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].
- 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.
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 structure of CotA 1w6l comprises three cupredoxin domains and four copper ions organised in Two copper centers:
a mononuclear blue type 1 copper center and a trinuclear center.[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
- ↑ Claus H. Laccases: structure, reactions, distribution. Micron. 2004;35(1-2):93-6. doi: 10.1016/j.micron.2003.10.029. PMID:15036303 doi:https://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:https://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:https://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:https://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:https://dx.doi.org/10.4061/2011/217861
