Maltase
| Alpha-glucosidase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 3.2.1.20 | ||||||||
| CAS number | Template:CAS | ||||||||
| 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[citation needed].
Vampire bats are the only vertebrates that do not exhibit intestinal maltase activity. [7]
See also
References
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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
