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| *<scene name='48/489290/Cv/6'>Acetylxylan esterase with paraoxon inhibitor, ethylene glycol, acetate and Ca+2 ions</scene>. | | *<scene name='48/489290/Cv/6'>Acetylxylan esterase with paraoxon inhibitor, ethylene glycol, acetate and Ca+2 ions</scene>. |
| *<scene name='48/489290/Cv/8'>Paraoxon inhibitor binding site</scene> ([[3m83]]). <ref>PMID:22411095</ref> | | *<scene name='48/489290/Cv/8'>Paraoxon inhibitor binding site</scene> ([[3m83]]). <ref>PMID:22411095</ref> |
| *<scene name='48/489290/Cv/9'>Ca+2 coordination site</scene>. | | *<scene name='48/489290/Cv/9'>Ca+2 coordination site</scene>. Water molecules are shown as red spheres. |
| </StructureSection> | | </StructureSection> |
| ==3D structures of acetylxylan esterase== | | ==3D structures of acetylxylan esterase== |
Revision as of 13:00, 17 December 2018
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Function
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.[1]
Relevance
Solubility of cellulose is critical for the use of this abundant biomass as biofuel. Xylan is the major constituent of hemicellulose which is the second most abundant polysaccharide in plants. Several enzymes are needed for making cellulose soluble via complete hydrolysis. Among those are cellulase, xylanase and AXE.
Structural Highlights
- ↑ 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
- ↑ 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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3D structures of acetylxylan esterase
Updated on 17-December-2018
{"openlevels":0}
- Acetylxylan esterase
- 3m83, 2axe – PpAXE – Penicillium purpurogenum
- 1g66 – PpAXE II
- 1qoz – AXE catalytic domain – Trichoderma reesei
- 1vlq, 3m81 – TmAXE – Thermotoga maritima
- 3fvr, 3fvt, 2xlb – BpAXE – Bacillus pumilus
- 5bn1, 3w7v, 4jhl - BsAXE - Bacillus stearothermophilus
- 4oao, 4oap, 4jj4, 4jj6, 4jko - BsAXE (mutant)
- 5x6s – AXE – Aspergillus awamori
- Acetylxylan esterase binary complex
- 2c71, 2c79 – AXE + metal ion – Clostridium thermocellum
- 3fyt – BpAXE (mutant) + β-D-xylopyranose
- 3fyu – BpAXE + D-xylose
- 2xlc – BpAXE + diethyl phosphonate
- 3m83 – TmAXE + paraoxon inhibitor
- 3m82 – TmAXE + PMSF inhibitor
References
