Alpha-glucosidase: Difference between revisions

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'''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>   
'''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>.
*'''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 />


For details see [[Sucrase-isomaltase]].
For details see [[Sucrase-isomaltase]].

Revision as of 11:45, 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].

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).[4] Water molecules shown as red spheres.

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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. 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