Functional characterisation of a putative rhamnogalacturonan II specific xylosyltransferase
Functional characterisation of a putative rhamnogalacturonan II specific xylosyltransferase
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DOI:
10.1016/j.febslet.2008.08.015
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发表时间:
2008-09-22
期刊:
影响因子:
3.5
通讯作者:
Petersen, Bent Larsen
中科院分区:
文献类型:
--
作者:
Egelund, Jack;Damager, Iben;Petersen, Bent Larsen
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.