Alpha-glucosidase (Saccharomyces cerevisiae) (S. cerevisiae α-glucosidase)

Alpha-glucosidase from Saccharomyces cerevisiae, commonly referred to as maltase, is a hydrolase enzyme responsible for the breakdown of alpha-1,4-glucosidic bonds in complex carbohydrates, releasing alpha-D-glucose (UniProt P07265). It plays a central role in yeast energy metabolism by processing maltose and sucrose into fermentable sugars. In medicinal chemistry and pharmacology, this enzyme is classified within the Glycoside Hydrolase Family 13 and serves as a fundamental in vitro model for screening anti-diabetic compounds (PubMed PMID: 26034187). Although the primary therapeutic targets are human intestinal alpha-glucosidases, the yeast-derived enzyme is a standard surrogate in early-stage drug discovery and natural product research to identify novel inhibitors. By inhibiting alpha-glucosidase activity, the hydrolysis of dietary carbohydrates is delayed, which results in a reduction of postprandial blood glucose spikes in Type 2 diabetes patients. Consequently, it is a vital tool for developing therapeutic strategies for glycemic control, though drugs targeting this mechanism are often associated with gastrointestinal side effects due to the fermentation of undigested carbohydrates in the colon.

Other names

Maltaseα-D-glucoside glucohydrolaseGlucan 1,4-alpha-glucosidaseMAL12MAL32MAL62

Competitive inhibition of the enzyme's catalytic site, which delays the hydrolysis of oligosaccharides into glucose, thereby reducing the rate of glucose absorption and lowering postprandial glycemic levels.