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| == Function == | | == Function == |
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| '''CotA laccase''' belong to the multi-copper oxidase family. | | '''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 == |
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| 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
| 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>[1]
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.[2][3]
For laccase with nitrotyrosine modification see Nitrotyrosine.
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.
- ↑ 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
- ↑ 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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3D structures of CotA laccase
Updated on 16-May-2019
{"openlevels":0}
- CotA laccase
- 1w6l, Nitrotyrosine, 1w6l, 1w6w, 1w8e, 1gsk – BsCotAl – Bacillus subtilis
- 2bhf - BsCotAl reduced
- 2wsd, 4ako, 4akp, 4akq – BsCotAl (mutant)
- 1of0, 3zdw - BsCotAl + ABTS
- 4a66, 4a67, 4a68 - BsSCP (mutant) + Cu + peroxide
- CotS laccase
- 1nps – CotSl N terminal – Myxococcus xanthus
- Laccase
- 3div - Lac - Cerrena maxima
- CueO laccase
See Blue copper oxidase CueO
References
