Laccase: Difference between revisions

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<applet load='1W6L' size='400' frame='true' align=|right| CAPTION='CotA laccase complex with glycerol, O2 and Cu+2 (orange), [[1w6l]]' />
<StructureSection load='1w6l' size='350' side='right' scene='' caption='CotA laccase complex with glycerol, O2 and Cu+2 (orange), [[1w6l]]'>
== Function ==


'''CotA laccase''' belong to the multi-copper oxidase family.
'''Laccase''' (Lac) or '''multicopper oxidase''' is a multi-copper protein which uses molecular oxygen to oxidize various aromatic and non-aromatic compounds by a radical-catalyzed reaction mechanism<ref>PMID:15036303</ref>. The multi-copper oxidases constitute a family of enzymes whose principal members are laccase (benzenediol oxygen oxidoreductase, EC 1.10.3.2), ascorbate oxidase (L-ascorbate oxygen oxidoreductase, EC 1.10.3.3) and ceruloplasmin (Fe(II) oxygen oxidoreductase, EC 1.16.3.1).  
The multi-copper oxidases constitute a family of enzymes whose
principal members are laccase (benzenediol oxygen oxidoreductase,
EC 1.10.3.2), ascorbate oxidase (L-ascorbate oxygen
oxidoreductase, EC 1.10.3.3) and ceruloplasmin (Fe(II) oxygen
oxidoreductase, EC 1.16.3.1). Similar to the other laccases the three dimensional struture of CotA [[1w6l]] comprises three cupredoxin domain and four copper ions organised in <scene name='CotA_laccase/Copper_centers/5'>Two copper centers</scene>:
a <scene name='CotA_laccase/Mononuclear_t1copper/1'>mononuclear blue type 1 copper center</scene> and <scene name='CotA_laccase/Copper_centers/7'>a trinuclear center</scene>


* '''Laccase 2''' (Lac2) acts in lignin degradation and in detoxification of lignin products. Typically, laccases show a three cupredoxin-domain folding<ref>PMID:25586560</ref>. 
*'''Two-domain laccase''' or small lactase have unusual resistance to inhibitors<ref>PMID:25778839</ref>. 
*'''CotA laccase''' belongs to the multi-copper oxidase family.  Similar to the other laccases the three dimensional structure of CotA [[1w6l]] comprises three cupredoxin domains and four copper ions organised in <scene name='CotA_laccase/Copper_centers/5'>Two copper centers</scene>:
a <scene name='40/404916/Cv/3'>mononuclear blue type 1 copper center</scene> and <scene name='40/404916/Cv/2'>a trinuclear center</scene>.<ref>PMID:11514528</ref><ref>PMID:16234932</ref>


For laccase with nitrotyrosine modification see [[Nitrotyrosine]].


The trinuclear center has two type 3 copper ions, that can be anti-ferromagnetically
== Relevance ==
 
Laccase from various fungi is used in adsorption of dyes from polluted environment</ref><ref>PMID:30997348</ref>.  Laccases play an important role in food industry, paper and pulp industry, textile industry, synthetic chemistry, cosmetics, soil bioremediation and biodegradation of phenolic pollutants<ref>PMID:21755038</ref>.
 
== Structural highlights ==
 
The trinuclear center of CotA laccase has two type 3 copper ions, that can be anti-ferromagnetically
coupled through an hydroxyl moiety in between them, and one
coupled through an hydroxyl moiety in between them, and one
type 2 copper ion.‡ The mononuclear copper is able to accept an
type 2 copper ion.‡ The mononuclear copper is able to accept an
electron froma variety of phenolic substrates and then transmits
electron from a variety of phenolic substrates and then transmit
it to the trinuclear centre.
it to the trinuclear centre.


==3D structures of CotA laccase==
==3D structures of laccase==
 
[[Laccase 3D structures]]
Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
{{#tree:id=OrganizedByTopic|openlevels=0|
 
*CotA laccase
 
**[[2x87]], [[2x88]], [[1w6l]], [[1w6w]], [[1w8e]], [[1gsk]] – BsCotAl – ''Bacillus subtilis''<br />
**[[2bhf]] - BsCotAl reduced<br />
**[[2wsd]], [[4ako]], [[4akp]], [[4akq]] – BsCotAl (mutant)<br /> 
**[[1of0]], [[3zdw]] - BsCotAl + EBS<br />
**[[4a66]], [[4a67]], [[4a68]] - BsSCP (mutant) + Cu + peroxide<br />
**[[1uvw]] - BsCotAl + ABTS
 
*CotS laccase
 
**[[1nps]] – CotSl N terminal – ''Myxococcus xanthus''


*CueO laccase
</StructureSection>
}}
== References ==
See [[Blue copper oxidase CueO]]
<references/>
[[Category:Topic Page]]
[[Category:Topic Page]]

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Isabel Bento, David Canner, Jaime Prilusky, Michal Harel, Alexander Berchansky