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Maltase

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Title: Maltase  
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Subject: Maltose, Isomaltase, Mannan oligosaccharide-based nutritional supplements, Carbohydrate digestion, HEXB
Collection: Ec 3.2.1
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Maltase

Alpha-glucosidase
Identifiers
EC number 3.2.1.20
CAS number 9001-42-7
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum

Maltase (EC 3.2.1.20, alpha-glucosidase, glucoinvertase, glucosidosucrase, maltase-glucoamylase, alpha-glucopyranosidase, glucosidoinvertase, alpha-D-glucosidase, alpha-glucoside hydrolase, alpha-1,4-glucosidase, alpha-D-glucoside glucohydrolase) is an enzyme located in on the brush border of the small intestine that breaks down the disaccharide maltose.[1][2][3][4][5][6] Maltase catalyzes the hydrolysis of maltose to the simple sugar glucose. This enzyme is found in plants, bacteria, and yeast. Acid maltase deficiency is categorized into three separate types based on the age of onset of symptoms in the affected individual.

In most cases, it is equivalent to alpha-glucosidase, but the term "maltase" emphasizes the disaccharide nature of the substrate from which glucose is cleaved, and "alpha-glucosidase" emphasizes the bond, whether the substrate is a disaccharide or polysaccharide .

In humans, maltase will break down the alpha form of the maltose.

Vampire bats are the only vertebrates that do not exhibit intestinal maltase activity. [7]

See also

References

  1. ^ "Maltase - Definition from the Merriam-Webster Online Dictionary". Retrieved 2009-04-06. 
  2. ^ Bruni, C.B., Sica, V., Auricchio, F. and Covelli, I. (1970). "Further kinetic and structural characterization of the lysosomal α-D-glucoside glucohydrolase from cattle liver". Biochim. Biophys. Acta 212 (3): 470–477.  
  3. ^ Flanagan, P.R. and Forstner, G.G. (1978). "Purification of rat intestinal maltase/glucoamylase and its anomalous dissociation either by heat or by low pH". Biochem. J. 173 (2): 553–563.  
  4. ^ Larner, J. (1960). "Other glucosidases". In Boyer, P.D., Lardy, H. and Myrbäck, K. The Enzymes 4 (2nd ed.). New York: Academic Press. pp. 369–378. 
  5. ^ Sivikami, S. and Radhakrishnan, A.N. (1973). "Purification of rabbit intestinal glucoamylase by affinity chromatography on Sephadex G-200". Indian J. Biochem. Biophys. 10 (4): 283–284.  
  6. ^ Sørensen, S.H., Norén, O., Sjöström, H. and Danielsen, E.M. (1982). "Amphiphilic pig intestinal microvillus maltase/glucoamylase. Structure and specificity". Eur. J. Biochem. 126: 559–568.  
  7. ^ Jorge E. Schondube, L. Gerardo Herrera-M., Carlos Martínez del Rio (2001). "Diet and the evolution of digestion and renal function in phyllostomid bats" (PDF). Zoology 104: 59–73. 

External links

  • Maltases at the US National Library of Medicine Medical Subject Headings (MeSH)
  • Structure and evolution of the mammalian maltase-glucoamylase and sucrase-isomaltase
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