AtFXG1, an Arabidopsis Gene Encoding α-L-Fucosidase Active against Fucosylated Xyloglucan Oligosaccharides

An α-L-fucosidase (EC 3.2.1.51) able to release the t-fucosyl residue from the side chain of xyloglucan oligosaccharides has been detected in the leaves of Arabidopsis plants. Moreover, an α-L-fucosidase with similar substrate specificity was purified from cabbage (Brassica oleracea) leaves to rende...

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Bibliographic Details
Published in:Plant physiology (Bethesda) 2002-01, Vol.128 (1), p.247-255
Main Authors: de la Torre, Francisco, Javier Sampedro, Ignacio Zarra, Gloria Revilla
Format: Article
Language:English
Subjects:
2'-fucosyl-lactitol
Acetates
alpha-L-Fucosidase - genetics
alpha-L-Fucosidase - isolation & purification
alpha-L-Fucosidase - metabolism
Amino Acid Sequence
Arabidopsis - enzymology
Arabidopsis - genetics
Arabidopsis thaliana
AtFUC1 gene
AtFXG1 gene
Biological and medical sciences
Brassica - enzymology
Brassica - genetics
Cabbages
Cell Biology and Signal Transduction
Cell walls
Complementary DNA
Enzymes
Fundamental and applied biological sciences. Psychology
Gene Expression Regulation, Enzymologic
Glucans
Glycosides - metabolism
Leaves
Metabolism
Molecular Sequence Data
Oligosaccharides
p-nitrophenyl-^a-L-fucopyranoside
Peas
Pichia pastoris
Plant cells
Plant Leaves - enzymology
Plant Leaves - genetics
Plant physiology and development
Plants
Polysaccharides - metabolism
Sequence Homology, Amino Acid
Sodium
Substrate Specificity
Xylans
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Description
Summary:An α-L-fucosidase (EC 3.2.1.51) able to release the t-fucosyl residue from the side chain of xyloglucan oligosaccharides has been detected in the leaves of Arabidopsis plants. Moreover, an α-L-fucosidase with similar substrate specificity was purified from cabbage (Brassica oleracea) leaves to render a single band on SDS-PAGE. Two peptide sequences were obtained from this protein band, and they were used to identify an Arabidopsis gene coding for an α-fucosidase that we propose to call AtFXG1. In addition, an Arabidopsis gene with homology with known α-L-fucosidases has been also found, and we proposed to name it as AtFUC1. Both AtFXG1 and ATFUC1 were heterologously expressed in Pichia pastoris cells and the α-L-fucosidase activities secreted to the culture medium. The α-L-fucosidase encoded by AtFXG1 was active against the oligosaccharides from xyloglucan XXFG as well as against 2′-fucosyl-lactitol but not against p-nitrophenyl-α-L-fucopyranoside. However, the AtFUC1 heterologously expressed was active only against 2′-fucosyl-lactitol. Thus, the former must be related to xyloglucan metabolism.
ISSN:0032-0889
1532-2548
DOI:10.1104/pp.010508