Molecular characterization of second tomato &agr;1,3/4-fucosidase (&agr;-Fuc’ase Sl-2), a member of glycosyl hydrolase family 29 active toward the core &agr;1,3-fucosyl residue in plant N-glycans

@article{Rahman2018MolecularCO,
  title={Molecular characterization of second tomato \&agr;1,3/4-fucosidase (\&agr;-Fuc’ase Sl-2), a member of glycosyl hydrolase family 29 active toward the core \&agr;1,3-fucosyl residue in plant N-glycans},
  author={Md. Ziaur Rahman and Yuta Tsujimori and Megumi Maeda and Md Anowar Hossain and Takeshi Ishimizu and Yoshinobu Kimura},
  journal={The Journal of Biochemistry},
  year={2018},
  volume={164},
  pages={53–63}
}
In a previous study, we molecular-characterized a tomato (Solanum lycopersicum) α1, 3/4-fucosidase (α-Fuc'ase Sl-1) encoded in a tomato gene (Solyc03g006980), indicating that α-Fuc'ase Sl-1 is involved in the turnover of Lea epitope-containing N-glycans. In this study, we have characterized another tomato gene (Solyc11g069010) encoding α1, 3/4-fucosidase (α-Fuc'ase Sl-2), which is also active toward the complex type N-glycans containing Lea epitope(s). The baculovirus-insect cell expression… Expand
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References

SHOWING 1-10 OF 42 REFERENCES
Molecular characterization of tomato &agr;1,3/4-fucosidase, a member of glycosyl hydrolase family 29 involved in the degradation of plant complex type N-glycans
TLDR
It was found that this tomato α-Fuc'ase S1-1 was inactive toward the core penta-oligosaccharide unit of plant complex-type N-glycans, which may be involved in the turnover of plantcomplex- type N- glycans. Expand
Degradation pathway of plant complex-type N-glycans: identification and characterization of a key α1,3-fucosidase from glycoside hydrolase family 29.
TLDR
Results showed that AtFUC1 is an α1,3-fucosidase acting on plant complex-type N-glycans and elucidated the degradation pathway of plantcomplex- type N- glycans. Expand
Purification and characterization of β-xylosidase that is active for plant complex type N-glycans from tomato (Solanum lycopersicum): removal of core α1-3 mannosyl residue is prerequisite for hydrolysis of β1-2 xylosyl residue
TLDR
Results suggest that the release of the β1-2 xylosyl residue by β-Xyl’ase Le-1 occurs at least after the removal the α-1,3-mannosyl residues in the core trimannosyl unit. Expand
Rice α-fucosidase active against plant complex type N-glycans containing Lewis a epitope: purification and characterization
TLDR
Rice α-fucosidase Os showed activity against α1-3 fucosyl linkage in Lacto-N-Fucopentaose III but not α1.1-4 fucose linkage in the core of plant N-glycans. Expand
1,3-1,4-α-l-Fucosynthase That Specifically Introduces Lewis a/x Antigens into Type-1/2 Chains*
TLDR
An α-l-fucosynthase is generated that specifically introduces Lea and Lex antigens into the type-1 and type-2 chains, respectively; i.e. the enzyme specifically accepts the disaccharide structures at the non-reducing ends and attaches a Fuc residue via an α-(1,4/3)-linkage to the GlcNAc. Expand
N-glycans harboring the Lewis a epitope are expressed at the surface of plant cells.
TLDR
It is shown that the antennae are composed of Lewis a (Le(a)) antigens, comprising the carbohydrate sequence Gal beta 1-3[Fuc alpha 1-4]GlcNAc, the first characterization in plants of a Lewis antigen that is usually found on cell-surface glycoconjugates in mammals and involved in recognition and adhesion processes. Expand
Structural features of free N-glycans occurring in plants and functional features of de-N-glycosylation enzymes, ENGase, and PNGase: the presence of unusual plant complex type N-glycans
TLDR
The findings suggest that endo-β-N-acetylglucosaminidase (ENGase) must be involved in the production of GN1 type FNGs, whereas only peptide:N-glycanase (PNGase) is involved in a plant complex type F NGs, and putative functions of FNGS are also discussed. Expand
AXY8 Encodes an α-Fucosidase, Underscoring the Importance of Apoplastic Metabolism on the Fine Structure of Arabidopsis Cell Wall Polysaccharides[W][OA]
TLDR
The genetic evidence indicates that the activity of glycosylhydrolases in the apoplast plays a major role in generating the heterogeneity of XyG side chains in the wall. Expand
Purification, characterization, and cell wall localization of an alpha-fucosidase that inactivates a xyloglucan oligosaccharin.
An alpha-fucosidase that releases fucosyl residues from oligosaccharide fragments of xyloglucan, a plant cell wall hemicellulosic polysaccharide, was purified to homogeneity from pea (Pisum sativum)Expand
Occurrence of complex type free N-glycans with a single GlcNAc residue at the reducing termini in the fresh-water plant, Egeria densa
TLDR
Results suggest that a mechanism responsible for the production of PCT-GN1-FNG is present in native plant tissues, which are found in fresh-water plant Egeria densa. Expand
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