PRO-E0051
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More information| Catalogue No. | PRO-E0051 |
|---|---|
| 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 [GH10 | glycoside hydrolase family 10 | member of clan GH-A] | CmXyn10B | Xyn10B (former annotation xylanase 10C (XylC; XYLC; XynC; xynC)) |
| 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. | AF049493 | O68541 |
| Molecular Weight | 42925.9 Da |
| Biological Function | Catalyses the endohydrolysis of (1?4)-?-D-xylosidic linkages in xylans |
| Comments | This enzyme (comprising residues 11-379 of the native sequence) displays the highest catalytic activity towards both glucurono- and arabinoxylans so far observed. A notable feature revealed by X-ray crystallographic analyses is a unique +1 subsite comprising two ?hydrophobic walls? | as opposed to a single hydrophobic patch in other family 10 enzymes. This extensive hydrophobic feature | formed predominantly by Phe-336 and Phe-340 | not only interacts with both the ?- and ?-faces of sugar residues located at the +1 subsite | but also forms a direct interaction (via Phe-340) with 4-O-MeGlcA side chains of substituted xylosyl residues occupying this subsite. The overall binding cleft comprises 6 major subsites running from ?2 and +4. PDB: 1UQY | 1UQZ | 1UR1 | 1UR2 | 2CNC |
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