4.4 Article

Heterologous Expression, Purification, and Characterization of an α-Mannosidase Belonging to Glycoside Hydrolase Family 99 of Shewanella amazonensis

Journal

BIOSCIENCE BIOTECHNOLOGY AND BIOCHEMISTRY
Volume 75, Issue 4, Pages 797-799

Publisher

TAYLOR & FRANCIS LTD
DOI: 10.1271/bbb.100874

Keywords

alpha-mannosidase; Shewanella amazonensis; glycoside hydrolase family 99; N-glycosylation; pyridylamino sugar

Funding

  1. Ministry of Education, Culture, Sports, Science, and Technology of Japan [20570103, 19380191]
  2. Grants-in-Aid for Scientific Research [19380191, 20570103] Funding Source: KAKEN

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Shewanella amazonensis a-mannosidase (Sama99), a member of glycoside hydrolase family 99, was expressed in Escherichia coli. The purified Sama99 hydrolyzed pyridylamino (PA)-sugars, Glc(1)Man(9)GlcNAc(2)-PA, and Glc(3)Man(9)GlcNAc(2)-PA, and the product was probably a pyridylamino-decasaccharide in both cases. The mode of action of Sama99 was found to be essentially identical to that of rat endo-alpha-1,2-mannosidase, but the specificity of Sama99 was low.

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