Rice α-fucosidase active against plant complex type N-glycans containing Lewis a epitope: Purification and characterization

Jiauru Rahman; Makoto Fujishige; Megumi Maeda; Yoshinobu Kimura

doi:10.1080/09168451.2015.1079479

Rice α-fucosidase active against plant complex type N-glycans containing Lewis a epitope: Purification and characterization

Jiauru Rahman, Makoto Fujishige, Megumi Maeda, Yoshinobu Kimura

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

9 Citations (Scopus)

Abstract

Rice α-fucosidase (α-fucosidase Os, 58 kDa) that is active for α1-4 fucosyl linkage in Lewis a unit of plant N-glycans was purified to homogeneity. α-fucosidase Os showed activity against α1-3 fucosyl linkage in Lacto-N-fucopentaose III but not α1-3 fucosyl linkage in the core of plant N-glycans. The N-terminal sequence of α-fucosidase Os was identified as A-A-PT- P-P-P-L-, and this sequence was found in the amino acid sequence of the putative rice α-fucosidase 1 (Os04g0560400).

Original language	English
Pages (from-to)	291-294
Number of pages	4
Journal	Bioscience, Biotechnology and Biochemistry
Volume	80
Issue number	2
DOIs	https://doi.org/10.1080/09168451.2015.1079479
Publication status	Published - 2016

Keywords

N-glycan degradation
Oryza sativa
Plant N-glycan
α-fucosidase

ASJC Scopus subject areas

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

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10.1080/09168451.2015.1079479

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title = "Rice α-fucosidase active against plant complex type N-glycans containing Lewis a epitope: Purification and characterization",

abstract = "Rice α-fucosidase (α-fucosidase Os, 58 kDa) that is active for α1-4 fucosyl linkage in Lewis a unit of plant N-glycans was purified to homogeneity. α-fucosidase Os showed activity against α1-3 fucosyl linkage in Lacto-N-fucopentaose III but not α1-3 fucosyl linkage in the core of plant N-glycans. The N-terminal sequence of α-fucosidase Os was identified as A-A-PT- P-P-P-L-, and this sequence was found in the amino acid sequence of the putative rice α-fucosidase 1 (Os04g0560400).",

keywords = "N-glycan degradation, Oryza sativa, Plant N-glycan, α-fucosidase",

author = "Jiauru Rahman and Makoto Fujishige and Megumi Maeda and Yoshinobu Kimura",

note = "Publisher Copyright: {\textcopyright} 2015 Japan Society for Bioscience, Biotechnology, and Agrochemistry.",

year = "2016",

doi = "10.1080/09168451.2015.1079479",

language = "English",

volume = "80",

pages = "291--294",

journal = "Bioscience, Biotechnology and Biochemistry",

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T1 - Rice α-fucosidase active against plant complex type N-glycans containing Lewis a epitope

T2 - Purification and characterization

AU - Rahman, Jiauru

AU - Fujishige, Makoto

AU - Maeda, Megumi

AU - Kimura, Yoshinobu

PY - 2016

Y1 - 2016

N2 - Rice α-fucosidase (α-fucosidase Os, 58 kDa) that is active for α1-4 fucosyl linkage in Lewis a unit of plant N-glycans was purified to homogeneity. α-fucosidase Os showed activity against α1-3 fucosyl linkage in Lacto-N-fucopentaose III but not α1-3 fucosyl linkage in the core of plant N-glycans. The N-terminal sequence of α-fucosidase Os was identified as A-A-PT- P-P-P-L-, and this sequence was found in the amino acid sequence of the putative rice α-fucosidase 1 (Os04g0560400).

AB - Rice α-fucosidase (α-fucosidase Os, 58 kDa) that is active for α1-4 fucosyl linkage in Lewis a unit of plant N-glycans was purified to homogeneity. α-fucosidase Os showed activity against α1-3 fucosyl linkage in Lacto-N-fucopentaose III but not α1-3 fucosyl linkage in the core of plant N-glycans. The N-terminal sequence of α-fucosidase Os was identified as A-A-PT- P-P-P-L-, and this sequence was found in the amino acid sequence of the putative rice α-fucosidase 1 (Os04g0560400).

KW - N-glycan degradation

KW - Oryza sativa

KW - Plant N-glycan

KW - α-fucosidase

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JO - Bioscience, Biotechnology and Biochemistry

JF - Bioscience, Biotechnology and Biochemistry

IS - 2

ER -

Rice α-fucosidase active against plant complex type N-glycans containing Lewis a epitope: Purification and characterization

Abstract

Keywords

ASJC Scopus subject areas

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