Alpha-glucosidase: Difference between revisions

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<StructureSection load='3a4a' size='340' side='right' caption='Structure of yeast isomaltase complex with glucose (stick model) and Ca+2 ion (green) (PDB code [[3a4a]]).' scene=''>
<StructureSection load='3a4a' size='340' side='right' caption='Structure of yeast isomaltase complex with α-D-glucose and Ca+2 ion (green) (PDB code [[3a4a]]).' scene='59/596427/Cv/1'>


== Function ==
== Function ==


'''Alpha glucosidase''' (AGS) or '''maltase''' beaks down the 1,4-α bonds in starch or disaccharides to produce glucose.  Maltase breaks down maltose.  '''Isomaltase''' breaks the 1,6 bond.<ref>PMID:18848471</ref>
'''Alpha glucosidase''' (AGS) or '''maltase''' breaks down the 1,4-α bonds in starch or disaccharides to produce glucose.  '''Maltase''' breaks down maltose.  '''Isomaltase''' or '''sucrase-isomaltase''' or '''oligo-1,6-glucosidase''' breaks the 1,6 bond.<ref>PMID:18848471</ref>
*'''Maltase-glucoamylase''' has important role in glucose production.  It hydrolize linear alpha-1,4-linked oligosaccharides<ref>PMID:22058037</ref>.<br />
*'''Acid-alpha gucosidase''' degrades glycogen polymers to glucose in the acidic lysosomes<ref>PMID:17217857</ref>.<br />
*'''6-phospho-alpha gucosidase''' hydrolyses maltose-6"-phosphate<ref>PMID:15341727</ref>.<br />
*'''Glucan 1,4-alpha gucosidase''' hydrolyses the terminal 1,4-linked alpha-D-glucose residues in polysaccharides to produce beta-glucose.<br />
For details see [[Sucrase-isomaltase]].
 
See also [[Kennedy research]] and [[Carbohydrate Metabolism]].


== Disease ==
== Disease ==
Line 9: Line 16:
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.
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.


</StructureSection>
== Structural highlights ==
<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>.


==3D structures of α-glucosidase==
==3D structures of α-glucosidase==
[[Alpha-glucosidase 3D structures]]


Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
</StructureSection>
{{#tree:id=OrganizedByTopic|openlevels=0|
 
*Alpha glucosidase
 
**[[2g3m]] – SsAGS – ''Sulfolobus solfataricus''<br />
**[[2ze0]] – AGS – ''Geobacillus''<br />
**[[3w38]] – bAGS - beet<br />
**[[2d73]], [[2jka]], [[3wfa]] – BtAGS – ''Bacterioides thetaiotaomicron''<br />
 
*Maltase complex
 
**[[1vjt]] – TmAGS + NAD – ''Thermotoga maritima''<br />
**[[1obb]] – TmAGS + NAD + maltose <br />
**[[2g3n]] – SsAGS + octylglucoside<br />
**[[3w37]] – bAGS + acarbose <br />
**[[3wel]], [[3wem]], [[3wen]], [[3weo]] – bAGS + acarviosyl-maltooligosaccharide <br />
 
*Isomaltase
 
**[[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 />
 
*Alpha-glucosidase complex
 
**[[2jke]] – BtAGS + deoxynojirimycin<br />
**[[2jkp]] – BtAGS + castasnospermine<br />
**[[2zq0]] – BtAGS + acarbose<br />
 
}}


== References ==
== References ==

Latest revision as of 11:54, 23 May 2024


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 or sucrase-isomaltase or oligo-1,6-glucosidase breaks the 1,6 bond.[1]

  • Maltase-glucoamylase has important role in glucose production. It hydrolize linear alpha-1,4-linked oligosaccharides[2].
  • Acid-alpha gucosidase degrades glycogen polymers to glucose in the acidic lysosomes[3].
  • 6-phospho-alpha gucosidase hydrolyses maltose-6"-phosphate[4].
  • Glucan 1,4-alpha gucosidase hydrolyses the terminal 1,4-linked alpha-D-glucose residues in polysaccharides to produce beta-glucose.

For details see Sucrase-isomaltase.

See also Kennedy research and Carbohydrate Metabolism.

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).[5] 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. ↑ Ren L, Qin X, Cao X, Wang L, Bai F, Bai G, Shen Y. Structural insight into substrate specificity of human intestinal maltase-glucoamylase. Protein Cell. 2011 Oct;2(10):827-36. Epub 2011 Nov 6. PMID:22058037 doi:10.1007/s13238-011-1105-3
  3. ↑ Fukuda T, Roberts A, Plotz PH, Raben N. Acid alpha-glucosidase deficiency (Pompe disease). Curr Neurol Neurosci Rep. 2007 Jan;7(1):71-7. PMID:17217857 doi:10.1007/s11910-007-0024-4
  4. ↑ Rajan SS, Yang X, Collart F, Yip VL, Withers SG, Varrot A, Thompson J, Davies GJ, Anderson WF. Novel catalytic mechanism of glycoside hydrolysis based on the structure of an NAD+/Mn2+ -dependent phospho-alpha-glucosidase from Bacillus subtilis. Structure. 2004 Sep;12(9):1619-29. PMID:15341727 doi:10.1016/j.str.2004.06.020
  5. ↑ 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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