Alpha-glucosidase
From Proteopedia
(Difference between revisions)
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<scene name='59/596427/Cv/3'>α-D-glucose binding site</scene> (PDB code [[3a4a]]).<ref>PMID:20812985</ref> Water molecules shown as red spheres. | <scene name='59/596427/Cv/3'>α-D-glucose binding site</scene> (PDB code [[3a4a]]).<ref>PMID:20812985</ref> Water molecules shown as red spheres. | ||
<scene name='59/596427/Cv/5'>Ca coordination site</scene>. | <scene name='59/596427/Cv/5'>Ca coordination site</scene>. | ||
| + | |||
| + | ==3D structures of α-glucosidase== | ||
| + | [[Alpha-glucosidase 3D structures]] | ||
</StructureSection> | </StructureSection> | ||
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**[[2g3m]] – SsAGS – ''Sulfolobus solfataricus''<br /> | **[[2g3m]] – SsAGS – ''Sulfolobus solfataricus''<br /> | ||
| - | **[[2ze0]] – | + | **[[2ze0]], [[5zcb]] – GeAGS – ''Geobacillus''<br /> |
**[[3w38]] – bAGS - beet<br /> | **[[3w38]] – bAGS - beet<br /> | ||
**[[2d73]], [[2jka]], [[3wfa]], [[5djw]], [[5f7c]], [[3wfa]], [[3a24]], [[5xfm]] – BtAGS – ''Bacterioides thetaiotaomicron''<br /> | **[[2d73]], [[2jka]], [[3wfa]], [[5djw]], [[5f7c]], [[3wfa]], [[3a24]], [[5xfm]] – BtAGS – ''Bacterioides thetaiotaomicron''<br /> | ||
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**[[3wel]], [[3wem]], [[3wen]], [[3weo]], [[3w37]] – bAGS + substrate<br /> | **[[3wel]], [[3wem]], [[3wen]], [[3weo]], [[3w37]] – bAGS + substrate<br /> | ||
**[[4xqm]] – fyAGS 2 MRH domain + mannose<br /> | **[[4xqm]] – fyAGS 2 MRH domain + mannose<br /> | ||
| + | **[[5zcc]] – GeAGS (mutant) + maltose<br /> | ||
| + | **[[5zcd]] – GeAGS (mutant) + maltotriose<br /> | ||
| + | **[[5zce]] – GeAGS (mutant) + maltotetraose<br /> | ||
| + | |||
| + | *Alpha-glucosidase YIHQ | ||
| + | |||
| + | **[[5ohs]] – RrYIHQ + sulfoquinovoside derivative – ''Rhizobium radiobacter''<br /> | ||
| + | **[[5ohy]] – RrYIHQ + inhibitor<br /> | ||
*Maltase | *Maltase | ||
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**[[5nn5]], [[5nn6]] – hAGS + jiromycin derivative<br /> | **[[5nn5]], [[5nn6]] – hAGS + jiromycin derivative<br /> | ||
| - | *Isomaltase | + | *Maltase-glucoamylase |
| + | |||
| + | **[[2qly]] – hAGS N-terminal catalytic subunit<br /> | ||
| + | **[[2qmj]] – hAGS N-terminal catalytic subunit + acarbose<br /> | ||
| + | **[[3ctt]] – hAGS N-terminal catalytic subunit + casuarine<br /> | ||
| + | |||
| + | *Isomaltase or oligo-1,6-glucosidase | ||
**[[3a47]], [[3aj7]] – yAGS – yeast<br /> | **[[3a47]], [[3aj7]] – yAGS – yeast<br /> | ||
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**[[3pha]], [[3poc]] – RoAGS (mutant) + acarbose<br /> | **[[3pha]], [[3poc]] – RoAGS (mutant) + acarbose<br /> | ||
**[[3mkk]] – RoAGS + isomaltose <br /> | **[[3mkk]] – RoAGS + isomaltose <br /> | ||
| + | **[[4m8u]], [[4maz]], [[4mb1]] – BsAGS 1 (mutant) – ''Bacillus subtilis''<br /> | ||
| + | **[[4m56]] – BsAGS 1 + glucose <br /> | ||
| + | **[[5wcz]] – BsAGS 1 + deoxynojirimycin analog<br /> | ||
| + | **[[1uok]] – AGS – Bacillus cereus<br /> | ||
| + | |||
| + | *Sucrase–isomaltase | ||
| + | |||
| + | **[[3lpo]] – hAGS N-terminal <br /> | ||
| + | **[[3lpp]] – hAGS N-terminal + kotalanol<br /> | ||
*Maltodextrin glucosidase | *Maltodextrin glucosidase | ||
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*6-phospho-α-glucosidase | *6-phospho-α-glucosidase | ||
| - | **[[1u8x]] – | + | **[[1u8x]] – BsPAGS + α-glucose phosphate + NAD <br /> |
| + | **[[6dux]] – KpPAGS + malate + NAD – ''Klebsiella pneumoniae''<br /> | ||
| + | **[[6dvv]] – KpPAGS + Mn + NAD <br /> | ||
| + | |||
| + | *Glucan 1,4-alpha glucosidase or glucoamylase | ||
| + | |||
| + | |||
| + | **[[6frv]] – AnGAGS catalytic domain residues 25-640<br /> | ||
| + | **[[5ghl]] – AnGAGS starch-binding domain residues 533-640<br /> | ||
| + | **[[6fhv]] – GAGS – Penicillium oxalicum<br /> | ||
| + | **[[6fhw]] – GAGS – Amorphotheca resinae<br /> | ||
| - | *Glucan 1,6-α-glucosidase | + | *Glucan 1,6-α-glucosidase or dextran glucosidase |
**[[4aie]] – GAGS – ''Lactobacillus acidophilus''<br /> | **[[4aie]] – GAGS – ''Lactobacillus acidophilus''<br /> | ||
Revision as of 08:19, 6 March 2019
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3D structures of α-glucosidase
Updated on 06-March-2019
References
- ↑ Gloster TM, Turkenburg JP, Potts JR, Henrissat B, Davies GJ. Divergence of catalytic mechanism within a glycosidase family provides insight into evolution of carbohydrate metabolism by human gut flora. Chem Biol. 2008 Oct 20;15(10):1058-67. Epub 2008 Oct 9. PMID:18848471 doi:10.1016/j.chembiol.2008.09.005
- ↑ Yamamoto K, Miyake H, Kusunoki M, Osaki S. Crystal structures of isomaltase from Saccharomyces cerevisiae and in complex with its competitive inhibitor maltose. FEBS J. 2010 Oct;277(20):4205-14. doi: 10.1111/j.1742-4658.2010.07810.x., Epub 2010 Aug 31. PMID:20812985 doi:10.1111/j.1742-4658.2010.07810.x
