Alpha-glucosidase: 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]] – AGS – ''Geobacillus''<br />
**[[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]] – PAGS + α-glucose phosphate + NAD – ''Bacillus subtilis''<br />
**[[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 (dextran glucosidase)
*Glucan 1,6-α-glucosidase or dextran glucosidase


**[[4aie]] – GAGS – ''Lactobacillus acidophilus''<br />
**[[4aie]] – GAGS – ''Lactobacillus acidophilus''<br />

Revision as of 11:19, 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

3D structures of α-glucosidase3D structures of α-glucosidase

Updated on 06-March-2019

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

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky