Acetylxylan esterase
acetylxylan esterase | |||||||||
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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 / EGO | ||||||||
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In enzymology, an acetylxylan esterase (EC 3.1.1.72) is an enzyme that catalyzes a chemical reaction, 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 of this enzyme class is likewise 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
- 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: 506–510. doi:10.1007/bf00172542.
- 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.
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