Laccase: Difference between revisions

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== Function ==
== Function ==


'''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>. '''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.
'''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,
* '''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>.   
EC 1.10.3.2), ascorbate oxidase (L-ascorbate oxygen
*'''Two-domain laccase''' or small lactase have unusual resistance to inhibitors<ref>PMID:25778839</ref>.   
oxidoreductase, EC 1.10.3.3) and ceruloplasmin (Fe(II) oxygen
*'''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>:
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>:
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>


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</StructureSection>
</StructureSection>
==3D structures of laccase==
Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
{{#tree:id=OrganizedByTopic|openlevels=0|
*Laccase
**[[1v10]] – Lac + Cu – ''Rigidoporus lignosus''<br />
**[[2h5u]] – Lac + Cu – ''Trametes maxima''<br />
**[[2hzh]] – Lac + Cu – ''Trametes ochracea''<br />
**[[3x1b]] – Lac + Cu – ''Lentinus''<br />
**[[5anh]] – Lac + Cu – ''Basidiomycete''<br />
**[[5ehf]] – Lac + Cu – ''Antrodiella faginea''<br />
**[[4a2d]], [[4a2e]], [[4a2f]], [[4a2g]], [[4a2h]], [[5a7e]] – Lac + Cu – ''Coriolopsis gallica''<br />
**[[4jhu]], [[4jhv]] – Lac + Cu – ''Coriolopsis caperata''<br />
**[[3t6v]], [[3t6w]], [[3t6x]], [[3t6z]], [[3t71]] – Lac + Cu – ''Steccherinum ochraceum''<br />
**[[3sqr]], [[4x4k]] – BaLac + Cu – ''Botrytis aclada''<br />
**[[3v9e]] – BaLac (mutant) + Cu <br />
**[[2xuw]], [[2xvb]] – TtLac – ''Thermus thermophilus''<br />
**[[2yap]], [[5jx9]], [[5k0d]], [[5k15]], [[5k3k]], [[5k5k]], [[5k7a]], [[5k84]] – TtLac + Cu <br />
**[[2xu9]] – TtLac (mutant) + Cu <br />
**[[2yae]], [[5jrr]] – TtLac + Cu + O2  <br />
**[[2yaf]], [[2yah]], [[2yam]], [[2yao]], [[2yaq]], [[2yar]], [[5afa]] – TtLac + Cu + OH  <br />
**[[2xyb]] – Lac + Cu + O2 – ''Pycnoporus cinnabarinus'' <br />
**[[3pps]] – Lac + Cu + O2 – ''Thielavia arenaria'' <br />
**[[3cg8]] – Lac + Cu + O – ''Streptomyces coelicolor'' <br />
**[[3tbb]] – Lac + Cu + O2 – ''Streptomyces viridosporus'' <br />
**[[4f7k]] – Lac – uncultured bacterium<br />
**[[5nq7]], [[5nq8]], [[5nq9]] – Lac + Cu + O2 – ''Trametes sanguinea''<br />
**[[5z1x]], [[5z22]] – Lac + Cu + O2 – ''Cerrena''<br />
*Laccase 1
**[[3qpk]] – MaLac1 + Cu – ''Melanocarpus albomyces''<br />
**[[1gw0]], [[2ih8]], [[2ih9]], [[2q9o]] – MaLac1 + Cu + O <br />
**[[3dkh]] – MaLac1 (mutant) + Cu + O2<br />
**[[3fu7]], [[3fu8]], [[3fu9]] – MaLac1 + Cu + O2 + phenol derivative<br />
**[[1hfu]] – icfLac1 + Cu – inky cap fungus<br />
**[[5ldu]] – wrfLac1 + Cu – white-rot fungus<br />
**[[6f5k]] – Lac1 + Cu + OH – ''Myceliophthora thermophila'' <br />
*Laccase 2
**[[1a65]] – icfLac2 + Cu + O <br />
**[[1gyc]], [[3fpx]], [[3kw7]], [[3pxl]] – wrfLac2 + Cu <br />
**[[3v9c]] – wrfLac2 + Cu + O2<br />
**[[1kya]] – Lac2 + Cu + arylamine – ''Trametes versicolor''<br />
**[[5e9n]], [[6rgh]] – SmLac2 + Cu – ''Steccherinum murashkinskyi''<br />
**[[5mej]], [[5mew]], [[5mhu]], [[5mhv]], [[5mhw]], [[5mhx]], [[5mhy]], [[5mhz]], [[5mi1]], [[5mi2]], [[5mia]], [[5mib]], [[5mic]], [[5mid]], [[5mie]], [[5mig]], [[6rgp]], [[6rhh]], [[6rhi]], [[6rho]], [[6rhp]], [[6rhr]], [[6rhu]], [[6rhx]], [[6ri0]], [[6ri2]], [[6ri4]], [[6ri6]], [[6ri8]], [[6rii]], [[6rik]], [[6ril]] – SmLac2 + Cu + O2<br />
*Two-domain laccase
**[[2zwn]] – Lac + Cu + Cu-O-Cu – metagenomes<br />
**[[5lhl]] – SgLac + Cu + O2 – ''Streptomyces griseoflavus'' <br />
**[[5mkm]], [[5o3k]], [[5o4i]], [[5o4q]], [[6fc7]], [[6fdj]] – SgLac (mutant) + Cu + O2 + O <br />
*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 + ABTS<br />
**[[4a66]], [[4a67]], [[4a68]] - BsSCP (mutant) + Cu + peroxide<br />
*CotS laccase
**[[1nps]] – CotSl N terminal – ''Myxococcus xanthus''
*Laccase
**[[3div]] - Lac - ''Cerrena maxima''<br />
*CueO laccase
}}
See [[Blue copper oxidase CueO]]
== References ==
== References ==
<references/>
<references/>
[[Category:Topic Page]]
[[Category:Topic Page]]

Latest revision as of 15:39, 7 July 2024

Function

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[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).

  • Laccase 2 (Lac2) acts in lignin degradation and in detoxification of lignin products. Typically, laccases show a three cupredoxin-domain folding[2].
  • Two-domain laccase or small lactase have unusual resistance to inhibitors[3].
  • 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 :

a and .[4][5]

For laccase with nitrotyrosine modification see Nitrotyrosine.

Relevance

Laccase from various fungi is used in adsorption of dyes from polluted environment</ref>[6]. Laccases play an important role in food industry, paper and pulp industry, textile industry, synthetic chemistry, cosmetics, soil bioremediation and biodegradation of phenolic pollutants[7].

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 type 2 copper ion.‡ The mononuclear copper is able to accept an electron from a variety of phenolic substrates and then transmit it to the trinuclear centre.

3D structures of laccase

Laccase 3D structures


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

Drag the structure with the mouse to rotate

ReferencesReferences

  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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