Abstract
The α1,2-mannosidase from Saccharomyces cerevisiae, which removes one specific α1,2-linked mannose residue from Man 9GlcNAc 2, is a member of the Class 1 α1,2-mannosidase family conserved from yeast to mammals. Although Class 1 α1,2-mannosidases are essential for the maturation of N-linked oligosaccharides in mammalian cells, nothing is known about their mechanism of action. The availability of sufficient quantities of recombinant yeast α1,2-mannosidase and its homology with the mammalian enzymes make it a good model to study the catalytic mechanism of this family of α1,2-mannosidases. The stereochemical course of hydrolysis of Man 9GlcNAc by the yeast enzyme was followed by proton nuclear magnetic resonance spectroscopy. It was observed that β-D-mannose is released from the oligosaccharide substrate, thereby demonstrating that the enzyme is of the inverting type.
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