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Functional characterisation of a putative rhamnogalacturonan II specific xylosyltransferase
- Source :
-
FEBS Letters . Sep2008, Vol. 582 Issue 21/22, p3217-3222. 6p. - Publication Year :
- 2008
-
Abstract
- Abstract: An Arabidopsis thaliana gene, At1g56550, was expressed in Pichia pastoris and the recombinant protein was shown to catalyse transfer of d-xylose from UDP-α-d-xylose onto methyl α-l-fucoside. The product formed was shown by 1D and 2D 1H NMR spectroscopy to be Me α-d-Xyl-(1,3)-α-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-α-l-fucopyranoside acted as an acceptor, although to a lesser extent than methyl α-l-fucoside. At1g56550 is suggested to encode a rhamnogalacturonan II specific xylosyltransferase. [Copyright &y& Elsevier]
Details
- Language :
- English
- ISSN :
- 00145793
- Volume :
- 582
- Issue :
- 21/22
- Database :
- Academic Search Index
- Journal :
- FEBS Letters
- Publication Type :
- Academic Journal
- Accession number :
- 34298485
- Full Text :
- https://doi.org/10.1016/j.febslet.2008.08.015