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* [http://bioinform.genetika.ru/members/Naumoff/MB2007E.pdf Structure and evolution of the mammalian maltase-glucoamylase and sucrase-isomaltase] |
* [http://bioinform.genetika.ru/members/Naumoff/MB2007E.pdf Structure and evolution of the mammalian maltase-glucoamylase and sucrase-isomaltase] |
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{{Sugar hydrolases}} |
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{{Esterases}} |
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[[Category:EC 3.2.1]] |
[[Category:EC 3.2.1]] |
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Revision as of 23:39, 23 January 2016
| Alpha-glucosidase | |||||||||
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| Identifiers | |||||||||
| EC no. | 3.2.1.20 | ||||||||
| CAS no. | 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 | ||||||||
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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 [citation needed].
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
- ^ "Maltase - Definition from the Merriam-Webster Online Dictionary". Retrieved 2009-04-06.
- ^ 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. doi:10.1016/0005-2744(70)90253-6. PMID 5466143.
{{cite journal}}: CS1 maint: multiple names: authors list (link) - ^ 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. PMID 29602.
{{cite journal}}: CS1 maint: multiple names: authors list (link) - ^ Larner, J. (1960). "Other glucosidases". In Boyer, P.D., Lardy, H. and Myrbäck, K. (ed.). The Enzymes. Vol. 4 (2nd ed.). New York: Academic Press. pp. 369–378.
{{cite book}}: CS1 maint: multiple names: editors list (link) - ^ 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. PMID 4792946.
{{cite journal}}: CS1 maint: multiple names: authors list (link) - ^ 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. doi:10.1111/j.1432-1033.1982.tb06817.x. PMID 6814909.
{{cite journal}}: CS1 maint: multiple names: authors list (link) - ^ 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.
{{cite journal}}: CS1 maint: multiple names: authors list (link)
External links
- Maltases at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
- Structure and evolution of the mammalian maltase-glucoamylase and sucrase-isomaltase