Laccase: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
← Older edit
Michal Harel (talk | contribs)
31,761 edits
No edit summary
Michal Harel (talk | contribs)
31,761 edits
No edit summary
 
(30 intermediate revisions by 3 users not shown)
Line 1: Line 1:
<applet load='1W6L' size='300' frame='true' align=|right| CAPTION='CotA laccase from' />
<StructureSection load='1w6l' size='350' side='right' scene='' caption='CotA laccase complex with glycerol, O2 and Cu+2 (orange), [[1w6l]]'>
== Function ==


CotA laccase belong to the multi-copper oxidase family.
'''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>. 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).  
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 struture of CotA [[1w6l]] comprises three cupredoxin domain 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>


* '''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.  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='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]].


The trinuclear center has two type 3 copper ions, that can be anti-ferromagnetically
== 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>.
 
== 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 froma variety of phenolic substrates and then transmits
electron from a variety of phenolic substrates and then transmit
it to the trinuclear centre.
it to the trinuclear centre.


==3D structures of CotA laccase==
==3D structures of laccase==
[[Laccase 3D structures]]


[[2x87]], [[2x88]], [[1w6l]], [[1w6w]], [[1w8e]], [[1gsk]] – BsCotAl – ''Bacillus subtilis''<br />
</StructureSection>
[[2bhf]] - BsCotAl reduced<br />
== References ==
[[2wsd]] – BsCotAl (mutant)<br />
<references/>
[[1of0]] - BsCotAl + EBS<br />
[[Category:Topic Page]]
[[1uvw]] - BsCotAl + ABTS

Latest revision as of 15:39, 7 July 2024

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]. 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).

  • 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. Similar to the other laccases the three dimensional structure of CotA 1w6l comprises three cupredoxin domains and four copper ions organised in :

a and .[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


CotA laccase complex with glycerol, O2 and Cu+2 (orange), 1w6l

Drag the structure with the mouse to rotate

ReferencesReferences

  1. ↑ 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
  2. ↑ 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
  3. ↑ 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
  4. ↑ 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
  5. ↑ 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
  6. ↑ 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
  7. ↑ 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

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Isabel Bento, David Canner, Jaime Prilusky, Michal Harel, Alexander Berchansky
Retrieved from "https://proteopedia.openfox.io/wiki/index.php?title=Laccase&oldid=4210191"