Acetylxylan esterase
acetylxylan esterase | |||||||||
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![]() Acetylxylan esterase oktamer, Geobacillus stearothermophilus | |||||||||
Identifiers | |||||||||
EC no. | 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 | ||||||||
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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 name is acetylxylan esterase.
Structural studies
[edit]As of late 2007, 4 structures have been solved for this class of enzymes, with PDB accession codes 1QOZ, 2C71, 2C79, and 2CC0.
References
[edit]- Sundberg M, Poutanen K (1991). "Purification and properties of two acetylxylan esterases of Trichoderma reesei". Biotechnol. Appl. Biochem. 13: 1–11.
- Poutanen K, Sundberg M, Korte H, Puls J (1990). "Deacetylation of xylans by acetyl esterases of Trichoderma reesei". Appl. Microbiol. Biotechnol. 33 (5): 506–510. doi:10.1007/bf00172542. S2CID 2757027.
- Margolles-Clark E, Tenkanen M, Soderlund H, Penttila M (1996). "Acetyl xylan esterase from Trichoderma reesei contains an active-site serine residue and a cellulose-binding domain". Eur. J. Biochem. 237 (3): 553–60. doi:10.1111/j.1432-1033.1996.0553p.x. PMID 8647098.