Alpha-glucosidase

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Line 25: Line 25:
**[[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 />
Line 32: Line 38:
**[[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
Line 38: Line 68:
**[[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
Line 49: Line 82:
**[[3mkk]] – RoAGS + isomaltose <br />
**[[3mkk]] – RoAGS + isomaltose <br />
-
*Alpha-glucosidase complex
+
*Maltodextrin glucosidase
 +
 
 +
**[[5bn7]] – EcAGS <br />
 +
 
-
**[[2jke]] – BtAGS + deoxynojirimycin<br />
 
-
**[[2jkp]] – BtAGS + castasnospermine<br />
 
-
**[[2zq0]] – BtAGS + acarbose<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 />
 
}}
}}

Revision as of 10:30, 1 March 2017

Structure of yeast isomaltase complex with α-D-glucose and Ca+2 ion (green) (PDB code 3a4a).

Drag the structure with the mouse to rotate

3D structures of α-glucosidase

Updated on 01-March-2017

References

  1. ↑ 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
  2. ↑ 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

Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky

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