Structural highlights
Function
GUNH_ACET2 This enzyme catalyzes the endohydrolysis of 1,4-beta-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The substrate binding regions of a beta-1,3:1,4 glucanase are revealed through structural analysis with a thio-oligosaccharide and kinetics of enzyme variants.
Probing the beta-1,3:1,4 glucanase, CtLic26A, with a thio-oligosaccharide and enzyme variants.,Money VA, Cartmell A, Guerreiro CI, Ducros VM, Fontes CM, Gilbert HJ, Davies GJ Org Biomol Chem. 2008 Mar 7;6(5):851-3. Epub 2008 Feb 4. PMID:18292875[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Money VA, Cartmell A, Guerreiro CI, Ducros VM, Fontes CM, Gilbert HJ, Davies GJ. Probing the beta-1,3:1,4 glucanase, CtLic26A, with a thio-oligosaccharide and enzyme variants. Org Biomol Chem. 2008 Mar 7;6(5):851-3. Epub 2008 Feb 4. PMID:18292875 doi:10.1039/b719288f
