Journal
FEBS LETTERS
Volume 582, Issue 21-22, Pages 3217-3222Publisher
WILEY
DOI: 10.1016/j.febslet.2008.08.015
Keywords
rhamnogalacturonan II; pectin; GT-family-77; xylosyltransferase; Pichia pastoris
Funding
- The Danish National Research Foundation
- The Carlsberg Foundation
- The Ministry of Science, Technology and Innovation
- The Villum Kann Rasmussen Foundation
- European Community FP6 Program
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An Arabidopsis thaliana gene, At1g56550, was expressed in Pichia pastoris and the recombinant protein was shown to catalyse transfer of D-xylose from UDP-alpha-D-xylose onto methyl alpha-L-fucoside. The product formed was shown by 1D and 2D H-1 NMR spectroscopy to be Me alpha-D-Xyl-(1,3)-alpha-L-Fuc, which is identical to the proposed target structure in the A-chain of rhamnogalacturonan II. Chemically synthesized methyl L-fucosides derivatized by methyl groups on either the 2-, 3- or 4 position were tested as acceptor substrates but only methyl 4-O-methyl-alpha-L-fucopyranoside acted as an acceptor, although to a lesser extent than methyl alpha-L-fucoside. At1g56550 is suggested to encode a rhamnogalacturonan II specific xylosyltransferase. (c) 2008 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
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