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| {{STRUCTURE_3m83| PDB=3m83 | SIZE=350| SCENE= |right|CAPTION=Acetylxylan esterase hexamer complex with paraoxon inhibitor, ethylene glycol, acetate and Ca+2 ions, [[3m83]] }}
| | <StructureSection load='3m83' size='350' side='right' scene='' caption='Acetylxylan esterase hexamer complex with paraoxon inhibitor, ethylene glycol, acetate and Ca+2 ions, [[3m83]]'> |
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| == Function == | | == Function == |
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| 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. | | 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. |
| | | </StructureSection> |
| ==3D structures of acetylxylan esterase== | | ==3D structures of acetylxylan esterase== |
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Revision as of 13:17, 1 December 2015
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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.
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.
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3D structures of acetylxylan esterase
Updated on 01-December-2015
{"openlevels":0}
- Acetylxylan esterase
- 1bs9, 2axe – PpAXE – Penicillium purpurogenum
- 1g66 – PpAXE II
- 1qoz – AXE catalytic domain – Trichoderma reesei
- 1vlq, 3m81 – TmAXE – Thermotoga maritima
- 3fvr, 3fvt, 2xlb – BpAXE – Bacillus pumilus
- 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
