Molecular characterization of tomato α1,3/4-fucosidase, a member of glycosyl hydrolase family 29 involved in the degradation of plant complex type N-glycans

Md Ziaur Rahman, Megumi Maeda, Satsuki Itano, Md Anowar Hossain, Takeshi Ishimizu, Yoshinobu Kimura

Research output: Contribution to journalArticle

4 Citations (Scopus)

Abstract

In this study, we identified a gene in tomato that encodes an acidic α-fucosidase (LOC101254568 or Solyc03g006980, α-Fuc'ase S1-1), which may be involved in the turnover of plant complex-type N-glycans. Recombinant α-Fuc'ase S1-1 (rFuc'ase S1-1) was expressed using a baculovirus-insect cell expression system. rFuc'ase Sl-1 is 55 kDa in size and has an optimum pH around 4.5. It substantially hydrolyzed the non-reducing terminal α1,3-fucose residue on LNFP III and α1,4-fucose residues of Lea epitopes on plant complex-type N-glycans, but not the α1,2-fucose residue on LNFP I or the α1,3-fucose residue on pyridylaminated Fucα1-3GlcNAc. Furthermore, we found that this tomato α-Fuc'ase S1-1 was inactive toward the core penta-oligosaccharide unit [Manβ1-4(Xylβ1-2)GlcNAcβ1-4(Fucα1-3)GlcNAc-PA] of plant complex-type N-glycans. Molecular 3D modelling of α-Fuc'ase Sl-1 and structure/sequence interpretation based on comparison with a homologous a-fucosidase from Bifidobacterium longum subsp. infantis (Blon-2336) indicated that residues Asp193 and Glu237 might be important for substrate binding.

Original languageEnglish
Pages (from-to)421-432
Number of pages12
JournalJournal of Biochemistry
Volume161
Issue number5
DOIs
Publication statusPublished - May 1 2017

Keywords

  • A-fucosidase
  • Plant glycoprotein
  • Plant N-glycan
  • Solanum lycopersicum
  • Tomato

ASJC Scopus subject areas

  • Medicine(all)
  • Biochemistry
  • Molecular Biology

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