Isolation of two endo-beta-N-acetylglucosaminidases with different specificities from Pseudomonas sp.
Two endo-beta-N-acetylglucosaminidases (PI and PII) have been isolated from the culture fluid of Pseudomonas sp. The substrate specificity of the PI enzyme was very similar to that of Endo-H from Streptomyces plicatus. On the contrary, the PII enzyme had a novel substrate specificity that degraded both high-mannose type and hybrid type oligosaccharides derived from ovalbumin, and the core structure of complex type oligosaccharides derived from human transferrin and porcine pancreatic lipase.
Takegawa
K
K
Department of Bioresource Science, Faculty of Agriculture, Kagawa University, Japan.
Naitoh
T
T
Iwahara
S
S
D006020:Glycopeptides / Q000378:metabolism; D006596:Hexosaminidases / Q000378:metabolism; D006863:Hydrogen-Ion Concentration; D008049:Lipase / Q000378:metabolism; D008358:Mannose / Q000737:chemistry / Q000378:metabolism; D017038:Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase / Q000302:isolation & purification* / Q000378:metabolism; D008970:Molecular Weight; D009844:Oligosaccharides / Q000378:metabolism*; D011549:Pseudomonas / Q000737:chemistry / Q000201:enzymology* / Q000276:immunology; D013302:Streptomyces / Q000737:chemistry / Q000201:enzymology / Q000276:immunology; D013379:Substrate Specificity; D014168:Transferrin / Q000378:metabolism
D006020:Glycopeptides; D009844:Oligosaccharides; D014168:Transferrin; D008049:Lipase; D006596:Hexosaminidases; D017038:Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase; D008358:Mannose