Mouse acidic mammalian chitinase exhibits transglycosylation activity at somatic tissue pH
Language English Country Great Britain, England Media print-electronic
Document type Letter
- Keywords
- (GlcNAc)2, acidic mammalian chitinase, chitinolytic activity, fluorescence-assisted gel electrophoresis, physiological condition, transglycosylation,
- MeSH
- Acetylglucosamine metabolism MeSH
- Chitin metabolism MeSH
- Chitinases genetics metabolism MeSH
- Dimerization MeSH
- Electrophoresis methods MeSH
- Escherichia coli genetics metabolism MeSH
- Gene Expression MeSH
- Fluorescence MeSH
- Glycosylation MeSH
- Hydrolysis MeSH
- Kinetics MeSH
- Cloning, Molecular MeSH
- Hydrogen-Ion Concentration MeSH
- Mice MeSH
- Lung enzymology MeSH
- Recombinant Proteins genetics metabolism MeSH
- Animals MeSH
- Check Tag
- Mice MeSH
- Animals MeSH
- Publication type
- Letter MeSH
- Names of Substances
- Acetylglucosamine MeSH
- AMCase, mouse MeSH Browser
- Chitin MeSH
- Chitinases MeSH
- Recombinant Proteins MeSH
Mouse acidic mammalian chitinase (AMCase) degrades chitin with highest efficiency at pH 2.0 and is active up to pH 8.0. Here, we report that mouse AMCase also exhibits transglycosylation activity under neutral conditions. We incubated natural and artificial chitin substrates with mouse AMCase at pH 2.0 or 7.0 and analyzed the resulting oligomers using an improved method of fluorescence-assisted carbohydrate electrophoresis. Mouse AMCase produces primarily dimers of N-acetyl-d-glucosamine [(GlcNAc)2 ] under both pH conditions while generating transglycosylated (GlcNAc)3 primarily at pH 7.0 and at lower levels at pH 2.0. These results indicate that mouse AMCase catalyzes hydrolysis as well as transglycosylation and suggest that this enzyme can play a novel role under physiological conditions in peripheral tissues, such as the lungs.
Bioinova Ltd Prague Czech Republic
Department of Applied Chemistry Kogakuin University Hachioji Tokyo Japan
Department of Chemistry and Life Science Kogakuin University Hachioji Tokyo Japan
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