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Related Experiment Videos

Insect cells encode a class II alpha-mannosidase with unique properties.

Z Kawar1, K Karaveg, K W Moremen

  • 1Department of Molecular Biology, University of Wyoming, Laramie, Wyoming 82071-3944, USA.

The Journal of Biological Chemistry
|March 30, 2001
PubMed
Summary
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Sf9 alpha-mannosidase III, a novel enzyme, differs from mammalian Golgi alpha-mannosidase II. Its unique properties suggest an alternative N-glycan processing pathway in insect cells.

Area of Science:

  • Biochemistry
  • Glycobiology
  • Enzymology

Background:

  • A previously cloned insect (Sf9) cell cDNA encoded a class II alpha-mannosidase with similarities to mammalian Golgi alpha-mannosidase II.
  • Mammalian class II alpha-mannosidases are known to participate in N-glycan processing.

Purpose of the Study:

  • To evaluate the catalytic properties of the Sf9 class II alpha-mannosidase.
  • To clarify its relationship to mammalian Golgi alpha-mannosidase II.

Main Methods:

  • Enzyme activity assays under varying pH and cofactor conditions.
  • Substrate specificity analysis using specific N-glycan structures.
  • Inhibition studies using swainsonine.

Main Results:

Related Experiment Videos

  • The Sf9 enzyme is cobalt-dependent.
  • It hydrolyzes Man(5)GlcNAc(2) to Man(3)GlcNAc(2) but not GlcNAcMan(5)GlcNAc(2).
  • The enzyme is not active at acidic pH and is localized in the Golgi apparatus, distinguishing it from lysosomal enzymes and other mammalian class II alpha-mannosidases.

    • Conclusions:

    • The Sf9 enzyme is distinct from Golgi alpha-mannosidase II and other known mammalian class II alpha-mannosidases.
    • Its unique properties, including swainsonine sensitivity, define it as Sf9 alpha-mannosidase III.
    • This enzyme likely represents an alternative N-glycan processing pathway in Sf9 cells.