Journal:Acta Cryst D:S205979832100677X
From Proteopedia
(Difference between revisions)
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| - | <StructureSection load='' size='450' side='right' scene='88/886503/Cv/ | + | <StructureSection load='' size='450' side='right' scene='88/886503/Cv/17' caption=''> |
===A GH13 α-glucosidase from ''Weissella cibaria'' uncommonly acts on short-chain maltooligosaccharides=== | ===A GH13 α-glucosidase from ''Weissella cibaria'' uncommonly acts on short-chain maltooligosaccharides=== | ||
<big>Karan Wangpaiboon, Pasunee Laohawuttichai, Sun-Yong Kim, Tomoyuki Mori, Santhana | <big>Karan Wangpaiboon, Pasunee Laohawuttichai, Sun-Yong Kim, Tomoyuki Mori, Santhana | ||
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<hr/> | <hr/> | ||
<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 <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. | + | 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. <scene name='88/886503/Cv/19'>A monomer of WcAG</scene>. Blue represents Domain A, whereas Domain B, C, and N are shown in yellow, red, and green, respectively. Calcium ion is in magenta. |
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| + | ''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 15:08, 1 July 2021
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This page complements a publication in scientific journals and is one of the Proteopedia's Interactive 3D Complement pages. For aditional details please see I3DC.
