Molecular characterization of second tomato α1,3/4-fucosidase (α-Fuc’ase Sl-2), a member of glycosyl hydrolase family 29 active toward the core α1,3-fucosyl residue in plant N-glycans-Reference-Cited by-同舟云学术

Molecular characterization of second tomato α1,3/4-fucosidase (α-Fuc’ase Sl-2), a member of glycosyl hydrolase family 29 active toward the core α1,3-fucosyl residue in plant N-glycans

Published:2018-02-10 Issue:1 Volume:164 Page:53-63
ISSN:0021-924X
Container-title:The Journal of Biochemistry
language:en
Short-container-title:

Author:

Rahman Md. Ziaur¹²,Tsujimori Yuta¹,Maeda Megumi¹,Hossain Md. Anowar³,Ishimizu Takeshi⁴,Kimura Yoshinobu¹

Affiliation:

1. Department of Biofunctional Chemistry, Graduate School of Environmental and Life Science, Okayama University, Okayama 700-8530, Japan

2. Institute of Food and Radiation Biology, Atomic Energy Research Establishment, Bangladesh Atomic Energy Commission, Ganakbari, Savar, Dhaka 1340, Bangladesh

3. Department of Biochemistry and Molecular Biology, University of Rajshahi, Rajshahi 6205, Bangladesh

4. College of Life Sciences, Ritsumeikan University, Kusatsu, Shiga 525-8577, Japan

Funder

Ministry of Education, Culture, Sports, Science and Technology of Japan

Basic Research C

Fostering Joint International Research

Research Grants of Mizutani Foundation for Glycoscience

Publisher

Oxford University Press (OUP)

Subject

Molecular Biology,Biochemistry,General Medicine

Link

http://academic.oup.com/jb/article-pdf/164/1/53/25063451/mvy029.pdf

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4. Plant protein glycosylation;Strasser;Glycobiology,2016

5. Structural features of free N-glycans occurring in plants and functional features of de-N-glycosylation enzymes, ENGase and PNGase;Maeda;Y. Front. Plant Sci,2014

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