Alpha-glucosidase: Difference between revisions

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</StructureSection>
</StructureSection>
==3D structures of α-glucosidase==
Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
{{#tree:id=OrganizedByTopic|openlevels=0|
*α glucosidase
**[[2g3m]] – SsAGS – ''Sulfolobus solfataricus''<br />
**[[2ze0]], [[5zcb]] – GeAGS – ''Geobacillus''<br />
**[[3w38]] – bAGS - beet<br />
**[[2d73]], [[2jka]], [[3wfa]], [[5djw]], [[5f7c]], [[3wfa]], [[3a24]], [[5xfm]] – 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 />
**[[5aed]], [[5aee]], [[5aeg]] – AGS - ''Esherichia coli''<br />
**[[3wy1]] – HaAGS - ''Halomonas''<br />
**[[4xpo]] – PsAGS - ''Pedobacter saltans''<br />
**[[4xpr]] – PsAGS (mutant)<br />
**[[2lvx]] – fyAGS 2 MRH domain – fission yeast - NMR<br />
**[[2n1h]] – fyAGS 2 MRH domain (mutant) - NMR<br />
*α-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 />
**[[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
**[[1vjt]] – TmAGS + NAD – ''Thermotoga maritima''<br />
**[[1obb]] – TmAGS + NAD + maltose <br />
**[[2g3n]] – SsAGS + octylglucoside<br />
**[[3ton]], [[5kzw]], [[5kzx]], [[5nn3]], [[5nn4]]  – hAGS C-terminal - human<br />
**[[5nn8]] – hAGS + acarbose <br />
**[[3top]] – hAGS C-terminal + acarbose <br />
**[[3l4y]], [[3l4z]], [[3l4x]], [[3l4w]], [[3l4v]], [[3l4u]], [[3l4t]] – hAGS N-terminal + inhibitor<br />
**[[5nn5]], [[5nn6]] – hAGS + jiromycin derivative<br />
*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 />
**[[3a4a]], [[3axh]] – yAGS + glucose<br />
**[[3axi]] – yAGS (mutant) + glucose<br />
**[[3n04]] – RoAGS – ''Ruminococcus obeum''<br />
**[[3nsx]], [[3nuk]] – RoAGS (mutant)<br />
**[[3pha]], [[3poc]] – RoAGS (mutant) + acarbose<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
**[[5bn7]] – EcAGS <br />
*6-phospho-α-glucosidase
**[[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 or dextran glucosidase
**[[4aie]] – GAGS – ''Lactobacillus acidophilus''<br />
**[[2zic]], [[4xb3]] – SmGAGS (mutant) – ''Streptococcus mutans''<br />
**[[4wlc]] – SmGAGS + glucose <br />
**[[2zid]] – SmGAGS (mutant) + isomaltotriose<br />
}}


== References ==
== References ==

Revision as of 11:21, 6 March 2019


Function

Alpha 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.

Disease

AGS 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

(PDB code 3a4a).[2] Water molecules shown as red spheres.

.

3D structures of α-glucosidase

Alpha-glucosidase 3D structures


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

ReferencesReferences

  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

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Michal Harel, Alexander Berchansky
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