PROSITE documentation PDOC00507Glycosyl hydrolases family 17 signature
It has been shown [1,2] that the following glycosyl hydrolases can be classified into a single family on the basis of sequence similarities:
- Glucan endo-1,3-β-D-glucosidases (EC 3.2.1.39) (endo-(1->3)-β- glucanase) from various plants. This enzyme may be involved in the defense of plants against pathogens through its ability to degrade fungal cell wall polysaccharides.
- Glucan 1,3-β-glucosidase (EC 3.2.1.58) (exo-(1->3)-β-glucanase) from yeast (gene BGL2). This enzyme may play a role in cell expansion during growth, in cell-cell fusion during mating, and in spore release during sporulation.
- Lichenases (EC 3.2.1.73) (endo-(1->3,1->4)-β-glucanase) from various plants.
The best conserved region in the sequence of these enzymes is located in their central section. This region contains a conserved tryptophan residue which could be involved in the interaction with the glucan substrates [2] and it also contains a conserved glutamate which has been shown [3] to act as the nucleophile in the catalytic mechanism. We have used this region as a signature pattern.
Expert(s) to contact by email: Last update:December 2004 / Pattern and text revised.
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PROSITE method (with tools and information) covered by this documentation:
1 | 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 |
2 | Authors | Ori N. Sessa G. Lotan T. Himmelhoch S. Fluhr R. |
Title | A major stylar matrix polypeptide (sp41) is a member of the pathogenesis-related proteins superclass. | |
Source | EMBO J. 9:3429-3436(1990). | |
PubMed ID | 2120041 |
3 | Authors | Varghese J.N. Garrett T.P.J. Colman P.M. Chen L. Hoj P.B. Fincher G.B. |
Title | Three-dimensional structures of two plant beta-glucan endohydrolases with distinct substrate specificities. | |
Source | Proc. Natl. Acad. Sci. U.S.A. 91:2785-2789(1994). | |
PubMed ID | 8146192 |
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