 |
|
| PROSITE documentation PDOC00414 |
Beta-amylase active sites
Description:
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.
Technical section:
PROSITE methods (with tools and information) covered by this documentation:
| BETA_AMYLASE_1, PS00506; Beta-amylase active site 1 (PATTERN) |
| Consensus pattern: |
H-x-C-G-G-N-V-G-D
D is an active site residue |
| Sequences known to belong to this class detected by the pattern: |
ALL |
| Other sequence(s) detected in Swiss-Prot: |
NONE. |
|
|
|
| Matching PDB structures:
1B1Y 1B90 1B9Z 1BFN ... [ALL] |
| BETA_AMYLASE_2, PS00679; Beta-amylase active site 2 (PATTERN) |
| Consensus pattern: |
G-x-[SA]-G-E-[LIVM]-R-Y-P-S-Y
E is an active site residue |
| Sequences known to belong to this class detected by the pattern: |
ALL |
| Other sequence(s) detected in Swiss-Prot: |
NONE. |
|
|
|
| Matching PDB structures:
1B1Y 1B90 1B9Z 1BFN ... [ALL] |
References:
| 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 |
Copyright:
PROSITE is copyright. It is produced by the Swiss Institute of
Bioinformatics (SIB). There are no restrictions on its use by non-profit
institutions as long as its content is in no way modified. Usage by and
for commercial entities requires a license agreement. For information
about the licensing scheme send an email to license@isb-sib.ch or
see: http://www.expasy.org/prosite/prosite_license.htm.
Miscellaneous:
View entry in original PROSITE document format
View entry in raw text format (no links)