Laccase

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== Function ==
== Function ==
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'''Laccase''' (Lac) is a multi-copper protein which uses molecular oxygen to oxidize various aromatic and non-aromatic compounds by a radical-catalyzed reaction mechanism</ref><ref>PMID:15036303</ref>
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'''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).
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'''CotA laccase''' belongs to the multi-copper oxidase family.
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The multi-copper oxidases constitute a family of enzymes whose
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* '''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>.
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principal members are laccase (benzenediol oxygen oxidoreductase,
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*'''Two-domain laccase''' or small lactase have unusual resistance to inhibitors<ref>PMID:25778839</ref>.
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EC 1.10.3.2), ascorbate oxidase (L-ascorbate oxygen
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*'''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>:
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oxidoreductase, EC 1.10.3.3) and ceruloplasmin (Fe(II) oxygen
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oxidoreductase, EC 1.16.3.1). 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>:
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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>
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]].
For laccase with nitrotyrosine modification see [[Nitrotyrosine]].
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== Relevance ==
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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 ==
== Structural highlights ==
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it to the trinuclear centre.
it to the trinuclear centre.
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==3D structures of laccase==
[[Laccase 3D structures]]
[[Laccase 3D structures]]
</StructureSection>
</StructureSection>
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==3D structures of CotA laccase==
 
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Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
 
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{{#tree:id=OrganizedByTopic|openlevels=0|
 
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*CotA laccase
 
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**[[2x87]], [[2x88]], [[1w6l]], [[1w6w]], [[1w8e]], [[1gsk]] – BsCotAl – ''Bacillus subtilis''<br />
 
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**[[2bhf]] - BsCotAl reduced<br />
 
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**[[2wsd]], [[4ako]], [[4akp]], [[4akq]] – BsCotAl (mutant)<br />
 
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**[[1of0]], [[3zdw]] - BsCotAl + ABTS<br />
 
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**[[4a66]], [[4a67]], [[4a68]] - BsSCP (mutant) + Cu + peroxide<br />
 
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*CotS laccase
 
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**[[1nps]] – CotSl N terminal – ''Myxococcus xanthus''
 
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*Laccase
 
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**[[3div]] - Lac - ''Cerrena maxima''<br />
 
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*CueO laccase
 
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}}
 
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See [[Blue copper oxidase CueO]]
 
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== References ==
== References ==
<references/>
<references/>
[[Category:Topic Page]]
[[Category:Topic Page]]

Current revision

CotA laccase complex with glycerol, O2 and Cu+2 (orange), 1w6l

Drag the structure with the mouse to rotate

References

  1. ↑ Claus H. Laccases: structure, reactions, distribution. Micron. 2004;35(1-2):93-6. doi: 10.1016/j.micron.2003.10.029. PMID:15036303 doi:http://dx.doi.org/10.1016/j.micron.2003.10.029
  2. ↑ Pardo I, Camarero S. Laccase engineering by rational and evolutionary design. Cell Mol Life Sci. 2015 Mar;72(5):897-910. doi: 10.1007/s00018-014-1824-8. Epub, 2015 Jan 14. PMID:25586560 doi:http://dx.doi.org/10.1007/s00018-014-1824-8
  3. ↑ Trubitsina LI, Tishchenko SV, Gabdulkhakov AG, Lisov AV, Zakharova MV, Leontievsky AA. Structural and functional characterization of two-domain laccase from Streptomyces viridochromogenes. Biochimie. 2015 May;112:151-9. doi: 10.1016/j.biochi.2015.03.005. Epub 2015 Mar, 13. PMID:25778839 doi:http://dx.doi.org/10.1016/j.biochi.2015.03.005
  4. ↑ Hullo MF, Moszer I, Danchin A, Martin-Verstraete I. CotA of Bacillus subtilis is a copper-dependent laccase. J Bacteriol. 2001 Sep;183(18):5426-30. PMID:11514528
  5. ↑ Bento I, Martins LO, Gato Lopes G, Armenia Carrondo M, Lindley PF. Dioxygen reduction by multi-copper oxidases; a structural perspective. Dalton Trans. 2005 Nov 7;(21):3507-13. Epub 2005 Sep 27. PMID:16234932 doi:10.1039/b504806k
  6. ↑ Bankole PO, Adekunle AA, Govindwar SP. Demethylation and desulfonation of textile industry dye, Thiazole Yellow G by Aspergillus niger LAG. Biotechnol Rep (Amst). 2019 Mar 28;23:e00327. doi: 10.1016/j.btre.2019.e00327., eCollection 2019 Sep. PMID:30997348 doi:http://dx.doi.org/10.1016/j.btre.2019.e00327
  7. ↑ Shraddha, Shekher R, Sehgal S, Kamthania M, Kumar A. Laccase: microbial sources, production, purification, and potential biotechnological applications. Enzyme Res. 2011;2011:217861. doi: 10.4061/2011/217861. Epub 2011 Jun 21. PMID:21755038 doi:http://dx.doi.org/10.4061/2011/217861
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