Sandbox Reserved 1104
From Proteopedia
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Multicopper oxidases are enzymes which oxidise their substrate by accepting electrons at a mononuclear copper centre and transferring them to a trinuclear copper centre.<ref>Wikipedia, Multicopper oxidase [https://en.wikipedia.org/wiki/Multicopper_oxidase]</ref> | Multicopper oxidases are enzymes which oxidise their substrate by accepting electrons at a mononuclear copper centre and transferring them to a trinuclear copper centre.<ref>Wikipedia, Multicopper oxidase [https://en.wikipedia.org/wiki/Multicopper_oxidase]</ref> | ||
- | Bilirubin oxidases are multicopper oxidases containing type 1, type 2, and type 3 coppers. Indeed, there is strong sequence homology between bilirubin oxidase and multicopper oxidases like laccase, ascorbate oxidase and even ceruloplasmin. Moreover, the His-Cys-His sequence, characteristic of multicopper oxidase, is present in bilirubin oxidase. Copper is essential for the enzyme activity.<ref name="multic">Atsushi Shimizu, ''Myrothecium verrucaria'' Bilirubin Oxidase and Its Mutants for Potential Copper Ligands (1999)[https://doi.org/10.1021/bi9819531]</ref> | + | Bilirubin oxidases are multicopper oxidases containing type 1, type 2, and type 3 coppers. Indeed, there is strong sequence homology between bilirubin oxidase and multicopper oxidases like laccase, ascorbate oxidase and even ceruloplasmin. Moreover, the His-Cys-His sequence, characteristic of multicopper oxidase, is present in bilirubin oxidase. Copper is essential for the enzyme activity.<ref name="multic">Atsushi Shimizu, Jung-Hee Kwon, Takashi Sasaki, Takanori Satoh, Nobuhiko Sakurai, Takeshi Sakurai, Shotaro Yamaguchi, Tatsuya Samejima, ''Myrothecium verrucaria'' Bilirubin Oxidase and Its Mutants for Potential Copper Ligands (1999)[https://doi.org/10.1021/bi9819531]</ref> |
== Function == | == Function == |
Revision as of 13:35, 12 January 2020
This Sandbox is Reserved from 25/11/2019, through 30/9/2020 for use in the course "Structural Biology" taught by Bruno Kieffer at the University of Strasbourg, ESBS. This reservation includes Sandbox Reserved 1091 through Sandbox Reserved 1115. |
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References
- ↑ Hanson, R. M., Prilusky, J., Renjian, Z., Nakane, T. and Sussman, J. L. (2013), JSmol and the Next-Generation Web-Based Representation of 3D Molecular Structure as Applied to Proteopedia. Isr. J. Chem., 53:207-216. doi:http://dx.doi.org/10.1002/ijch.201300024
- ↑ Herraez A. Biomolecules in the computer: Jmol to the rescue. Biochem Mol Biol Educ. 2006 Jul;34(4):255-61. doi: 10.1002/bmb.2006.494034042644. PMID:21638687 doi:10.1002/bmb.2006.494034042644
- ↑ Wikipedia, Multicopper oxidase [1]
- ↑ Atsushi Shimizu, Jung-Hee Kwon, Takashi Sasaki, Takanori Satoh, Nobuhiko Sakurai, Takeshi Sakurai, Shotaro Yamaguchi, Tatsuya Samejima, Myrothecium verrucaria Bilirubin Oxidase and Its Mutants for Potential Copper Ligands (1999)[2]
- ↑ 5.0 5.1 A. de Poulpiquet, Reprinted from Electrochemistry Communications, Volume 42 (2014). [3]
- ↑ 6.0 6.1 A. de Poulpiquet, Design of a H2/O2 biofuel cell based on thermostable enzymes (2014). [4]