page_title: Alpha-glucosidase
section_title: Structure
hierarchical_section_title: Alpha-glucosidase / Structure
caption_attribution_description: English: From Thermotoga Maritima Beacteria
context_page_description: Alpha-glucosidase is a glucosidase located in the brush border of the small intestine that acts upon α bonds. This is in contrast to beta-glucosidase. Alpha-glucosidase breaks down starch and disaccharides to glucose. Maltase, a similar enzyme that cleaves maltose, is nearly functionally equivalent.
  Other glucosidases include:
  Cellulase
  Beta-glucosidase
  Debranching enzyme
context_section_description: Alpha-glucosidases can be divided, according to primary structure, into two families.
  The gene coding for human lysosomal alpha-glucosidase is about 20 kb long and its structure has been cloned and confirmed.
  Human lysosomal alpha-glucosidase has been studied for the significance of the Asp-518 and other residues in proximity of the enzyme's active site. It was found that substituting Asp-513 with Glu-513 interferes with posttranslational modification and intracellular transport of alpha-glucosidase's precursor. Additionally, the Trp-516 and Asp-518 residues have been deemed critical for the enzyme's  catalytic functionality.
  Kinetic changes in alpha-glucosidase have been shown to be induced by denaturants such as guanidinium chloride (GdmCl) and SDS solutions. These denaturants cause loss of activity and conformational change.  A loss of enzyme activity occurs at much lower concentrations of denaturant than required for conformational changes.  This leads to a conclusion that the enzyme's active site conformation is less stable than the whole enzyme conformation in response to the two denaturants.
caption: Alpha-glucosidase in complex with maltose and NAD+
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