PROSITE documentation PDOC00414
Beta-amylase active sites


β-amylase (EC [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.


These proteins belong to family 14 in the classification of glycosyl hydrolases [5,E1].

Last update:

November 1997 / Text revised.


Technical section

PROSITE methods (with tools and information) covered by this documentation:

BETA_AMYLASE_1, PS00506; Beta-amylase active site 1  (PATTERN)

BETA_AMYLASE_2, PS00679; Beta-amylase active site 2  (PATTERN)


1AuthorsMikami B. Morita Y. Fukazawa C.
TitlePrimary structure and function of beta-amylase.
SourceSeikagaku 60:211-216(1988).
PubMed ID2457058

2AuthorsFriedberg F. Rhodes C.
TitleSegments of amino acid sequence similarity in beta-amylases.
SourceProtein Seq. Data Anal. 1:499-501(1988).
PubMed ID2464171

3AuthorsNitta Y. Isoda Y. Toda H. Sakiyama F.
TitleIdentification of glutamic acid 186 affinity-labeled by 2,3-epoxypropyl alpha-D-glucopyranoside in soybean beta-amylase.
SourceJ. Biochem. 105:573-576(1989).
PubMed ID2474529

4AuthorsTotsuka A. Nong V.H. Kadokawa H. Kim C.-S. Itoh Y. Fukazawa C.
TitleResidues essential for catalytic activity of soybean beta-amylase.
SourceEur. J. Biochem. 221:649-654(1994).
PubMed ID8174545

5AuthorsHenrissat B.
TitleA classification of glycosyl hydrolases based on amino acid sequence similarities.
SourceBiochem. J. 280:309-316(1991).
PubMed ID1747104


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.


View entry in original PROSITE document format
View entry in raw text format (no links)