Acetylxylan esterase

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== Function ==
== Function ==
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'''Acetylxylan esterase''' (AXE) catalyzes the deacetylation of xylans and xylo-oligosaccharides. AXE is involved in the biodegradation of hemicellulose. AXE hydrolyzes the ester linkages of the acetyl groups in position 2 and/or 3 of xylose moiety of naturally acetylated xylan from hardwood. AXE is one of the accessory enzymes which are part of the xylanolytic system. Together with xylanase, β-xylosidase, α-arabinofuranosidase and methylglucoronidase, AXE is required for the complete degradation of xylan.
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'''Acetylxylan esterase''' (AXE) catalyzes the deacetylation of xylans and xylo-oligosaccharides. AXE is involved in the biodegradation of hemicellulose. AXE hydrolyzes the ester linkages of the acetyl groups in position 2 and/or 3 of xylose moiety of naturally acetylated xylan from hardwood. AXE is one of the accessory enzymes which are part of the xylanolytic system. Together with xylanase, β-xylosidase, α-arabinofuranosidase and methylglucoronidase, AXE is required for the complete degradation of xylan.<ref>PMID:8647098</ref>
== Relevance ==
== Relevance ==

Revision as of 13:59, 1 December 2015

Acetylxylan esterase hexamer complex with paraoxon inhibitor, ethylene glycol, acetate and Ca+2 ions, 3m83

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3D structures of acetylxylan esterase

Updated on 01-December-2015

References

  1. Margolles-Clark E, Tenkanen M, Soderlund H, Penttila M. Acetyl xylan esterase from Trichoderma reesei contains an active-site serine residue and a cellulose-binding domain. Eur J Biochem. 1996 May 1;237(3):553-60. PMID:8647098
  2. Levisson M, Han GW, Deller MC, Xu Q, Biely P, Hendriks S, Ten Eyck LF, Flensburg C, Roversi P, Miller MD, McMullan D, von Delft F, Kreusch A, Deacon AM, van der Oost J, Lesley SA, Elsliger MA, Kengen SW, Wilson IA. Functional and structural characterization of a thermostable acetyl esterase from Thermotoga maritima. Proteins. 2012 Jan 27. doi: 10.1002/prot.24041. PMID:22411095 doi:10.1002/prot.24041

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Michal Harel, Alexander Berchansky, Joel L. Sussman

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