PROSITE documentation PDOC00646Glucoamylase active site region signature
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.
Note:These proteins belong to family 15 in the classification of glycosyl hydrolases [3,E1].
Note:A GA from Schwanniomyces occidentalis is not a member of this family but belongs to family 31 (see <PDOC00120>).
Last update:July 1998 / Text revised.
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PROSITE method (with tools and information) covered by this documentation:
| 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 |
| E1 | Source | http://www.cazy.org/GH15.html |
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