10 Glycosyltransferases of the GT47 Family

Annual Plant Reviews book series, Volume 41: Plant Polysaccharides
Naomi Geshi

Naomi Geshi

University of Copenhagen, Faculty of Life Sciences, Department of Plant Biology and Biotechnology, Thorvaldsensvej 40, Frederiksberg, 1871 Denmark

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Jesper Harholt

Jesper Harholt

University of Copenhagen, Faculty of Life Sciences, Department of Plant Biology and Biotechnology, Thorvaldsensvej 40, Frederiksberg, 1871 Denmark

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Yumiko Sakuragi

Yumiko Sakuragi

University of Copenhagen, Faculty of Life Sciences, Department of Plant Biology and Biotechnology, Thorvaldsensvej 40, Frederiksberg, 1871 Denmark

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Jacob Krüger Jensen

Jacob Krüger Jensen

University of Copenhagen, Faculty of Life Sciences, Department of Plant Biology and Biotechnology, Thorvaldsensvej 40, Frederiksberg, 1871 Denmark

Michigan State University, MSU-DOE Plant Research Laboratory, Plant Biology Building, East Lansing, MI, 48824 USA

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Henrik Vibe Scheller

Henrik Vibe Scheller

University of Copenhagen, Faculty of Life Sciences, Department of Plant Biology and Biotechnology, Thorvaldsensvej 40, Frederiksberg, 1871 Denmark

Lawrence Berkeley National Laboratory, Joint BioEnergy Institute, 5885 Hollis St, Emeryville, CA, 94608 USA

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First published: 19 April 2018
Citations: 3
This article was originally published in 2011 in Plant Polysaccharides, Volume 41 (ISBN 9781405181723) of the Annual Plant Reviews book series, this volume edited by Peter Ulvskov. The article was republished in Annual Plant Reviews online in April 2018.
Manuscript received December 2009

Abstract

CAZy glycosyltransferase family 47 (GT47) consists of enzymes that are all predicted to be inverting glycosyltransferases. The family includes enzymes with diverse donor and acceptor specificities, making it difficult to predict the function of family members that have not been biochemically characterized. The GT47 family is dominated by plant proteins, many or all of which are likely involved in cell wall biosynthesis and located in the Golgi vesicles. Based on the phylogeny, the plant sequences can be classified into six groups (A–E). Most of them remain to have their biochemical function determined, but a few members are relatively well characterized: MUR3 and XGD1 have been shown biochemically to function as xyloglucan β-1,2-galactosyltransferase and xylogalacturonan β-1,3-xylosyltransferase, respectively. Wall phenotype has been demonstrated in mutants of arad1, gut1/irx10 and fra8/irx7, but biochemical function of the corresponding proteins remains to be elucidated. The mutant phenotypes suggest that ARAD1 functions as a pectin arabinosyltransferase while GUT1/IRX10L and FRA8/IRX7 are involved in xylan biosynthesis.

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