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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.
Y Sakamoto, and
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Y Tsuji
January 1990,
Agricultural and biological chemistry,
Y Sakamoto, and
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Y Tsuji
March 1984,
Tanpakushitsu kakusan koso. Protein, nucleic acid, enzyme,
Y Sakamoto, and
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Y Tsuji
February 1985,
Tanpakushitsu kakusan koso. Protein, nucleic acid, enzyme,
Y Sakamoto, and
Y Kurimura, and
Y Tsuji
August 1982,
Proceedings of the National Academy of Sciences of the United States of America,
Y Sakamoto, and
Y Kurimura, and
Y Tsuji
February 1978,
Journal of biochemistry,
Y Sakamoto, and
Y Kurimura, and
Y Tsuji
January 1978,
Methods in enzymology,
Y Sakamoto, and
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Y Tsuji
January 1978,
Methods in enzymology,
Y Sakamoto, and
Y Kurimura, and
Y Tsuji
October 1975,
Comptes rendus hebdomadaires des seances de l'Academie des sciences. Serie D: Sciences naturelles,
Y Sakamoto, and
Y Kurimura, and
Y Tsuji
May 1976,
Biochemical and biophysical research communications,
Y Sakamoto, and
Y Kurimura, and
Y Tsuji
February 1974,
The Journal of biological chemistry,
