PROSITE documentation PDOC00414Beta-amylase active sites
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].
Last update:November 1997 / Text revised.
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PROSITE methods (with tools and information) covered by this documentation:
| 1 | Authors | Mikami B. Morita Y. Fukazawa C. |
| Title | Primary structure and function of beta-amylase. | |
| Source | Seikagaku 60:211-216(1988). | |
| PubMed ID | 2457058 |
| 2 | Authors | Friedberg F. Rhodes C. |
| Title | Segments of amino acid sequence similarity in beta-amylases. | |
| Source | Protein Seq. Data Anal. 1:499-501(1988). | |
| PubMed ID | 2464171 |
| 3 | Authors | Nitta Y. Isoda Y. Toda H. Sakiyama F. |
| Title | Identification of glutamic acid 186 affinity-labeled by 2,3-epoxypropyl alpha-D-glucopyranoside in soybean beta-amylase. | |
| Source | J. Biochem. 105:573-576(1989). | |
| PubMed ID | 2474529 |
| 4 | Authors | Totsuka A. Nong V.H. Kadokawa H. Kim C.-S. Itoh Y. Fukazawa C. |
| Title | Residues essential for catalytic activity of soybean beta-amylase. | |
| Source | Eur. J. Biochem. 221:649-654(1994). | |
| PubMed ID | 8174545 |
| 5 | Authors | Henrissat B. |
| Title | A classification of glycosyl hydrolases based on amino acid sequence similarities. | |
| Source | Biochem. J. 280:309-316(1991). | |
| PubMed ID | 1747104 |
| E1 | Title | https://www.uniprot.org/docs/glycosid |
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