β-amylase (EC 3.2.1.2) [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 [3] to be involved in the catalytic
mechanism. The second, located in a more central location, is centered around
a glutamate which is also involved [4] in the catalytic mechanism. We use
both regions as signature patterns.
Note:
These proteins belong to family 14 in the classification of glycosyl
hydrolases [5,E1].
PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and
distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives
(CC BY-NC-ND 4.0) License, see prosite_license.html.