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A multigene family of glycosyltransferases in a model plant, Arabidopsis thaliana

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A multigene family of glycosyltransferases in a model plant, Arabidopsis thaliana. / Bowles, D.

In: Biochemical Society transactions, Vol. 30, 04.2002, p. 301-306.

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Bowles, D 2002, 'A multigene family of glycosyltransferases in a model plant, Arabidopsis thaliana', Biochemical Society transactions, vol. 30, pp. 301-306.

APA

Bowles, D. (2002). A multigene family of glycosyltransferases in a model plant, Arabidopsis thaliana. Biochemical Society transactions, 30, 301-306.

Vancouver

Bowles D. A multigene family of glycosyltransferases in a model plant, Arabidopsis thaliana. Biochemical Society transactions. 2002 Apr;30:301-306.

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Bowles, D. / A multigene family of glycosyltransferases in a model plant, Arabidopsis thaliana. In: Biochemical Society transactions. 2002 ; Vol. 30. pp. 301-306.

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@article{b003fc6dfca344e3bd4c726f191b0041,
title = "A multigene family of glycosyltransferases in a model plant, Arabidopsis thaliana",
abstract = "Glycosyltransferases transfer sugars from NDP-sugar donors to acceptors. The multigene family of transferases described in this paper typically, transfer glucose from UDP-glucose to low-molecular-mass acceptors in the cytosol of plant cells. There are 107 sequences in the genome of Arabidopsis thaliana that contain a consensus, suggesting they belong to this Group 1 multigene family. The family has been analysed phylo-genetically, and a functional genomics approach has been applied to explore the relatedness of sequence similarity to catalytic specificity and stereoselectivity. Enzymes belonging to this class of transferases glycosylate a vast array of acceptors, including natural products such as secondary metabolites and hormones, as well as xenobiotics absorbed by the plant, such as herbicides and pesticides. Conjugation to glucose potentially changes the activity of the acceptor molecule and invariably changes its location within the plant cell. Using the genomics approach described, a platform of knowledge has been constructed that will enable an understanding to be gained on the role of these enzymes in cellular homoeostasis, as well as their activity in biotransformations in vitro that require strict regioselectivity of glycosylation.",
keywords = "catalysis, genomics, glycosyltransferase, natural product chemistry, plants, ENZYMIC-SYNTHESIS, RAPHANUS-SATIVUS, UDP-GLUCOSE, GLUCOSYLTRANSFERASE, COTYLEDONS, GENE, INDOL-3-YLACETYL-MYO-INOSITOL, IDENTIFICATION, METABOLISM",
author = "D Bowles",
year = "2002",
month = apr,
language = "English",
volume = "30",
pages = "301--306",
journal = "Biochemical Society transactions",
issn = "0300-5127",
publisher = "Portland Press Ltd.",

}

RIS (suitable for import to EndNote) - Download

TY - JOUR

T1 - A multigene family of glycosyltransferases in a model plant, Arabidopsis thaliana

AU - Bowles, D

PY - 2002/4

Y1 - 2002/4

N2 - Glycosyltransferases transfer sugars from NDP-sugar donors to acceptors. The multigene family of transferases described in this paper typically, transfer glucose from UDP-glucose to low-molecular-mass acceptors in the cytosol of plant cells. There are 107 sequences in the genome of Arabidopsis thaliana that contain a consensus, suggesting they belong to this Group 1 multigene family. The family has been analysed phylo-genetically, and a functional genomics approach has been applied to explore the relatedness of sequence similarity to catalytic specificity and stereoselectivity. Enzymes belonging to this class of transferases glycosylate a vast array of acceptors, including natural products such as secondary metabolites and hormones, as well as xenobiotics absorbed by the plant, such as herbicides and pesticides. Conjugation to glucose potentially changes the activity of the acceptor molecule and invariably changes its location within the plant cell. Using the genomics approach described, a platform of knowledge has been constructed that will enable an understanding to be gained on the role of these enzymes in cellular homoeostasis, as well as their activity in biotransformations in vitro that require strict regioselectivity of glycosylation.

AB - Glycosyltransferases transfer sugars from NDP-sugar donors to acceptors. The multigene family of transferases described in this paper typically, transfer glucose from UDP-glucose to low-molecular-mass acceptors in the cytosol of plant cells. There are 107 sequences in the genome of Arabidopsis thaliana that contain a consensus, suggesting they belong to this Group 1 multigene family. The family has been analysed phylo-genetically, and a functional genomics approach has been applied to explore the relatedness of sequence similarity to catalytic specificity and stereoselectivity. Enzymes belonging to this class of transferases glycosylate a vast array of acceptors, including natural products such as secondary metabolites and hormones, as well as xenobiotics absorbed by the plant, such as herbicides and pesticides. Conjugation to glucose potentially changes the activity of the acceptor molecule and invariably changes its location within the plant cell. Using the genomics approach described, a platform of knowledge has been constructed that will enable an understanding to be gained on the role of these enzymes in cellular homoeostasis, as well as their activity in biotransformations in vitro that require strict regioselectivity of glycosylation.

KW - catalysis

KW - genomics

KW - glycosyltransferase

KW - natural product chemistry

KW - plants

KW - ENZYMIC-SYNTHESIS

KW - RAPHANUS-SATIVUS

KW - UDP-GLUCOSE

KW - GLUCOSYLTRANSFERASE

KW - COTYLEDONS

KW - GENE

KW - INDOL-3-YLACETYL-MYO-INOSITOL

KW - IDENTIFICATION

KW - METABOLISM

M3 - Article

VL - 30

SP - 301

EP - 306

JO - Biochemical Society transactions

JF - Biochemical Society transactions

SN - 0300-5127

ER -