Biology:Acetylxylan esterase
From HandWiki
Short description: Class of enzymes
| acetylxylan esterase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 Acetylxylan esterase oktamer, Geobacillus stearothermophilus | |||||||||
| Identifiers | |||||||||
| EC number | 3.1.1.72 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
The enzyme acetylxylan esterase (EC 3.1.1.72) catalyzes the deacetylation of xylans and xylo-oligosaccharides.
This enzyme belongs to the family of hydrolases, specifically those acting on carboxylic ester bonds. The systematic nameis acetylxylan esterase.
Structural studies
As of late 2007, 4 structures have been solved for this class of enzymes, with PDB accession codes 1QOZ, 2C71, 2C79, and 2CC0.
References
- "Purification and properties of two acetylxylan esterases of Trichoderma reesei". Biotechnol. Appl. Biochem. 13: 1–11. 1991.
- "Deacetylation of xylans by acetyl esterases of Trichoderma reesei". Appl. Microbiol. Biotechnol. 33 (5): 506–510. 1990. doi:10.1007/bf00172542.
- "Acetyl xylan esterase from Trichoderma reesei contains an active-site serine residue and a cellulose-binding domain". Eur. J. Biochem. 237 (3): 553–60. 1996. doi:10.1111/j.1432-1033.1996.0553p.x. PMID 8647098.
 |  |
