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J. Dattagupta, A. Podder, C. Chakrabarti, U. Sen, Debashis Mukhopadhyay, S. Dutta, Manoranjan Singh (1998)
Refined crystal structure (2.3 Å) of a double‐headed winged bean α‐chymotrypsin inhibitor and location of its second reactive siteProteins: Structure, 35
O. Bahl (1970)
Glycosidases of Aspergillus niger II. PURIFICATION AND GENERAL PROPERTIES OF 1,2-α-l-FUCOSIDASEJournal of Biological Chemistry, 245
O. Bahl (2002)
Glycosidases of Aspergillus niger
A. Codina, M. Gairí, T. Tarragó, A. Viguera, M. Feliz, D. Ludevid, E. Giralt (2002)
Letter to the Editor: 1H(N), 15N, 13CO, 13Cα, 13Cβ assignment and secondary structure of a 20 kDa α-l-fucosidase from pea using TROSYJournal of Biomolecular NMR, 22
A. Codina, I. Fernández, E. Giralt, I. Martínez, D. Ludevid (2001)
Combined use of ESI-MS and UV diode-array detection for localization of disulfide bonds in proteins: application to an alpha-L-fucosidase of pea.The journal of peptide research : official journal of the American Peptide Society, 57 6
T. Occhiodoro, K. Beckmann, C. Morris, J. Hopwood (1989)
Human alpha-L-fucosidase: complete coding sequence from cDNA clones.Biochemical and biophysical research communications, 164 1
Sharon Wong-Madden, David Landry (1995)
Purification and characterization of novel glycosidases from the bacterial genus Xanthomonas.Glycobiology, 5 1
C. Prakash, I. Vijay (1983)
A new fluorescent tag for labeling of saccharides.Analytical biochemistry, 128 1
S. Terada, H. Katayama, K. Noda, S. Fujimura, E. Kimoto (1994)
Amino acid sequences of Kunitz family subtilisin inhibitors from seeds of Canavalia lineata.Journal of biochemistry, 115 3
A. Codina, M. Gairi, T. Tarrago, A.R. Viguera, M. Feliz, D. Ludevid, E. Giralt (2002)
1H(N), 15N, 13CO, 13C?, 13C? assignment and secondary structure of a 20 kDa ?-L-fucosidase from pea using TROSYJ. Biomol. NMR, 22
C. Augur, N. Benhamou, A. Darvill, P. Albersheim (1993)
Purification, characterization, and cell wall localization of an alpha-fucosidase that inactivates a xyloglucan oligosaccharin.The Plant journal : for cell and molecular biology, 3 3
F. Torre, J. Sampedro, I. Zarra, G. Revilla (2002)
AtFXG1, an Arabidopsis gene encoding alpha-L-fucosidase active against fucosylated xyloglucan oligosaccharides.Plant physiology, 128 1
D. Blow, J. Janin, R. Sweet (1974)
Mode of action of soybean trypsin inhibitor (Kunitz) as a model for specific protein–protein interactionsNature, 249
S. Clough, A. Bent (1998)
Floral dip: a simplified method for Agrobacterium-mediated transformation of Arabidopsis thaliana.The Plant journal : for cell and molecular biology, 16 6
H. Koiwa, R. Bressan, P. Hasegawa (1997)
Regulation of protease inhibitors and plant defenseTrends in Plant Science, 2
S. Onesti, Peter Brick, David Blow (1991)
Crystal structure of a Kunitz-type trypsin inhibitor from Erythrina caffra seeds.Journal of molecular biology, 217 1
M. Bevan (1984)
Binary Agrobacterium vectors for plant transformation.Nucleic acids research, 12 22
V. Farkaš, R. Hanna, G. Maclachlan (1991)
Xyloglucan oligosaccharide alpha-L-fucosidase activity from growing pea stems and germinating nasturtium seeds.Phytochemistry, 30 10
C. Augur, V. Stiefel, A. Darvill, P. Albersheim, P. Puigdoménech (1995)
Molecular Cloning and Pattern of Expression of an α-L-Fucosidase Gene from Pea Seedlings (*)The Journal of Biological Chemistry, 270
(1977)
AlphaL-fucosidases from almond emulsin: characterization of the two
Vargas-Rechia, Reicher, Rita M, Heyraud, Driguez, Linart (1998)
Xyloglucan octasaccharide XXLGol derived from the seeds of hymenaea courbaril acts as a signaling moleculePlant physiology, 116 3
M. Ogata-Arakawa, T. Muramatsu, A. Kobata (1977)
alpha-L-fucosidases from almond emulsin: characterization of the two enzymes with different specificities.Archives of biochemistry and biophysics, 181 1
An α-L-fucosidase purified from pea (Pisum sativum L. cv Alaska) epicotyl was previously described as a cell wall enzyme of 20 kDa that hydrolyses terminal α-L-fucosidic linkages from oligosaccharide fragments of xyloglucan. cDNA and genomic copies were further isolated and sequenced. The predicted product of the cDNA and the genomic clone (fuc1), was a 20 kDa protein containing a signal peptide and five cysteines. This was the first α-L-fucosidase gene to be cloned in plants but its fucosidase activity has not been demonstrated. Here, our biochemical and immuno analyses suggest that fuc1 does not encode an α-L-fucosidase. Pea fuc1 expressed in Escherichia coli, insect cells and Arabidopsis thaliana produced recombinant proteins without α-L-fucosidase activity. Pea plants had endogenous α-L-fucosidase activity, but the enzyme was not recognised by an antibody produced against recombinant FUC1 protein expressed in E. coli. In contrast, the antibody immunoprecipitated a 20 kDa protein which was inactive. By chromatographic analysis of pea protein extracts, we separated α-L-fucosidase-active fractions from the 20 kDa protein fractions. We conclude that the α-L-fucosidase activity is not attributable to the 20 kDa FUC1 protein. A new function for fuc1 gene product, now named PIP20 (for protease inhibitor from pea) is proposed.
Plant Molecular Biology – Springer Journals
Published: Oct 7, 2004
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