This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
Laccase
From Proteopedia
(Difference between revisions)
| Line 2: | Line 2: | ||
== Function == | == 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><ref>PMID:15036303</ref> | + | '''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>. '''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. |
| - | '''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, | ||
| Line 12: | Line 11: | ||
For laccase with nitrotyrosine modification see [[Nitrotyrosine]]. | For laccase with nitrotyrosine modification see [[Nitrotyrosine]]. | ||
| + | |||
| + | == 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 == | == Structural highlights == | ||
| Line 21: | Line 24: | ||
it to the trinuclear centre. | it to the trinuclear centre. | ||
| + | ==3D structures of laccase== | ||
[[Laccase 3D structures]] | [[Laccase 3D structures]] | ||
</StructureSection> | </StructureSection> | ||
| - | ==3D structures of | + | ==3D structures of laccase== |
Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}} | Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}} | ||
{{#tree:id=OrganizedByTopic|openlevels=0| | {{#tree:id=OrganizedByTopic|openlevels=0| | ||
| + | |||
| + | *Laccase | ||
| + | |||
| + | **[[1v10]] – Lac + Cu – ''Rigidoporus lignosus''<br /> | ||
| + | **[[2h5u]] – Lac + Cu – ''Trametes maxima''<br /> | ||
| + | **[[2hzh]] – Lac + Cu – ''Trametes ochracea''<br /> | ||
| + | **[[3x1b]] – Lac + Cu – ''Lentinus''<br /> | ||
| + | **[[5anh]] – Lac + Cu – ''Basidiomycete''<br /> | ||
| + | **[[5ehf]] – Lac + Cu – ''Antrodiella faginea''<br /> | ||
| + | **[[4a2d]], [[4a2e]], [[4a2f]], [[4a2g]], [[4a2h]], [[5a7e]] – Lac + Cu – ''Coriolopsis gallica''<br /> | ||
| + | **[[4jhu]], [[4jhv]] – Lac + Cu – ''Coriolopsis caperata''<br /> | ||
| + | **[[3t6v]], [[3t6w]], [[3t6x]], [[3t6z]], [[3t71]] – Lac + Cu – ''Steccherinum ochraceum''<br /> | ||
| + | **[[3sqr]], [[4x4k]] – BaLac + Cu – ''Botrytis aclada''<br /> | ||
| + | **[[3v9e]] – BaLac (mutant) + Cu <br /> | ||
| + | **[[2xuw]], [[2xvb]] – TtLac – ''Thermus thermophilus''<br /> | ||
| + | **[[2yap]], [[5jx9]], [[5k0d]], [[5k15]], [[5k3k]], [[5k5k]], [[5k7a]], [[5k84]] – TtLac + Cu <br /> | ||
| + | **[[2xu9]] – TtLac (mutant) + Cu <br /> | ||
| + | **[[2yae]], [[5jrr]] – TtLac + Cu + O2 <br /> | ||
| + | **[[2yaf]], [[2yah]], [[2yam]], [[2yao]], [[2yaq]], [[2yar]], [[5afa]] – TtLac + Cu + OH <br /> | ||
| + | **[[2xyb]] – Lac + Cu + O2 – ''Pycnoporus cinnabarinus'' <br /> | ||
| + | **[[3pps]] – Lac + Cu + O2 – ''Thielavia arenaria'' <br /> | ||
| + | **[[3cg8]] – Lac + Cu + O – ''Streptomyces coelicolor'' <br /> | ||
| + | **[[3tbb]] – Lac + Cu + O2 – ''Streptomyces viridosporus'' <br /> | ||
| + | **[[4f7k]] – Lac – uncultured bacterium<br /> | ||
| + | **[[5nq7]], [[5nq8]], [[5nq9]] – Lac + Cu + O2 – ''Trametes sanguinea''<br /> | ||
| + | **[[5z1x]], [[5z22]] – Lac + Cu + O2 – ''Cerrena''<br /> | ||
| + | |||
| + | *Laccase 1 | ||
| + | |||
| + | **[[3qpk]] – MaLac1 + Cu – ''Melanocarpus albomyces''<br /> | ||
| + | **[[1gw0]], [[2ih8]], [[2ih9]], [[2q9o]] – MaLac1 + Cu + O <br /> | ||
| + | **[[3dkh]] – MaLac1 (mutant) + Cu + O2<br /> | ||
| + | **[[3fu7]], [[3fu8]], [[3fu9]] – MaLac1 + Cu + O2 + phenol derivative<br /> | ||
| + | **[[1hfu]] – icfLac1 + Cu – inky cap fungus<br /> | ||
| + | **[[5ldu]] – wrfLac1 + Cu – white-rot fungus<br /> | ||
| + | **[[6f5k]] – Lac1 + Cu + OH – ''Myceliophthora thermophila'' <br /> | ||
| + | |||
| + | *Laccase 2 | ||
| + | |||
| + | **[[1a65]] – icfLac2 + Cu + O <br /> | ||
| + | **[[1gyc]], [[3fpx]], [[3kw7]], [[3pxl]] – wrfLac2 + Cu <br /> | ||
| + | **[[3v9c]] – wrfLac2 + Cu + O2<br /> | ||
| + | **[[1kya]] – Lac2 + Cu + arylamine – ''Trametes versicolor''<br /> | ||
| + | **[[5e9n]], [[6rgh]] – SmLac2 + Cu – ''Steccherinum murashkinskyi''<br /> | ||
| + | **[[5mej]], [[5mew]], [[5mhu]], [[5mhv]], [[5mhw]], [[5mhx]], [[5mhy]], [[5mhz]], [[5mi1]], [[5mi2]], [[5mia]], [[5mib]], [[5mic]], [[5mid]], [[5mie]], [[5mig]], [[6rgp]], [[6rhh]], [[6rhi]], [[6rho]], [[6rhp]], [[6rhr]], [[6rhu]], [[6rhx]], [[6ri0]], [[6ri2]], [[6ri4]], [[6ri6]], [[6ri8]], [[6rii]], [[6rik]], [[6ril]] – SmLac2 + Cu + O2<br /> | ||
| + | |||
| + | *Two-domain laccase | ||
| + | |||
| + | **[[2zwn]] – Lac + Cu + Cu-O-Cu – metagenomes<br /> | ||
| + | **[[5lhl]] – SgLac + Cu + O2 – ''Streptomyces griseoflavus'' <br /> | ||
| + | **[[5mkm]], [[5o3k]], [[5o4i]], [[5o4q]], [[6fc7]], [[6fdj]] – SgLac (mutant) + Cu + O2 + O <br /> | ||
*CotA laccase | *CotA laccase | ||
Revision as of 10:04, 16 May 2019
| |||||||||||
3D structures of 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
- ↑ 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
- ↑ 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
- ↑ 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:http://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:http://dx.doi.org/10.4061/2011/217861
Proteopedia Page Contributors and Editors (what is this?)
Michal Harel, Isabel Bento, Alexander Berchansky, David Canner, Jaime Prilusky

