β-amylase (EC 188.8.131.52) [1,2] is an enzyme that hydrolyzes 1,4-α-glucosidic linkages in starch-type polysaccharide substrates so as to remove
successive maltose units from the non-reducing ends of the chains. β-amylase is present in certain bacteria as well as in plants.
Three highly conserved sequence regions are found in all known β-amylases.
The first of these regions is located in the N-terminal section of the enzymes
and contains an aspartate which is known  to be involved in the catalytic
mechanism. The second, located in a more central location, is centered around
a glutamate which is also involved  in the catalytic mechanism. We use
both regions as signature patterns.
These proteins belong to family 14 in the classification of glycosyl
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