Purification and substrate specificity of a ginkgo biloba glycosidase active in β-1,2-xylosidic linkage in plant complex type n-glycans

Megumi Maeda; Tsuyoshi Akiyama; Daisuke Yokouchi; Kwan Kit Woo; Yoshinobu Kimura

doi:10.1271/bbb.130303

Purification and substrate specificity of a ginkgo biloba glycosidase active in β-1,2-xylosidic linkage in plant complex type n-glycans

Megumi Maeda, Tsuyoshi Akiyama, Daisuke Yokouchi, Kwan Kit Woo, Yoshinobu Kimura

Research output: Contribution to journal › Article › peer-review

4 Citations (Scopus)

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(Fucβ1-3)GlcNAc-PA, but not that from Manβ1-6(Manβ1-3)(Xylβ1-2)Manβ1- 4GlcNAcβ1- 4(Fucβ1-3)GlcNAc-PA.

Original language	English
Pages (from-to)	1973-1976
Number of pages	4
Journal	Bioscience, Biotechnology and Biochemistry
Volume	77
Issue number	9
DOIs	https://doi.org/10.1271/bbb.130303
Publication status	Published - 2013

Keywords

Ginkgo biloba
N-glycan turnover
Plant N-glycan
Β-xylosidase activity

ASJC Scopus subject areas

Biotechnology
Analytical Chemistry
Biochemistry
Applied Microbiology and Biotechnology
Molecular Biology
Organic Chemistry

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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(Fucβ1-3)GlcNAc-PA, but not that from Manβ1-6(Manβ1-3)(Xylβ1-2)Manβ1- 4GlcNAcβ1- 4(Fucβ1-3)GlcNAc-PA.",

keywords = "Ginkgo biloba, N-glycan turnover, Plant N-glycan, Β-xylosidase activity",

author = "Megumi Maeda and Tsuyoshi Akiyama and Daisuke Yokouchi and Woo, {Kwan Kit} and Yoshinobu Kimura",

note = "Funding Information: This work was partially supported by grants from the Ministry of Education, Culture, Sports, Science, and Technology of Japan (Basic Research (C), no. 24580494 to M.M. and no. 24580495 to Y.K.), and by grant from Program to Disseminate Tenure Tracking System (FY 2011–2013) from the Ministry of Education, Culture, Sports, Science and Technology of Japan (to M.M.).",

year = "2013",

doi = "10.1271/bbb.130303",

language = "English",

volume = "77",

pages = "1973--1976",

journal = "Bioscience, Biotechnology and Biochemistry",

issn = "0916-8451",

publisher = "Japan Society for Bioscience Biotechnology and Agrochemistry",

number = "9",

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T1 - Purification and substrate specificity of a ginkgo biloba glycosidase active in β-1,2-xylosidic linkage in plant complex type n-glycans

AU - Maeda, Megumi

AU - Akiyama, Tsuyoshi

AU - Yokouchi, Daisuke

AU - Woo, Kwan Kit

AU - Kimura, Yoshinobu

N1 - Funding Information: This work was partially supported by grants from the Ministry of Education, Culture, Sports, Science, and Technology of Japan (Basic Research (C), no. 24580494 to M.M. and no. 24580495 to Y.K.), and by grant from Program to Disseminate Tenure Tracking System (FY 2011–2013) from the Ministry of Education, Culture, Sports, Science and Technology of Japan (to M.M.).

PY - 2013

Y1 - 2013

N2 - 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(Fucβ1-3)GlcNAc-PA, but not that from Manβ1-6(Manβ1-3)(Xylβ1-2)Manβ1- 4GlcNAcβ1- 4(Fucβ1-3)GlcNAc-PA.

AB - 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(Fucβ1-3)GlcNAc-PA, but not that from Manβ1-6(Manβ1-3)(Xylβ1-2)Manβ1- 4GlcNAcβ1- 4(Fucβ1-3)GlcNAc-PA.

KW - Ginkgo biloba

KW - N-glycan turnover

KW - Plant N-glycan

KW - Β-xylosidase activity

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SN - 0916-8451

VL - 77

SP - 1973

EP - 1976

JO - Bioscience, Biotechnology and Biochemistry

JF - Bioscience, Biotechnology and Biochemistry

IS - 9

ER -

Purification and substrate specificity of a ginkgo biloba glycosidase active in β-1,2-xylosidic linkage in plant complex type n-glycans

Abstract

Keywords

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