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

  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},
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
4 Citations
α-L-Fucosidase from Bombyx mori has broad substrate specificity and hydrolyzes core fucosylated N-glycans.
Recombinant BmFucA was cloned and recombinantly expressed as a glutathione-S-transferase tagged protein and exhibited broad substrate specificity and hydrolysis activity for core-fucosylated glycans attached to phospholipase A2 from bee venom. Expand
Plant complex type free N-glycans occur in tomato xylem sap
The occurrence of PCT-FNGs in the xylem sap of the stem of the tomato plant is reported and indicates involvement of acidic peptide:N-glycanase during the degradation of dysfunctional glycoproteins. Expand
Identification and characterization of a novel glycoprotein core xylosidase from the bacterium Elizabethkingia meningoseptica.
IgE-specific reactions were detected in 55% of serum samples collected from 40 allergic patients, and the reactions were significantly attenuated by removal of the core xylose of the allergen by treatment with gpcXase I, a novel tool for basic and clinical glycomics. Expand
Comparative Analyses of Four Chemicals Used to Control Black Mold Disease in Tomato and Its Effects on Defense Signaling Pathways, Productivity and Quality Traits
Pre-harvest chitosan and salicylic acid in vivo application with six sprays could be recommended as effective safe alternatives to fungicides against black mold disease in tomato fruits. Expand


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
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.
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
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
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*
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.
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
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]
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
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