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Related Experiment Videos

Characterization of a novel mouse recombinant processing alpha-mannosidase

J Schneikert1, A Herscovics

  • 1McGill Cancer Centre, McGill University, Montréal, Québec, Canada.

Glycobiology
|August 1, 1994
PubMed
Summary

Researchers identified a novel mouse alpha-mannosidase, crucial for glycoprotein processing. This enzyme trims specific mannose structures, requiring divalent cations like calcium for optimal activity.

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Area of Science:

  • Biochemistry
  • Glycobiology
  • Molecular Biology

Background:

  • A novel mouse alpha-mannosidase cDNA was previously isolated using homology between yeast and rabbit liver enzymes.
  • The isolated cDNA encodes a type II membrane protein with a cytoplasmic tail and a C-terminal region containing a Ca(2+)-binding sequence.

Purpose of the Study:

  • To characterize the enzymatic properties of the novel mouse alpha-mannosidase.
  • To determine the substrate specificity and cation requirements of the enzyme.

Main Methods:

  • Transient expression of the C-terminal portion of the enzyme in COS cells.
  • Investigation of enzymatic properties using a fusion protein bound to IgG-Sepharose.
  • Assays to determine substrate specificity and cation dependency.

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Main Results:

  • The enzyme functions as an alpha 1,2-mannosidase, trimming Man9GlcNAc to Man5 GlcNAc.
  • Enzymatic activity requires divalent cations, with Ca(2+) being the most effective.
  • The enzyme is inhibited by 1-deoxymannojirimycin but not by swainsonine.

Conclusions:

  • The novel mouse alpha-mannosidase cDNA likely encodes mouse Golgi alpha-mannosidase IB.
  • This enzyme plays a role in the N-linked oligosaccharide processing pathway in the Golgi apparatus.