PRO-E0062
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More information| Catalogue No. | PRO-E0062 |
|---|---|
| EC | 3.2.1.8 |
| Synonyms | Endo-(1?4)-?-xylan 4-xylanohydrolase; endo1 | 4-xylanase; xylanase; ?-1 | 4-xylanase; endo1 | 4-xylanase; endo-?-1 | 4-xylanase; endo-1 | 4-?D-xylanase; 1 | 4-?-xylan xylanohydrolase; ?-xylanase; ?-1 | 4-xylan xylanohydrolase; endo-1 | 4-?-xylanase; ?-Dxylanase; 4-?-D-xylan xylanohydrolase; endo-(1?4)-beta-xylan 4-xylanohydrolase; beta-1 | 4-xylanase; endo-beta1 | 4-xylanase; endo-1 | 4-beta-D-xylanase; 1 | 4-beta-xylan xylanohydrolase; beta-xylanase; beta-1 | 4-xylan xylanohydrolase; endo-1 | 4-beta-xylanase; beta-D-xylanase; 4-beta-D-xylan xylanohydrolase |
| Nomenclature | CAZy [GH11 | glycoside hydrolase family 11 | member of clan GH-C] | NpXyn11A | XynA | XylA |
| Specific Activity | NOTE: this product has been produced and is awaiting assay. It is thus currently available for purchase by the mg only |
| Accession No. | CAA46498 | P29127 |
| Molecular Weight | 25981.7 Da |
| Biological Function | Catalyses the endohydrolysis of (1?4)-?-D-xylosidic linkages in xylans |
| Comments | This truncated enzyme is the C-terminal catalytic module from the native enzyme (residues 275-499). The native enzyme displays unusually high catalytic activity and is one of the few fungal GH11 proteins not inhibited by the wheat protein XIP-I. A notable feature revealed by X-ray crystallographic analyses is a relatively extended binding cleft for GH11 enzymes comprising potentially 6 subsites running from ?3 and +3. PDB: 2C1F | 2VG9 |
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