Acetylxylan esterase: Difference between revisions

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<StructureSection load='' size='350' side='right' scene='48/489290/Cv/5' caption='Acetylxylan esterase hexamer complex with paraoxon inhibitor, ethylene glycol, acetate and Ca+2 ions, [[3m83]]'>
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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.  Xylan is the major constituent of hemicellulose which is the second most abundant polysaccharide in plants.


==3D structures of acetylxylan esterase==
== 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.<ref>PMID:8647098</ref> 
 
== 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 ==
*<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/9'>Ca+2 coordination site</scene>. Water molecules are shown as red spheres.


[[1bs9]], [[2axe]] – PpAXE – ''Penicillium purpurogenum''<br />
==3D structures of acetylxylan esterase==
[[1g66]] – PpAXE II<br />
[[Acetylxylan esterase 3D structures]]
[[1qoz]] – AXE catalytic domain – ''Trichoderma reesei''<br />
[[1vlq]], [[3m81]] – TmAXE – ''Thermotoga maritima''<br />
[[3fvr]], [[3fvt]], [[2xlb]] – BpAXE – ''Bacillus pumilus''


'''Acetylxylan esterase binary complex'''
</StructureSection>


[[2c71]], [[2c79]] – AXE + metal ion – ''Clostridium thermocellum''<br />
== References ==
[[3fyt]] – BpAXE (mutant) + β-D-xylopyranose<br />
<references/>
[[3fyu]] – BpAXE + D-xylose<br />
[[Category:Topic Page]]
[[2xlc]] – BpAXE + diethyl phosphonate<br />
[[3m83]] – TmAXE + paraoxon inhibitor<br />
[[3m82]] – TmAXE + PMSF inhibitor

Latest revision as of 10:11, 25 February 2019

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

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References

Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky, Joel L. Sussman

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