Laccase
From Proteopedia
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<applet load='1W6L' size='400' frame='true' align=|right| CAPTION='CotA laccase complex with glycerol, O2 and Cu+2 (orange), [[1w6l]]' /> | <applet load='1W6L' size='400' frame='true' align=|right| CAPTION='CotA laccase complex with glycerol, O2 and Cu+2 (orange), [[1w6l]]' /> | ||
+ | == Function == | ||
'''CotA laccase''' belong to the multi-copper oxidase family. | '''CotA laccase''' belong to the multi-copper oxidase family. | ||
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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 <scene name='CotA_laccase/Mononuclear_t1copper/1'>mononuclear blue type 1 copper center</scene> and <scene name='CotA_laccase/Copper_centers/7'>a trinuclear center</scene> | + | a <scene name='CotA_laccase/Mononuclear_t1copper/1'>mononuclear blue type 1 copper center</scene> and <scene name='CotA_laccase/Copper_centers/7'>a trinuclear center</scene><ref>PMID:11514528</ref> |
- | + | ||
+ | == Structural highlights == | ||
The trinuclear center has two type 3 copper ions, that can be anti-ferromagnetically | The trinuclear center 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. | ||
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}} | }} | ||
See [[Blue copper oxidase CueO]] | See [[Blue copper oxidase CueO]] | ||
+ | |||
+ | == References == | ||
+ | <references/> | ||
[[Category:Topic Page]] | [[Category:Topic Page]] |
Revision as of 11:25, 14 December 2015
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Contents |
Function
CotA laccase belong 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 : a and [1]
Structural highlights
The trinuclear center 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 CotA laccase
Updated on 14-December-2015
References
- ↑ 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
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Michal Harel, Isabel Bento, Alexander Berchansky, David Canner, Jaime Prilusky