title: Purification and substrate specificity of a Ginkgo biloba glycosidase active in β-1,2-xylosidic linkage in plant complex type N-glycans.
abstract: The β-xylosidase, which is active against plant complex type N-glycans, was purified to homogeneity from Ginkgo biloba seeds. The N-terminal amino acid sequence, G-S-A-A-G-N-R-, of the Ginkgo β-xylosidase (β-Xyl'ase Gb) was consistent with the deduced internal amino acid sequence of an Arabidopsis β-xylosidase (AtBXL1). β-Xyl'ase Gb hydrolyzed the β1-2 xylosyl residue from Xylβ1-2Manβ1-4GlcNAcβ1-4GlcNAc-PA and Xylβ1-2Manβ1-4GlcNAcβ1-4(Fucα1-3)GlcNAc-PA, but not that from Manα1-6(Manα1-3)(Xylβ1-2)Manβ1-4GlcNAcβ1-4(Fucα1-3)GlcNAc-PA.
authors.affiliation: Department of Biofunctional Chemistry, Graduate School of Environmental and Life Science, Okayama University.
authors.forename: Megumi
authors.initials: M
authors.lastname: Maeda
authors.forename: Tsuyoshi
authors.initials: T
authors.lastname: Akiyama
authors.forename: Daisuke
authors.initials: D
authors.lastname: Yokouchi
authors.forename: Kwan Kit
authors.initials: KK
authors.lastname: Woo
authors.forename: Yoshinobu
authors.initials: Y
authors.lastname: Kimura
mesh_terms: D000595:Amino Acid Sequence; D002240:Carbohydrate Sequence; D020441:Ginkgo biloba / Q000201:enzymology*; D008969:Molecular Sequence Data; D011134:Polysaccharides / Q000737:chemistry* / Q000378:metabolism*; D011485:Protein Binding; D013379:Substrate Specificity; D014994:Xylose / Q000378:metabolism*; D014995:Xylosidases / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism*
chemical_list: D011134:Polysaccharides; D014994:Xylose; D014995:Xylosidases