Sandbox Reserved 1104
From Proteopedia
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== Introduction == | == Introduction == | ||
- | Bilirubin oxidase is an enzyme known to catalyze the oxidation of bilirubin to biliverdin by reducting O2 in water. It’s a multicopper oxidase which can exist under two different structures in the ascomycete Myrothecium verrucaria (see the 3abg one | + | Bilirubin oxidase is an enzyme known to catalyze the oxidation of bilirubin to biliverdin by reducting O2 in water. It’s a multicopper oxidase which can exist under two different structures in the ascomycete Myrothecium verrucaria (see the 3abg one <ref> [http://proteopedia.org/wiki/index.php/3abg]). The 2xII form is a 4 chain structure with 8 ligands NAG-NAG belonging to the family of oxidoreductases. |
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It was first isolated in 1981 by the scientists Sawao Murao and Noriaki Tanaka as they tried to find a microorganism able to decolore raw sewage and to use it as an analytical tool in clinical fields. Now, bilirubin oxidase may be used to determine free hemoglobin in icteric specimens and can be use as a treatment for neonatal jaundice. | It was first isolated in 1981 by the scientists Sawao Murao and Noriaki Tanaka as they tried to find a microorganism able to decolore raw sewage and to use it as an analytical tool in clinical fields. Now, bilirubin oxidase may be used to determine free hemoglobin in icteric specimens and can be use as a treatment for neonatal jaundice. | ||
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Moreover, the bilirubin oxidase is an enzyme that is active in porphyrin and chlorophyll metabolism. | Moreover, the bilirubin oxidase is an enzyme that is active in porphyrin and chlorophyll metabolism. | ||
Revision as of 13:53, 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
- ↑ [1]). The 2xII form is a 4 chain structure with 8 ligands NAG-NAG belonging to the family of oxidoreductases.
It was first isolated in 1981 by the scientists Sawao Murao and Noriaki Tanaka as they tried to find a microorganism able to decolore raw sewage and to use it as an analytical tool in clinical fields. Now, bilirubin oxidase may be used to determine free hemoglobin in icteric specimens and can be use as a treatment for neonatal jaundice.
Moreover, the bilirubin oxidase is an enzyme that is active in porphyrin and chlorophyll metabolism.
Structure
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]</li> <li id="cite_note-multic-3">↑ <sup>[[#cite_ref-multic_3-0|4.0]]</sup> <sup>[[#cite_ref-multic_3-1|4.1]]</sup> <sup>[[#cite_ref-multic_3-2|4.2]]</sup> Shimizu A, Kwon JH, Sasaki T, Satoh T, Sakurai N, Sakurai T, Yamaguchi S, Samejima T. Myrothecium verrucaria bilirubin oxidase and its mutants for potential copper ligands. Biochemistry. 1999 Mar 9;38(10):3034-42. doi: 10.1021/bi9819531. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10074356 10074356] doi:[http://dx.doi.org/10.1021/bi9819531 http://dx.doi.org/10.1021/bi9819531]</li> <li id="cite_note-bcell-4">↑ <sup>[[#cite_ref-bcell_4-0|5.0]]</sup> <sup>[[#cite_ref-bcell_4-1|5.1]]</sup> A. de Poulpiquet, A. Ciaccafava, R. Gadiou, S. Gounel, M.T. Giudici-Orticoni, N. Mano, E. Lojou, Reprinted from Electrochemistry Communications, Volume 42 (2014). [http://archives.cnrs.fr/inc/article/lojou]</li> <li id="cite_note-bcell2-5">↑ <sup>[[#cite_ref-bcell2_5-0|6.0]]</sup> <sup>[[#cite_ref-bcell2_5-1|6.1]]</sup> A. de Poulpiquet, A. Ciaccafava, R. Gadiou, S. Gounel, M.T. Giudici-Orticoni, N. Mano, E. Lojou, Design of a H2/O2 biofuel cell based on thermostable enzymes (2014) [ https://doi.org/10.1016/j.elecom.2014.02.012
]</li></ol></ref>