancomycin aglycon. In contrast to prior work, optimal antibacterial activity via lipidation resulted from modification of the glucose C3' or C4'. This study highlighted the efficiency of neoglycorandomization in small molecule drug discovery.
    • Griffith B.R., Krepel C., Fu X., Blanchard S., Ahmed A., Edmiston C.E., and Thorson J.S. Model for antibiotic optimization via neoglycosylation: Synthesis of liponeoglycopeptides active against VRE. J Am Chem Soc 129 (2007) 8150-8155. This paper describes the installation of all possible N-decanoylglucopyranose and N-biphenoylglucopyranose regioisomers onto the vancomycin aglycon. In contrast to prior work, optimal antibacterial activity via lipidation resulted from modification of the glucose C3' or C4'. This study highlighted the efficiency of neoglycorandomization in small molecule drug discovery.
    • (2007) J Am Chem Soc , vol.129 , pp. 8150-8155
    • Griffith, B.R.1    Krepel, C.2    Fu, X.3    Blanchard, S.4    Ahmed, A.5    Edmiston, C.E.6    Thorson, J.S.7
  • 16
    • 34247626294 scopus 로고    scopus 로고
    • Unusual sugar biosynthesis and natural product glycodiversification
    • This review expertly summarizes both in vivo and in vitro approaches to natural product glycodiversification.
    • Thibodeaux C.J., Melancon C.E., and Liu H.W. Unusual sugar biosynthesis and natural product glycodiversification. Nature 446 (2007) 1008-1016. This review expertly summarizes both in vivo and in vitro approaches to natural product glycodiversification.
    • (2007) Nature , vol.446 , pp. 1008-1016
    • Thibodeaux, C.J.1    Melancon, C.E.2    Liu, H.W.3
  • 17
    • 34247511117 scopus 로고    scopus 로고
    • Engineering the glycosylation of natural products in actinomycetes
    • Salas J.A., and Mendez C. Engineering the glycosylation of natural products in actinomycetes. Trends Microbiol 15 (2007) 219-232
    • (2007) Trends Microbiol , vol.15 , pp. 219-232
    • Salas, J.A.1    Mendez, C.2
  • 18
    • 17844409813 scopus 로고    scopus 로고
    • Diversifying vancomycin via chemoenzymatic strategies
    • Fu X., Albermann C., Zhang C., and Thorson J.S. Diversifying vancomycin via chemoenzymatic strategies. Org Lett 7 (2005) 1513-1515
    • (2005) Org Lett , vol.7 , pp. 1513-1515
    • Fu, X.1    Albermann, C.2    Zhang, C.3    Thorson, J.S.4
  • 19
    • 33845935524 scopus 로고    scopus 로고
    • The in vitro characterization of the iterative avermectin glycosyltransferase AveBI reveals reaction reversibility and sugar nucleotide flexibility
    • Zhang C., Albermann C., Fu X., and Thorson J.S. The in vitro characterization of the iterative avermectin glycosyltransferase AveBI reveals reaction reversibility and sugar nucleotide flexibility. J Am Chem Soc 128 (2006) 16420-16421
    • (2006) J Am Chem Soc , vol.128 , pp. 16420-16421
    • Zhang, C.1    Albermann, C.2    Fu, X.3    Thorson, J.S.4
  • 20
    • 33748302743 scopus 로고    scopus 로고
    • Exploiting the reversibility of natural product glycosyltransferase-catalyzed reactions
    • In this seminal report, the reversibility of four GTs was used to prepare more than 70 differentially glycosylated calicheamicin and vancomycin analogs in 'sugar-exchange' and 'aglycone-exchange' reactions.
    • Zhang C., Griffith B.R., Fu Q., Albermann C., Fu X., Lee I.K., Li L., and Thorson J.S. Exploiting the reversibility of natural product glycosyltransferase-catalyzed reactions. Science 313 (2006) 1291-1294. In this seminal report, the reversibility of four GTs was used to prepare more than 70 differentially glycosylated calicheamicin and vancomycin analogs in 'sugar-exchange' and 'aglycone-exchange' reactions.
    • (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    Li, L.7    Thorson, J.S.8
  • 22
    • 18244392948 scopus 로고    scopus 로고
    • Enzymatic approach to unnatural glycosides with diverse aglycon scaffolds using glycosyltransferase VinC
    • This study reports on the substrate promiscuity of a macrolactam GT VinC. The authors discovered that the enzyme accepted both α- and β-anomers of several dTDP-2-deoxy-d-sugars to produce the β- and α-glycosides, respectively. Subsequently, a set of 22 diverse glycosides was constructed using VinC, and a mechanistic model proposed to explain the finding.
    • Minami A., Uchida R., Eguchi T., and Kakinuma K. Enzymatic approach to unnatural glycosides with diverse aglycon scaffolds using glycosyltransferase VinC. J Am Chem Soc 127 (2005) 6148-6149. This study reports on the substrate promiscuity of a macrolactam GT VinC. The authors discovered that the enzyme accepted both α- and β-anomers of several dTDP-2-deoxy-d-sugars to produce the β- and α-glycosides, respectively. Subsequently, a set of 22 diverse glycosides was constructed using VinC, and a mechanistic model proposed to explain the finding.
    • (2005) J Am Chem Soc , vol.127 , pp. 6148-6149
    • Minami, A.1    Uchida, R.2    Eguchi, T.3    Kakinuma, K.4
  • 23
    • 34247496765 scopus 로고    scopus 로고
    • Substrate flexibility of vicenisaminyltransferase VinC involved in the biosynthesis of vicenistatin
    • Minami A., and Eguchi T. Substrate flexibility of vicenisaminyltransferase VinC involved in the biosynthesis of vicenistatin. J Am Chem Soc 129 (2007) 5102-5107
    • (2007) J Am Chem Soc , vol.129 , pp. 5102-5107
    • Minami, A.1    Eguchi, T.2
  • 25
    • 34247518972 scopus 로고    scopus 로고
    • The in vitro characterization of the erythronolide mycarosyltransferase EryBV and its utility in macrolide diversification
    • Zhang C., Fu Q., Albermann C., Li L., and Thorson J.S. The in vitro characterization of the erythronolide mycarosyltransferase EryBV and its utility in macrolide diversification. ChemBioChem 8 (2007) 385-390
    • (2007) ChemBioChem , vol.8 , pp. 385-390
    • Zhang, C.1    Fu, Q.2    Albermann, C.3    Li, L.4    Thorson, J.S.5
  • 26
    • 0345255629 scopus 로고    scopus 로고
    • Creation of the first anomeric d/l-sugar kinase by means of directed evolution
    • Hoffmeister D., Yang J., Liu L., and Thorson J.S. Creation of the first anomeric d/l-sugar kinase by means of directed evolution. Proc Natl Acad Sci U S A 100 (2003) 13184-13189
    • (2003) Proc Natl Acad Sci U S A , vol.100 , pp. 13184-13189
    • Hoffmeister, D.1    Yang, J.2    Liu, L.3    Thorson, J.S.4
  • 27
    • 4644229580 scopus 로고    scopus 로고
    • Structure-based enhancement of the first anomeric glucokinase
    • Yang J., Liu L., and Thorson J.S. Structure-based enhancement of the first anomeric glucokinase. ChemBioChem 5 (2004) 992-996
    • (2004) ChemBioChem , vol.5 , pp. 992-996
    • Yang, J.1    Liu, L.2    Thorson, J.S.3
  • 28
    • 24944496018 scopus 로고    scopus 로고
    • Structure-based engineering of E. coli galactokinase as a first step toward in vivo glycorandomization
    • Yang J., Fu X., Liao J., Liu L., and Thorson J.S. Structure-based engineering of E. coli galactokinase as a first step toward in vivo glycorandomization. Chem Biol 12 (2005) 657-664
    • (2005) Chem Biol , vol.12 , pp. 657-664
    • Yang, J.1    Fu, X.2    Liao, J.3    Liu, L.4    Thorson, J.S.5
  • 30
    • 0037109032 scopus 로고    scopus 로고
    • Expanding pyrimidine diphosphosugar libraries via structure-based nucleotidylyltransferase engineering
    • Barton W.A., Biggins J.B., Jiang J., Thorson J.S., and Nikolov D.B. Expanding pyrimidine diphosphosugar libraries via structure-based nucleotidylyltransferase engineering. Proc Natl Acad Sci U S A 99 (2002) 13397-13402
    • (2002) Proc Natl Acad Sci U S A , vol.99 , pp. 13397-13402
    • Barton, W.A.1    Biggins, J.B.2    Jiang, J.3    Thorson, J.S.4    Nikolov, D.B.5
  • 31
    • 34447114483 scopus 로고    scopus 로고
    • Enhancing the latent nucleotide triphosphate flexibility of the glucose-1-phosphate thymidylyltransferase RmlA
    • Moretti R., and Thorson J.S. Enhancing the latent nucleotide triphosphate flexibility of the glucose-1-phosphate thymidylyltransferase RmlA. J Biol Chem 282 (2007) 16942-16947
    • (2007) J Biol Chem , vol.282 , pp. 16942-16947
    • Moretti, R.1    Thorson, J.S.2
  • 32
    • 54049156219 scopus 로고    scopus 로고
    • Zhang C, Jiang J, Moretti R, Thorson J: The in vitro characterization of polyene glycosyltransferases AmphDI and NysDI. Chembiochem, in press.
    • Zhang C, Jiang J, Moretti R, Thorson J: The in vitro characterization of polyene glycosyltransferases AmphDI and NysDI. Chembiochem, in press.
  • 33
    • 33947147200 scopus 로고    scopus 로고
    • Exploiting nucleotidylyltransferases to prepare sugar nucleotides
    • Timmons S.C., Mosher R.H., Knowles S.A., and Jakeman D.L. Exploiting nucleotidylyltransferases to prepare sugar nucleotides. Org Lett 9 (2007) 857-860
    • (2007) Org Lett , vol.9 , pp. 857-860
    • Timmons, S.C.1    Mosher, R.H.2    Knowles, S.A.3    Jakeman, D.L.4
  • 34
    • 38549153782 scopus 로고    scopus 로고
    • Lipophilic sugar nucleotide synthesis by structure-based design of nucleotidylyltransferase substrates
    • Huestis M.P., Aish G.A., Hui J.P., Soo E.C., and Jakeman D.L. Lipophilic sugar nucleotide synthesis by structure-based design of nucleotidylyltransferase substrates. Org Biomol Chem 6 (2008) 477-484
    • (2008) Org Biomol Chem , vol.6 , pp. 477-484
    • Huestis, M.P.1    Aish, G.A.2    Hui, J.P.3    Soo, E.C.4    Jakeman, D.L.5
  • 35
    • 38749094876 scopus 로고    scopus 로고
    • Enzyme-catalyzed synthesis of furanosyl nucleotides
    • Bacterial nucleotidyltransferases are usually used for the synthesis of hexopyranosyl nucleotides. This report describes the ability of several bacterial enzymes to couple four hexofuranosyl-1-phosphates with dTDP. This discovery should allow more extensive analysis of GT donor promiscuity.
    • Timmons S.C., Hui J.P., Pearson J.L., Peltier P., Daniellou R., Nugier-Chauvin C., Soo E.C., Syvitski R.T., Ferrieres V., and Jakeman D.L. Enzyme-catalyzed synthesis of furanosyl nucleotides. Org Lett 10 (2008) 161-163. Bacterial nucleotidyltransferases are usually used for the synthesis of hexopyranosyl nucleotides. This report describes the ability of several bacterial enzymes to couple four hexofuranosyl-1-phosphates with dTDP. This discovery should allow more extensive analysis of GT donor promiscuity.
    • (2008) Org Lett , vol.10 , pp. 161-163
    • Timmons, S.C.1    Hui, J.P.2    Pearson, J.L.3    Peltier, P.4    Daniellou, R.5    Nugier-Chauvin, C.6    Soo, E.C.7    Syvitski, R.T.8    Ferrieres, V.9    Jakeman, D.L.10
  • 36
    • 10344249453 scopus 로고    scopus 로고
    • Unusually broad substrate tolerance of a heat-stable archaeal sugar nucleotidyltransferase for the synthesis of sugar nucleotides
    • Mizanur R.M., Zea C.J., Pohl N.L., Ko K.S., Zea C.J., and Pohl N.L. Unusually broad substrate tolerance of a heat-stable archaeal sugar nucleotidyltransferase for the synthesis of sugar nucleotides. J Am Chem Soc 126 (2004) 15993-15998
    • (2004) J Am Chem Soc , vol.126 , pp. 15993-15998
    • Mizanur, R.M.1    Zea, C.J.2    Pohl, N.L.3    Ko, K.S.4    Zea, C.J.5    Pohl, N.L.6
  • 37
    • 14544299580 scopus 로고    scopus 로고
    • Strategies for the chemoenzymatic synthesis of deoxysugar nucleotides: substrate binding versus catalysis
    • Ko K.S., Zea C.J., Pohl N.L., Mizanur R.M., Zea C.J., and Pohl N.L. Strategies for the chemoenzymatic synthesis of deoxysugar nucleotides: substrate binding versus catalysis. J Org Chem 70 (2005) 1919-1921
    • (2005) J Org Chem , vol.70 , pp. 1919-1921
    • Ko, K.S.1    Zea, C.J.2    Pohl, N.L.3    Mizanur, R.M.4    Zea, C.J.5    Pohl, N.L.6
  • 38
    • 43049088411 scopus 로고    scopus 로고
    • A comparison of sugar indicators enables a universal high-throughput sugar-1-phosphate nucleotidyltransferase assay
    • Moretti R., and Thorson J.S. A comparison of sugar indicators enables a universal high-throughput sugar-1-phosphate nucleotidyltransferase assay. Anal Biochem 377 (2008) 251-258
    • (2008) Anal Biochem , vol.377 , pp. 251-258
    • Moretti, R.1    Thorson, J.S.2
  • 39
    • 38049110218 scopus 로고    scopus 로고
    • Exploring specificity of glycosyltransferases: synthesis of new sugar nucleotide related molecules as putative donor substrates
    • Khaled A., Piotrowska O., Dominiak K., and Auge C. Exploring specificity of glycosyltransferases: synthesis of new sugar nucleotide related molecules as putative donor substrates. Carbohydr Res 343 (2008) 167-178
    • (2008) Carbohydr Res , vol.343 , pp. 167-178
    • Khaled, A.1    Piotrowska, O.2    Dominiak, K.3    Auge, C.4
  • 40
    • 33744523569 scopus 로고    scopus 로고
    • Enzymatic tools for engineering natural product glycosylation
    • Blanchard S., and Thorson J.S. Enzymatic tools for engineering natural product glycosylation. Curr Opin Chem Biol 10 (2006) 263-271
    • (2006) Curr Opin Chem Biol , vol.10 , pp. 263-271
    • Blanchard, S.1    Thorson, J.S.2
  • 41
    • 0035986693 scopus 로고    scopus 로고
    • Engineering deoxysugar biosynthetic pathways from antibiotic-producing microorganisms. A tool to produce novel glycosylated bioactive compounds
    • Rodriguez L., Aguirrezabalaga I., Allende N., Brana A.F., Mendez C., and Salas J.A. Engineering deoxysugar biosynthetic pathways from antibiotic-producing microorganisms. A tool to produce novel glycosylated bioactive compounds. Chem Biol 9 (2002) 721-729
    • (2002) Chem Biol , vol.9 , pp. 721-729
    • Rodriguez, L.1    Aguirrezabalaga, I.2    Allende, N.3    Brana, A.F.4    Mendez, C.5    Salas, J.A.6
  • 42
    • 10644221353 scopus 로고    scopus 로고
    • Engineering biosynthetic pathways for deoxysugars: branched-chain sugar pathways and derivatives from the antitumor tetracenomycin
    • Lombo F., Gibson M., Greenwell L., Brana A.F., Rohr J., Salas J.A., and Mendez C. Engineering biosynthetic pathways for deoxysugars: branched-chain sugar pathways and derivatives from the antitumor tetracenomycin. Chem Biol 11 (2004) 1709-1718
    • (2004) Chem Biol , vol.11 , pp. 1709-1718
    • Lombo, F.1    Gibson, M.2    Greenwell, L.3    Brana, A.F.4    Rohr, J.5    Salas, J.A.6    Mendez, C.7
  • 43
    • 33750087290 scopus 로고    scopus 로고
    • Combinatorial biosynthesis of antitumor deoxysugar pathways in Streptomyces griseus: Reconstitution of "unnatural natural gene clusters" for the biosynthesis of four 2,6-D-dideoxyhexoses
    • Perez M., Lombo F., Baig I., Brana A.F., Rohr J., Salas J.A., and Mendez C. Combinatorial biosynthesis of antitumor deoxysugar pathways in Streptomyces griseus: Reconstitution of "unnatural natural gene clusters" for the biosynthesis of four 2,6-D-dideoxyhexoses. Appl Environ Microbiol 72 (2006) 6644-6652
    • (2006) Appl Environ Microbiol , vol.72 , pp. 6644-6652
    • Perez, M.1    Lombo, F.2    Baig, I.3    Brana, A.F.4    Rohr, J.5    Salas, J.A.6    Mendez, C.7
  • 44
    • 33847000219 scopus 로고    scopus 로고
    • Bioassay-Guided evolution of glycosylated macrolide antibiotics in Escherichia coli
    • This article describes the construction and evolutionary-optimized macrolide glycosylation pathway in E. coli and sets the stage for high-level fermentation of novel macrolide glycosides.
    • Lee H.Y., and Khosla C. Bioassay-Guided evolution of glycosylated macrolide antibiotics in Escherichia coli. PLoS Biology 5 (2007) 243-250. This article describes the construction and evolutionary-optimized macrolide glycosylation pathway in E. coli and sets the stage for high-level fermentation of novel macrolide glycosides.
    • (2007) PLoS Biology , vol.5 , pp. 243-250
    • Lee, H.Y.1    Khosla, C.2
  • 45
    • 34547596928 scopus 로고    scopus 로고
    • Selective detection of sugar phosphates by capillary electrophoresis/mass spectrometry and its application to an engineered E. coli host
    • Hui J.P., Yang J., Thorson J.S., and Soo E.C. Selective detection of sugar phosphates by capillary electrophoresis/mass spectrometry and its application to an engineered E. coli host. ChemBioChem 8 (2007) 1180-1188
    • (2007) ChemBioChem , vol.8 , pp. 1180-1188
    • Hui, J.P.1    Yang, J.2    Thorson, J.S.3    Soo, E.C.4
  • 46
    • 0034976452 scopus 로고    scopus 로고
    • Two sequence elements of glycosyltransferases involved in urdamycin biosynthesis are responsible for substrate specificity and enzymatic activity
    • Hoffmeister D., Ichinose K., and Bechthold A. Two sequence elements of glycosyltransferases involved in urdamycin biosynthesis are responsible for substrate specificity and enzymatic activity. Chem Biol 8 (2001) 557-567
    • (2001) Chem Biol , vol.8 , pp. 557-567
    • Hoffmeister, D.1    Ichinose, K.2    Bechthold, A.3
  • 48
    • 4143092938 scopus 로고    scopus 로고
    • Alteration of sugar donor specificities of plant glycosyltransferases by a single point mutation
    • Kubo A., Arai Y., Nagashima S., and Yoshikawa T. Alteration of sugar donor specificities of plant glycosyltransferases by a single point mutation. Arch Biochem Biophys 429 (2004) 198-203
    • (2004) Arch Biochem Biophys , vol.429 , pp. 198-203
    • Kubo, A.1    Arai, Y.2    Nagashima, S.3    Yoshikawa, T.4
  • 49
    • 33846815083 scopus 로고    scopus 로고
    • Characterization and engineering of glycosyltransferases responsible for steroid saponin biosynthesis in Solanaceous plants
    • Kohara A., Nakajima C., Yoshida S., and Muranaka T. Characterization and engineering of glycosyltransferases responsible for steroid saponin biosynthesis in Solanaceous plants. Phytochemistry 68 (2007) 478-486
    • (2007) Phytochemistry , vol.68 , pp. 478-486
    • Kohara, A.1    Nakajima, C.2    Yoshida, S.3    Muranaka, T.4
  • 50
    • 2442440054 scopus 로고    scopus 로고
    • Crystal structure of vancosaminyltransferase GtfD from the vancomycin biosynthetic pathway: interactions with acceptor and nucleotide ligands
    • Mulichak A.M., Lu W., Losey H.C., Walsh C.T., and Garavito R.M. Crystal structure of vancosaminyltransferase GtfD from the vancomycin biosynthetic pathway: interactions with acceptor and nucleotide ligands. Biochemistry 43 (2004) 5170-5180
    • (2004) Biochemistry , vol.43 , pp. 5170-5180
    • Mulichak, A.M.1    Lu, W.2    Losey, H.C.3    Walsh, C.T.4    Garavito, R.M.5
  • 51
    • 34248396073 scopus 로고    scopus 로고
    • The crystal structure of two macrolide glycosyltransferases provides a blueprint for host cell antibiotic immunity
    • The Streptomyces antibioticus GTs OleI and OleD are involved in host cell immunity from endogenous and exogenous agents. The crystal structures of these enzymes in conjunction with active-site mutational analysis provided insight into the mechanism of action and substrate specificity. The failure however to engineer UDP-Glc/UDP-Gal activity or to alter acceptor macrolide specificity by loop grafting and mutagenesis highlights that directed evolution methods are likely required.
    • Bolam D.N., Roberts S., Proctor M.R., Turkenburg J.P., Dodson E.J., Martinez-Fleites C., Yang M., Davis B.G., Davies G.J., and Gilbert H.J. The crystal structure of two macrolide glycosyltransferases provides a blueprint for host cell antibiotic immunity. Proc Natl Acad Sci U S A 104 (2007) 5336-5341. The Streptomyces antibioticus GTs OleI and OleD are involved in host cell immunity from endogenous and exogenous agents. The crystal structures of these enzymes in conjunction with active-site mutational analysis provided insight into the mechanism of action and substrate specificity. The failure however to engineer UDP-Glc/UDP-Gal activity or to alter acceptor macrolide specificity by loop grafting and mutagenesis highlights that directed evolution methods are likely required.
    • (2007) Proc Natl Acad Sci U S A , vol.104 , pp. 5336-5341
    • Bolam, D.N.1    Roberts, S.2    Proctor, M.R.3    Turkenburg, J.P.4    Dodson, E.J.5    Martinez-Fleites, C.6    Yang, M.7    Davis, B.G.8    Davies, G.J.9    Gilbert, H.J.10
  • 52
    • 33750974777 scopus 로고    scopus 로고
    • Insights into the synthesis of lipopolysaccharide and antibiotics through the structures of two retaining glycosyltransferases from family GT4
    • Martinez-Fleites C., Proctor M., Roberts S., Bolam D.N., Gilbert H.J., and Davies G.J. Insights into the synthesis of lipopolysaccharide and antibiotics through the structures of two retaining glycosyltransferases from family GT4. Chem Biol 13 (2006) 1143-1152
    • (2006) Chem Biol , vol.13 , pp. 1143-1152
    • Martinez-Fleites, C.1    Proctor, M.2    Roberts, S.3    Bolam, D.N.4    Gilbert, H.J.5    Davies, G.J.6
  • 53
    • 0036913910 scopus 로고    scopus 로고
    • Remarkable structural similarities between diverse glycosyltransferases
    • Hu Y., and Walker S. Remarkable structural similarities between diverse glycosyltransferases. Chem Biol 9 (2002) 1287-1296
    • (2002) Chem Biol , vol.9 , pp. 1287-1296
    • Hu, Y.1    Walker, S.2
  • 54
    • 47049087906 scopus 로고    scopus 로고
    • A kinetic analysis of regiospecific glucosylation by two glycosyltransferases of Arabidopsis thaliana: domain swapping to introduce new activities
    • Cartwright A.M., Lim E.K., Kleanthous C., and Bowles D.J. A kinetic analysis of regiospecific glucosylation by two glycosyltransferases of Arabidopsis thaliana: domain swapping to introduce new activities. J Biol Chem 283 (2008) 15724-15731
    • (2008) J Biol Chem , vol.283 , pp. 15724-15731
    • Cartwright, A.M.1    Lim, E.K.2    Kleanthous, C.3    Bowles, D.J.4
  • 55
    • 38049146159 scopus 로고    scopus 로고
    • Characterization and engineering of the bifunctional N- and O-glucosyltransferase involved in xenobiotic metabolism in plants
    • In vitro assay of a library of plant GTs identified a bifunctional N/O-GT. Subsequent crystal structure determination and successful protein engineering was used to provide unique insight into the dual N/O-glucosylation activity of the GT.
    • Brazier-Hicks M., Offen W.A., Gershater M.C., Revett T.J., Lim E.K., Bowles D.J., Davies G.J., and Edwards R. Characterization and engineering of the bifunctional N- and O-glucosyltransferase involved in xenobiotic metabolism in plants. Proc Natl Acad Sci U S A 104 (2007) 20238-20243. In vitro assay of a library of plant GTs identified a bifunctional N/O-GT. Subsequent crystal structure determination and successful protein engineering was used to provide unique insight into the dual N/O-glucosylation activity of the GT.
    • (2007) Proc Natl Acad Sci U S A , vol.104 , pp. 20238-20243
    • Brazier-Hicks, M.1    Offen, W.A.2    Gershater, M.C.3    Revett, T.J.4    Lim, E.K.5    Bowles, D.J.6    Davies, G.J.7    Edwards, R.8
  • 56
    • 33845928213 scopus 로고    scopus 로고
    • Mutational analysis of the Medicago glycosyltransferase UGT71G1 reveals residues that control regioselectivity for (iso)flavonoid glycosylation
    • He X.Z., Wang X., and Dixon R.A. Mutational analysis of the Medicago glycosyltransferase UGT71G1 reveals residues that control regioselectivity for (iso)flavonoid glycosylation. J Biol Chem 281 (2006) 34441-34447
    • (2006) J Biol Chem , vol.281 , pp. 34441-34447
    • He, X.Z.1    Wang, X.2    Dixon, R.A.3
  • 57
    • 39749108951 scopus 로고    scopus 로고
    • Applications of glycosyltransferases in the site-specific conjugation of biomolecules and the development of a targeted drug delivery system and contrast agents for MRI
    • Ramakrishnan B., Boeggeman E., and Qasba P.K. Applications of glycosyltransferases in the site-specific conjugation of biomolecules and the development of a targeted drug delivery system and contrast agents for MRI. Expert Opin Drug Deliv 5 (2008) 149-153
    • (2008) Expert Opin Drug Deliv , vol.5 , pp. 149-153
    • Ramakrishnan, B.1    Boeggeman, E.2    Qasba, P.K.3
  • 58
    • 45149125575 scopus 로고    scopus 로고
    • Site-specific linking of biomolecules via glycan residues using glycosyltransferases
    • Qasba P.K., Boeggeman E., and Ramakrishnan B. Site-specific linking of biomolecules via glycan residues using glycosyltransferases. Biotechnol Prog 24 (2008) 520-526
    • (2008) Biotechnol Prog , vol.24 , pp. 520-526
    • Qasba, P.K.1    Boeggeman, E.2    Ramakrishnan, B.3
  • 61
    • 34547651180 scopus 로고    scopus 로고
    • Structure and action of the C-C bond-forming glycosyltransferase UrdGT2 involved in the biosynthesis of the antibiotic urdamycin
    • Mittler M., Bechthold A., and Schulz G.E. Structure and action of the C-C bond-forming glycosyltransferase UrdGT2 involved in the biosynthesis of the antibiotic urdamycin. J Mol Biol 372 (2007) 67-76
    • (2007) J Mol Biol , vol.372 , pp. 67-76
    • Mittler, M.1    Bechthold, A.2    Schulz, G.E.3
  • 64
    • 34548685673 scopus 로고    scopus 로고
    • Expanding the promiscuity of a natural-product glycosyltransferase by directed evolution
    • A simple fluorescence based screen employing a surrogate acceptor substrate was used to evolve for the first time a natural product GT. Promiscuity toward donor and acceptor was significantly broadened. This study provides a foundation for the creation of variant GTs with novel activities for use in drug discovery.
    • Williams G.J., Zhang C., and Thorson J.S. Expanding the promiscuity of a natural-product glycosyltransferase by directed evolution. Nat Chem Biol 3 (2007) 657-662. A simple fluorescence based screen employing a surrogate acceptor substrate was used to evolve for the first time a natural product GT. Promiscuity toward donor and acceptor was significantly broadened. This study provides a foundation for the creation of variant GTs with novel activities for use in drug discovery.
    • (2007) Nat Chem Biol , vol.3 , pp. 657-662
    • Williams, G.J.1    Zhang, C.2    Thorson, J.S.3
  • 65
    • 21644437191 scopus 로고    scopus 로고
    • Probing the breadth of macrolide glycosyltransferases: in vitro remodeling of a polyketide antibiotic creates active bacterial uptake and enhances potency
    • Yang M., Proctor M.R., Bolam D.N., Errey J.C., Field R.A., Gilbert H.J., and Davis B.G. Probing the breadth of macrolide glycosyltransferases: in vitro remodeling of a polyketide antibiotic creates active bacterial uptake and enhances potency. J Am Chem Soc 127 (2005) 9336-9337
    • (2005) J Am Chem Soc , vol.127 , pp. 9336-9337
    • Yang, M.1    Proctor, M.R.2    Bolam, D.N.3    Errey, J.C.4    Field, R.A.5    Gilbert, H.J.6    Davis, B.G.7
  • 66
    • 40649092405 scopus 로고    scopus 로고
    • A high-throughput fluorescence-based glycosyltransferase screen and its application in directed evolution
    • Williams G.J., and Thorson J.S. A high-throughput fluorescence-based glycosyltransferase screen and its application in directed evolution. Nat. Protocols 3 (2008) 357-362
    • (2008) Nat. Protocols , vol.3 , pp. 357-362
    • Williams, G.J.1    Thorson, J.S.2
  • 67
    • 41849084518 scopus 로고    scopus 로고
    • Development of novobiocin analogues that manifest anti-proliferative activity against several cancer cell lines
    • Burlison J.A., Avila C., Vielhauer G., Lubbers D.J., Holzbeierlein J., and Blagg B.S. Development of novobiocin analogues that manifest anti-proliferative activity against several cancer cell lines. J Org Chem 73 (2008) 2130-2137
    • (2008) J Org Chem , vol.73 , pp. 2130-2137
    • Burlison, J.A.1    Avila, C.2    Vielhauer, G.3    Lubbers, D.J.4    Holzbeierlein, J.5    Blagg, B.S.6
  • 68
    • 41949101106 scopus 로고    scopus 로고
    • Optimizing glycosyltransferase specificity via "hot spot" saturation mutagenesis presents a catalyst for novobiocin glycorandomization
    • Williams G.J., Goff R.D., Zhang C., and Thorson J.S. Optimizing glycosyltransferase specificity via "hot spot" saturation mutagenesis presents a catalyst for novobiocin glycorandomization. Chem Biol 15 (2008) 393-401
    • (2008) Chem Biol , vol.15 , pp. 393-401
    • Williams, G.J.1    Goff, R.D.2    Zhang, C.3    Thorson, J.S.4
  • 69
    • 0142214752 scopus 로고    scopus 로고
    • Directed evolution of an amine oxidase possessing both broad substrate specificity and high enantioselectivity
    • Carr R., Alexeeva M., Enright A., Eve T.S., Dawson M.J., and Turner N.J. Directed evolution of an amine oxidase possessing both broad substrate specificity and high enantioselectivity. Angew Chem Int Ed Engl 42 (2003) 4807-4810
    • (2003) Angew Chem Int Ed Engl , vol.42 , pp. 4807-4810
    • Carr, R.1    Alexeeva, M.2    Enright, A.3    Eve, T.S.4    Dawson, M.J.5    Turner, N.J.6
  • 70
    • 43849103990 scopus 로고    scopus 로고
    • A high-throughput pH indicator assay for screening glycosyltransferase saturation mutagenesis libraries
    • Persson M., and Palcic M.M. A high-throughput pH indicator assay for screening glycosyltransferase saturation mutagenesis libraries. Anal Biochem 378 (2008) 1-7
    • (2008) Anal Biochem , vol.378 , pp. 1-7
    • Persson, M.1    Palcic, M.M.2
  • 71
    • 33646784006 scopus 로고    scopus 로고
    • Enabling glycosyltransferase evolution: a facile substrate-attachment strategy for phage-display enzyme evolution
    • Love K.R., Swoboda J.G., Noren C.J., and Walker S. Enabling glycosyltransferase evolution: a facile substrate-attachment strategy for phage-display enzyme evolution. Chembiochem 7 (2006) 753-756
    • (2006) Chembiochem , vol.7 , pp. 753-756
    • Love, K.R.1    Swoboda, J.G.2    Noren, C.J.3    Walker, S.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.