Most members of the glycoside hydrolase family 13 are α-amylases. The maltogenic α-amylase is an enzyme which catalyzes hydrolysis of 1,4-α-D-glucosidic linkages in polysaccharides so as to remove successive α-maltose residues from the non-reducing ends of the chains. The catalytic domain has a structure consisting of an eight-stranded α/β barrel that contains the active site, interrupted by a 70 amino acid calcium-binding domain protruding between β-strand 3 and α-helix 3, and a carboxyl-terminal Greek key β-barrel domain [1].
Allergens from this family were identified in diverse organisms. The group 4 mite and group 11 cockroach allergens are minor allergens binding IgE from about 40% of mite or cockroach allergic patients' sera [2, 3]. Cereal α-amylases are important allergens for patients with baker's asthma [4]. Some of these patients also show IgE reactivity to fungal α-amylases used as baking additives or present in mold contaminated flour [5].
Family-defining Pfam domains (at least one of these domains is present in each family member):
| Pfam domain | Pfam clan | ||
| PF00128 | Alpha amylase, catalytic domain | CL0058 | Tim barrel glycosyl hydrolase superfamily |
| PF02806 | Alpha amylase, C-terminal all-beta domain | CL0369 | Glycosyl hydrolase domain superfamily |
Additional Pfam domains found in some family members:
| Pfam domain | Pfam clan | ||
| PF09260 | Domain of unknown function (DUF1966) | CL0369 | Glycosyl hydrolase domain superfamily |
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