A novel fungal endo-beta-N-acetylglucosaminidase that specifically acts on plant glycoproteins.
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.
Research Laboratory of Higashimaru Shoyu Co. Ltd., Hyogo, Japan.
Y
Y
Sakamoto
Y
Y
Kurimura
Y
Y
Tsuji
D001963:Bromelains / Q000737:chemistry; D002240:Carbohydrate Sequence; D002851:Chromatography, High Pressure Liquid; D003470:Culture Media / Q000737:chemistry; D004591:Electrophoresis, Polyacrylamide Gel; D004795:Enzyme Stability; D005658:Fungi / Q000737:chemistry*; D006023:Glycoproteins / Q000378:metabolism; D006735:Horseradish Peroxidase / Q000737:chemistry; D006863:Hydrogen-Ion Concentration; D017038:Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase / Q000302:isolation & purification* / Q000378:metabolism; D008969:Molecular Sequence Data; D010940:Plant Proteins / Q000378:metabolism*; D013379:Substrate Specificity; D014994:Xylose
D003470:Culture Media; D006023:Glycoproteins; D010940:Plant Proteins; D001963:Bromelains; D014994:Xylose; D006735:Horseradish Peroxidase; D017038:Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase