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Building Custom Polysaccharides in Vitro with an Efficient, Broad-Specificity Xyloglucan Glycosynthase and a Fucosyltransferase

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Building Custom Polysaccharides in Vitro with an Efficient, Broad-Specificity Xyloglucan Glycosynthase and a Fucosyltransferase. / Spadiut, Oliver; Ibatullin, Farid M.; Peart, Jonelle; Gullfot, Fredrika; Martinez-Fleites, Carlos; Ruda, Marcus; Xu, Chunlin; Sundqvist, Gustav; Davies, Gideon J.; Brumer, Harry.

In: Journal of the American Chemical Society, Vol. 133, No. 28, 20.07.2011, p. 10892-10900.

Research output: Contribution to journalArticle

Harvard

Spadiut, O, Ibatullin, FM, Peart, J, Gullfot, F, Martinez-Fleites, C, Ruda, M, Xu, C, Sundqvist, G, Davies, GJ & Brumer, H 2011, 'Building Custom Polysaccharides in Vitro with an Efficient, Broad-Specificity Xyloglucan Glycosynthase and a Fucosyltransferase', Journal of the American Chemical Society, vol. 133, no. 28, pp. 10892-10900. https://doi.org/10.1021/ja202788q

APA

Spadiut, O., Ibatullin, F. M., Peart, J., Gullfot, F., Martinez-Fleites, C., Ruda, M., ... Brumer, H. (2011). Building Custom Polysaccharides in Vitro with an Efficient, Broad-Specificity Xyloglucan Glycosynthase and a Fucosyltransferase. Journal of the American Chemical Society, 133(28), 10892-10900. https://doi.org/10.1021/ja202788q

Vancouver

Spadiut O, Ibatullin FM, Peart J, Gullfot F, Martinez-Fleites C, Ruda M et al. Building Custom Polysaccharides in Vitro with an Efficient, Broad-Specificity Xyloglucan Glycosynthase and a Fucosyltransferase. Journal of the American Chemical Society. 2011 Jul 20;133(28):10892-10900. https://doi.org/10.1021/ja202788q

Author

Spadiut, Oliver ; Ibatullin, Farid M. ; Peart, Jonelle ; Gullfot, Fredrika ; Martinez-Fleites, Carlos ; Ruda, Marcus ; Xu, Chunlin ; Sundqvist, Gustav ; Davies, Gideon J. ; Brumer, Harry. / Building Custom Polysaccharides in Vitro with an Efficient, Broad-Specificity Xyloglucan Glycosynthase and a Fucosyltransferase. In: Journal of the American Chemical Society. 2011 ; Vol. 133, No. 28. pp. 10892-10900.

Bibtex - Download

@article{2e81d62f832741e49e5faf9b8f3951f6,
title = "Building Custom Polysaccharides in Vitro with an Efficient, Broad-Specificity Xyloglucan Glycosynthase and a Fucosyltransferase",
abstract = "The current drive for applications of biomass-derived compounds, for energy and advanced materials, has led to a resurgence of interest in the manipulation of plant polymers. The xyloglucans, a family of structurally complex plant polysaccharides, have attracted significant interest due to their intrinsic high affinity for cellulose, both in muro and in technical applications. Moreover, current cell wall models are limited by the lack of detailed structure-property relationships of xyloglucans, due to a lack of molecules with well-defined branching patterns. Here, we have developed a new, broad-specificity {"}xyloglucan glycosynthase{"}, selected from active-site mutants of a bacterial endoxyloglucanase, which catalyzed the synthesis of high molar mass polysaccharides, with complex side-chain structures, from suitable glycosyl fluoride donor substrates. The product range was further extended by combination with an Arabidopsis thaliana alpha(1 -> 2)-fucosyltransferase to achieve the in vitro synthesis of fucosylated xyloglucans typical of dicot primary cell walls. These enzymes thus comprise a toolkit for the controlled enzymatic synthesis of xyloglucans that are otherwise impossible to obtain from native sources. Moreover, this study demonstrates the validity of a chemo-enzymatic approach to polysaccharide synthesis, in which the simplicity and economy of glycosynthase technology is harnessed together with the exquisite specificity of glycosyltransferases to control molecular complexity.",
keywords = "ENDO-TRANSGLYCOSYLASE, PLANT, MUTANT, BIOSYNTHESIS, CELLULOSE, CELL-WALL, ARABIDOPSIS, GLYCOSIDASES, CRYSTALLINE, OLIGOSACCHARIDE SYNTHESIS",
author = "Oliver Spadiut and Ibatullin, {Farid M.} and Jonelle Peart and Fredrika Gullfot and Carlos Martinez-Fleites and Marcus Ruda and Chunlin Xu and Gustav Sundqvist and Davies, {Gideon J.} and Harry Brumer",
year = "2011",
month = "7",
day = "20",
doi = "10.1021/ja202788q",
language = "English",
volume = "133",
pages = "10892--10900",
journal = "Journal of the American Chemical Society",
issn = "0002-7863",
publisher = "American Chemical Society",
number = "28",

}

RIS (suitable for import to EndNote) - Download

TY - JOUR

T1 - Building Custom Polysaccharides in Vitro with an Efficient, Broad-Specificity Xyloglucan Glycosynthase and a Fucosyltransferase

AU - Spadiut, Oliver

AU - Ibatullin, Farid M.

AU - Peart, Jonelle

AU - Gullfot, Fredrika

AU - Martinez-Fleites, Carlos

AU - Ruda, Marcus

AU - Xu, Chunlin

AU - Sundqvist, Gustav

AU - Davies, Gideon J.

AU - Brumer, Harry

PY - 2011/7/20

Y1 - 2011/7/20

N2 - The current drive for applications of biomass-derived compounds, for energy and advanced materials, has led to a resurgence of interest in the manipulation of plant polymers. The xyloglucans, a family of structurally complex plant polysaccharides, have attracted significant interest due to their intrinsic high affinity for cellulose, both in muro and in technical applications. Moreover, current cell wall models are limited by the lack of detailed structure-property relationships of xyloglucans, due to a lack of molecules with well-defined branching patterns. Here, we have developed a new, broad-specificity "xyloglucan glycosynthase", selected from active-site mutants of a bacterial endoxyloglucanase, which catalyzed the synthesis of high molar mass polysaccharides, with complex side-chain structures, from suitable glycosyl fluoride donor substrates. The product range was further extended by combination with an Arabidopsis thaliana alpha(1 -> 2)-fucosyltransferase to achieve the in vitro synthesis of fucosylated xyloglucans typical of dicot primary cell walls. These enzymes thus comprise a toolkit for the controlled enzymatic synthesis of xyloglucans that are otherwise impossible to obtain from native sources. Moreover, this study demonstrates the validity of a chemo-enzymatic approach to polysaccharide synthesis, in which the simplicity and economy of glycosynthase technology is harnessed together with the exquisite specificity of glycosyltransferases to control molecular complexity.

AB - The current drive for applications of biomass-derived compounds, for energy and advanced materials, has led to a resurgence of interest in the manipulation of plant polymers. The xyloglucans, a family of structurally complex plant polysaccharides, have attracted significant interest due to their intrinsic high affinity for cellulose, both in muro and in technical applications. Moreover, current cell wall models are limited by the lack of detailed structure-property relationships of xyloglucans, due to a lack of molecules with well-defined branching patterns. Here, we have developed a new, broad-specificity "xyloglucan glycosynthase", selected from active-site mutants of a bacterial endoxyloglucanase, which catalyzed the synthesis of high molar mass polysaccharides, with complex side-chain structures, from suitable glycosyl fluoride donor substrates. The product range was further extended by combination with an Arabidopsis thaliana alpha(1 -> 2)-fucosyltransferase to achieve the in vitro synthesis of fucosylated xyloglucans typical of dicot primary cell walls. These enzymes thus comprise a toolkit for the controlled enzymatic synthesis of xyloglucans that are otherwise impossible to obtain from native sources. Moreover, this study demonstrates the validity of a chemo-enzymatic approach to polysaccharide synthesis, in which the simplicity and economy of glycosynthase technology is harnessed together with the exquisite specificity of glycosyltransferases to control molecular complexity.

KW - ENDO-TRANSGLYCOSYLASE

KW - PLANT

KW - MUTANT

KW - BIOSYNTHESIS

KW - CELLULOSE

KW - CELL-WALL

KW - ARABIDOPSIS

KW - GLYCOSIDASES

KW - CRYSTALLINE

KW - OLIGOSACCHARIDE SYNTHESIS

UR - http://www.scopus.com/inward/record.url?scp=79960267493&partnerID=8YFLogxK

U2 - 10.1021/ja202788q

DO - 10.1021/ja202788q

M3 - Article

VL - 133

SP - 10892

EP - 10900

JO - Journal of the American Chemical Society

JF - Journal of the American Chemical Society

SN - 0002-7863

IS - 28

ER -