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Laccase
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| - | + | <StructureSection load='1w6l' size='350' side='right' scene='' caption='CotA laccase complex with glycerol, O2 and Cu+2 (orange), [[1w6l]]'> | |
| - | < | + | == Function == |
| - | CotA laccase | + | '''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>. '''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. |
The multi-copper oxidases constitute a family of enzymes whose | The multi-copper oxidases constitute a family of enzymes whose | ||
principal members are laccase (benzenediol oxygen oxidoreductase, | principal members are laccase (benzenediol oxygen oxidoreductase, | ||
EC 1.10.3.2), ascorbate oxidase (L-ascorbate oxygen | EC 1.10.3.2), ascorbate oxidase (L-ascorbate oxygen | ||
oxidoreductase, EC 1.10.3.3) and ceruloplasmin (Fe(II) 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 | + | 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 mononuclear blue type 1 copper | + | 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]]. | |
| - | + | ||
| - | + | ||
| + | == 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>. | ||
| - | The trinuclear | + | == 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 | + | electron from a variety of phenolic substrates and then transmit |
it to the trinuclear centre. | it to the trinuclear centre. | ||
| + | |||
| + | ==3D structures of laccase== | ||
| + | [[Laccase 3D structures]] | ||
| + | |||
| + | </StructureSection> | ||
| + | == References == | ||
| + | <references/> | ||
| + | [[Category:Topic Page]] | ||
Current revision
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References
- ↑ 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
- ↑ 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
- ↑ 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
- ↑ 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
- ↑ 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
- ↑ 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
- ↑ 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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