Table 1.
Biochemical characteristics of the three endo‐β‐1,3‐glucanases (EGases) from Vitis.
| EGase1 | EGase2 | EGase3 | |
|---|---|---|---|
| Gene | VIT_205s0077g01150 | VIT_206s0061g00120 | VIT_208s0007g06060 |
| Accession no. | Q9M563 | A7PQW3 | F6HLL8 |
| GH family number | GH17 | GH17 | GH17 |
| Clan | GH‐A | GH‐A | GH‐A |
| Three‐dimensional structure status | (β/α)8 | (β/α)8 | (β/α)8 |
| E.C. | 3.2.1.39 | 3.2.1.39 | 3.2.1.39 |
| Residues | 376 | 344 | 345 |
| MW (Da) | 41286.04 | 37092.64 | 37501.89 |
| pI | 9.5 | 4.93 | 9.39 |
| Catalytic Glu | 132; 278 | 123; 268 | 127; 269 |
| Predicted mature protein | 39–278 | 27–268 | 27–269 |
Accession number is from UniprotKB. GH family number, clan, three‐dimensional structure status and E.C. are from the CAZy (carbohydrate‐active enzymes database) site (http://www.cazy.org). Molecular weights (MW) and pI were determined from the enzyme sequences. Catalytic glutamic acid (Glu) residues were predicted using PROSITE.