Alpha-glucosidase: Difference between revisions
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**[[2ze0]] – AGS – ''Geobacillus''<br /> | **[[2ze0]] – AGS – ''Geobacillus''<br /> | ||
**[[3w38]] – bAGS - beet<br /> | **[[3w38]] – bAGS - beet<br /> | ||
**[[2d73]], [[2jka]], [[3wfa]], [[5djw]], [[5f7c]], [[3wfa]] – BtAGS – ''Bacterioides thetaiotaomicron''<br /> | **[[2d73]], [[2jka]], [[3wfa]], [[5djw]], [[5f7c]], [[3wfa]], [[3a24]] – BtAGS – ''Bacterioides thetaiotaomicron''<br /> | ||
**[[5hq4]] – PaAGS - ''Pseudoalteromonas''<br /> | |||
**[[1lf6]] – TtAGS – ''Thermoanaerobobacterium thermosaccharolyticum''<br /> | |||
**[[1kum]], [[1kul]] – AnAGS starch-binding domain – ''Aspergillus niger'' - NMR<br /> | |||
**[[3eqa]] – AnAGS catalytic domain <br /> | |||
**[[1glm]], [[3gly]] – AaAGS – ''Aspergillus awamori''<br /> | |||
**[[1ayx]], [[2fba]] – SfAGS – ''Saccharomycopsis fibuligera''<br /> | |||
**[[5f0e]] – mAGS - mouse<br /> | **[[5f0e]] – mAGS - mouse<br /> | ||
**[[5aed]], [[5aee]], [[5aeg]] – AGS - ''Esherichia coli''<br /> | **[[5aed]], [[5aee]], [[5aeg]] – AGS - ''Esherichia coli''<br /> | ||
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**[[4xpr]] – PsAGS (mutant)<br /> | **[[4xpr]] – PsAGS (mutant)<br /> | ||
*Alpha-glucosidase complex | |||
**[[2jke]] – BtAGS + deoxynojirimycin<br /> | |||
**[[2jkp]] – BtAGS + castasnospermine<br /> | |||
**[[2zq0]] – BtAGS + acarbose<br /> | |||
**[[5hqa]] – PaAGS + acarbose <br /> | |||
**[[5hqb]] – PaAGS (mutant) + panose <br /> | |||
**[[1lf9]] – TtAGS + acarbose<br /> | |||
**[[1gai]], [[1gah]], [[1agm]] – AaAGS + acarbose<br /> | |||
**[[2f6d]] – SfAGS + acarbose<br /> | |||
**[[1dog]] – AaAGS + deoxynojirimycin<br /> | |||
**[[1acz]], [[1ac0]] – AGS starch-binding domain + cyclodextrin - NMR<br /> | |||
**[[5hjr]] – AGS + glucosidase subunit beta - mouse<br /> | |||
**[[5h9o]] – mAGS + glucose<br /> | |||
**[[5hjo]] – mAGS + substrate analog<br /> | |||
**[[5h9r]] – mAGS + intermediate<br /> | |||
**[[5ied]], [[5iee]], [[5ief]], [[5ieg]] – mAGS + iminosugar antiviral<br /> | |||
**[[3wy2]] – HaAGS + glucose<br /> | |||
**[[3wy3]] – HaAGS (mutant) + glucose<br /> | |||
**[[3wy4]] – HaAGS (mutant) + maltose<br /> | |||
**[[4xpp]] – PsAGS + galactose<br /> | |||
**[[4xpq]] – PsAGS + fucose<br /> | |||
**[[4xps]] – PsAGS (mutant) + galactpiranoside<br /> | |||
**[[3wel]], [[3wem]], [[3wen]], [[3weo]], [[3w37]] – bAGS + substrate<br /> | |||
*Maltase complex | *Maltase complex | ||
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**[[1obb]] – TmAGS + NAD + maltose <br /> | **[[1obb]] – TmAGS + NAD + maltose <br /> | ||
**[[2g3n]] – SsAGS + octylglucoside<br /> | **[[2g3n]] – SsAGS + octylglucoside<br /> | ||
**[[3ton]] – hAGS C-terminal - human<br /> | |||
**[[3top]] – hAGS C-terminal + acarbose <br /> | |||
**[[3l4y]], [[3l4z]], [[3l4x]], [[3l4w]], [[3l4v]], [[3l4u]], [[3l4t]] – hAGS N-terminal + inhibitor<br /> | |||
*Isomaltase | *Isomaltase | ||
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**[[3mkk]] – RoAGS + isomaltose <br /> | **[[3mkk]] – RoAGS + isomaltose <br /> | ||
* | *Maltodextrin glucosidase | ||
**[[5bn7]] – EcAGS <br /> | |||
}} | }} | ||
Revision as of 13:30, 1 March 2017
FunctionAlpha glucosidase (AGS) or maltase breaks down the 1,4-α bonds in starch or disaccharides to produce glucose. Maltase breaks down maltose. Isomaltase breaks the 1,6 bond.[1] See also Kennedy research. DiseaseAGS deficiency is the cause of Pompe Disease. AGS inhibitors are used as anti-diabetic drugs and can potentially prevent the fusion of HIV and hepatitis B virus to cells. Structural highlights
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3D structures of α-glucosidase3D structures of α-glucosidase
Updated on 01-March-2017
ReferencesReferences
- ↑ 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