Journal:Acta Cryst D:S205979832100677X

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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. WcAG 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 maltotriose and acarbose, while it cannot hydrolyse cyclic oligosaccharides and polysaccharides. WcAG 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.
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Ligands:
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Ligand binding sites:
*<scene name='88/886503/Cv/4'>Glycerols</scene> PDB ID: [[7d9b]].
*<scene name='88/886503/Cv/4'>Glycerols</scene> PDB ID: [[7d9b]].
*<scene name='88/886503/Cv/6'>Maltose</scene> PDB ID: [[7d9c]].
*<scene name='88/886503/Cv/6'>Maltose</scene> PDB ID: [[7d9c]].

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