Α-Galactosidase

Enzyme From Wikipedia, the free encyclopedia

Α-Galactosidase

α-Galactosidase ( EC 3.2.1.22, α-GAL, α-GAL A; systematic name α-D-galactoside galactohydrolase) is a glycoside hydrolase enzyme that catalyses the following reaction:[1]

Hydrolysis of terminal, non-reducing α-D-galactose residues in α-D-galactosides, including galactose oligosaccharides, galactomannans and galactolipids

It catalyzes many catabolic processes, including cleavage of glycoproteins, glycolipids, and polysaccharides.

The enzyme is encoded by the GLA gene.[2]

Function

This enzyme is a homodimeric glycoprotein that hydrolyses the terminal α-galactosyl moieties from glycolipids and glycoproteins. It predominantly hydrolyzes ceramide trihexoside, and it can catalyze the hydrolysis of melibiose into galactose and glucose.[citation needed]

Reaction mechanism

Thumb
A double displacement reaction mechanism of α-GAL's catalytic action.The ligand (black) when bound in the active site of the enzyme (blue). The two key amino acid residues in the active site are Asp-170 and Asp-231. First, Asp-170 performs a nucleophilic attack on the glycosidic bond to release the terminal α-galactose molecule from the ligand. Then, Asp-231 serves as an acid to remove a proton from water, making it more nucleophilic to attack the galactose-Asp complex and release α-galactose from the active site.[3][4][5]

Applications

α-Galactosidase from Aspergillus niger is the active ingredient in Beano, a dietary supplement for bloating and flatulence.[6][7]

Recombinant α-galactosidase made by baker's yeast is approved in Europe as a feed additive intended to make poultry food more digestible.[8]

See also

References

Loading related searches...

Wikiwand - on

Seamless Wikipedia browsing. On steroids.