Journal:Acta Cryst D:S205979832100677X
From Proteopedia
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<b>Molecular Tour</b><br> | <b>Molecular Tour</b><br> | ||
| - | α-Glucosidase (E.C.3.2.1.20) is a carbohydrate-hydrolyzing enzyme, which generally cleaves α-1,4 glycosidic bonds of oligosaccharides and starch from the non-reducing ends. However, α-glucosidase from ''Weissella cibaria'' BBK-1 (''Wc''AG) exhibited distinct hydrolysis activity against α-1,4 linkages of short chain oligosaccharides from the reducing end. It prefers to hydrolyse maltotriose and acarbose, while it cannot hydrolyse cyclic oligosaccharides and polysaccharides. ''Wc''AG formed a homodimer, of which the N-terminal domain of one monomer orientated in proximity to the catalytic domain of another, creating the substrate-binding groove. The active site of ''Wc''AG was naturally designed to fit perfectly with maltotriose. The Arg-Glu salt bridge gate (R176-E296) in front of the active site modulates the substrate specificity of ''Wc''AG. | + | α-Glucosidase (E.C.3.2.1.20) is a carbohydrate-hydrolyzing enzyme, which generally cleaves α-1,4 glycosidic bonds of oligosaccharides and starch from the non-reducing ends. However, α-glucosidase from ''Weissella cibaria'' BBK-1 (''Wc''AG) exhibited distinct hydrolysis activity against α-1,4 linkages of short chain oligosaccharides from the reducing end. It prefers to hydrolyse <scene name='88/886503/Cv/8'>maltotriose</scene> and <scene name='88/886503/Cv/10'>acarbose</scene>, while it cannot hydrolyse cyclic oligosaccharides and polysaccharides. ''Wc''AG formed a homodimer, of which the N-terminal domain of one monomer orientated in proximity to the catalytic domain of another, creating the substrate-binding groove. The active site of ''Wc''AG was naturally designed to fit perfectly with maltotriose. The Arg-Glu salt bridge gate (R176-E296) in front of the active site modulates the substrate specificity of ''Wc''AG. |
Ligand binding sites: | Ligand binding sites: | ||
Revision as of 12:25, 1 July 2021
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