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| PROSITE documentation PDOC00646 |
Glucoamylase active site region signature
Description
Glucoamylase (GA) (EC 3.2.1.3) is an enzyme that catalyzes the release of D-glucose from the non-reducing ends of starch and other oligo- or
polysaccharides. Extensive studies of fungal GA have shown [1,E1] that three
closely clustered acidic residues play a role in the catalytic mechanism of
GA. The region that includes these residues is also conserved in a recently
sequenced bacterial GA [2]. We used this region as a signature pattern.
These proteins belong to family 15 in the classification of glycosyl
hydrolases [3,E1].
A GA from Schwanniomyces occidentalis is not a member of this family
but belongs to family 31 (see <PDOC00120>).
July 1998 / Text revised.
Technical section
PROSITE method (with tools and information) covered by this documentation:
| GLUCOAMYLASE, PS00820; Glucoamylase active site region signature (PATTERN) |
| Consensus pattern: |
[STN]-[GP]-x(1,2)-[DE]-x-W-E-E-x(2)-[GS]
All D/E are active site residues |
| Sequences known to belong to this class detected by the pattern: |
ALL |
| Other sequence(s) detected in Swiss-Prot: |
1. |
|
|
|
| Matching PDB structures:
1AGM 1AYX 1DOG 1GAH ... [ALL] |
References
| 1 |
Authors |
Sierks M.R., Ford C., Reilly P.J., Svensson B. |
| Title |
Catalytic mechanism of fungal glucoamylase as defined by mutagenesis of Asp176, Glu179 and Glu180 in the enzyme from Aspergillus awamori. |
| Source |
Protein Eng. 3:193-198(1990). |
| PubMed ID |
1970434 |
| 2 |
Authors |
Ohnishi H., Kitamura H., Minowa T., Sakai H., Ohta T. |
| Title |
Molecular cloning of a glucoamylase gene from a thermophilic Clostridium and kinetics of the cloned enzyme. |
| Source |
Eur. J. Biochem. 207:413-418(1992). |
| PubMed ID |
1633799 |
| 3 |
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 |
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Miscellaneous
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