Enzymes
| UniProtKB help_outline | 1 proteins |
Reaction participants Show >> << Hide
- Name help_outline nigerose Identifier CHEBI:7570 (CAS: 497-48-3) help_outline Charge 0 Formula C12H22O11 InChIKeyhelp_outline QIGJYVCQYDKYDW-NSYYTRPSSA-N SMILEShelp_outline OC[C@H]1O[C@H](O[C@@H]2[C@@H](O)C(O)O[C@H](CO)[C@H]2O)[C@H](O)[C@@H](O)[C@@H]1O 2D coordinates Mol file for the small molecule Search links Involved in 2 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline H2O Identifier CHEBI:15377 (CAS: 7732-18-5) help_outline Charge 0 Formula H2O InChIKeyhelp_outline XLYOFNOQVPJJNP-UHFFFAOYSA-N SMILEShelp_outline [H]O[H] 2D coordinates Mol file for the small molecule Search links Involved in 6,485 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline α-D-glucose Identifier CHEBI:17925 (Beilstein: 1281608,5730158; CAS: 492-62-6) help_outline Charge 0 Formula C6H12O6 InChIKeyhelp_outline WQZGKKKJIJFFOK-DVKNGEFBSA-N SMILEShelp_outline OC[C@H]1O[C@H](O)[C@H](O)[C@@H](O)[C@@H]1O 2D coordinates Mol file for the small molecule Search links Involved in 17 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline D-glucose Identifier CHEBI:4167 (CAS: 2280-44-6) help_outline Charge 0 Formula C6H12O6 InChIKeyhelp_outline WQZGKKKJIJFFOK-GASJEMHNSA-N SMILEShelp_outline OC[C@H]1OC(O)[C@H](O)[C@@H](O)[C@@H]1O 2D coordinates Mol file for the small molecule Search links Involved in 163 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:68800 | RHEA:68801 | RHEA:68802 | RHEA:68803 | |
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| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
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Publications
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Contribution of the Individual Small Intestinal alpha-Glucosidases to Digestion of Unusual alpha-Linked Glycemic Disaccharides.
Lee B.H., Rose D.R., Lin A.H., Quezada-Calvillo R., Nichols B.L., Hamaker B.R.
The mammalian mucosal α-glucosidase complexes, maltase-glucoamylase (MGAM) and sucrase-isomaltase (SI), have two catalytic subunits (N- and C-termini). Concurrent with the desire to modulate glycemic response, there has been a focus on di-/oligosaccharides with unusual α-linkages that are digested ... >> More
The mammalian mucosal α-glucosidase complexes, maltase-glucoamylase (MGAM) and sucrase-isomaltase (SI), have two catalytic subunits (N- and C-termini). Concurrent with the desire to modulate glycemic response, there has been a focus on di-/oligosaccharides with unusual α-linkages that are digested to glucose slowly by these enzymes. Here, we look at disaccharides with various possible α-linkages and their hydrolysis. Hydrolytic properties of the maltose and sucrose isomers were determined using rat intestinal and individual recombinant α-glucosidases. The individual α-glucosidases had moderate to low hydrolytic activities on all α-linked disaccharides, except trehalose. Maltase (N-terminal MGAM) showed a higher ability to digest α-1,2 and α-1,3 disaccharides, as well as α-1,4, making it the most versatile in α-hydrolytic activity. These findings apply to the development of new glycemic oligosaccharides based on unusual α-linkages for extended glycemic response. It also emphasizes that mammalian mucosal α-glucosidases must be used in in vitro assessment of digestion of such carbohydrates. << Less
J. Agric. Food Chem. 64:6487-6494(2016) [PubMed] [EuropePMC]
This publication is cited by 4 other entries.