1. A Novel Fungal Endo-β-N-acetylglucosaminidase that Specifically Acts on Plant Glycoproteins
- Author
-
Yasunobu Tsuji, Yoshiro Kurimura, and Sakamoto Yoko
- Subjects
Glycan ,Stereochemistry ,Molecular Sequence Data ,Xylose ,Applied Microbiology and Biotechnology ,Biochemistry ,Horseradish peroxidase ,Substrate Specificity ,Analytical Chemistry ,chemistry.chemical_compound ,Hydrolysis ,Enzyme Stability ,Sugar ,Molecular Biology ,Chromatography, High Pressure Liquid ,Horseradish Peroxidase ,Glycoproteins ,Plant Proteins ,chemistry.chemical_classification ,biology ,Organic Chemistry ,Fungi ,General Medicine ,Hydrogen-Ion Concentration ,Bromelains ,Culture Media ,Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase ,Enzyme ,Carbohydrate Sequence ,chemistry ,biology.protein ,Stem bromelain ,Electrophoresis, Polyacrylamide Gel ,Glycoprotein ,Biotechnology - Abstract
An endo-beta-N-acetylglucosaminidase specific for plant glycoprotein oligosaccharides was purified from the culture fluid of a fungus. The Mr of the purified enzyme was 89,000. This enzyme was stable at pH 5.5-7.0, up to 30 degrees C, and showed the highest activity at pH 6.0. Among sugar chains tested, xylose-containing sugar chains (M3X, M3FX, and M2FX) were the most favored substrates. Oligomannose type (M3, M5, and M9) and hybrid type (GNM3) sugar chains were hydrolyzed much more slowly than xylose-containing sugar chains, and a complex type sugar chain (GN2M3) was not hydrolyzed at all by the enzyme. Moreover, the enzyme released sugar chains from native horseradish peroxidase and stem bromelain, which were not hydrolyzed by other endo-beta-N-acetylglucosaminidases (Endo H, D, and F). The enzyme could transfer the xylose-containing sugar chain from bromelain to DNS-Asn-GlcNAc-Fuc.
- Published
- 1998