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Laccase
From Proteopedia
(Difference between revisions)
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== Function == | == Function == | ||
| - | '''CotA laccase''' | + | '''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> |
| + | '''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, | ||
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== Structural highlights == | == Structural highlights == | ||
| - | The trinuclear center has two type 3 copper ions, that can be anti-ferromagnetically | + | 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 | ||
Revision as of 09:29, 16 May 2019
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3D structures of CotA laccase
Updated on 16-May-2019
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
- ↑ 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
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