User:Estelle Blochouse/ Sandbox 1497

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== Function ==
== Function ==
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Multicopper oxidases are enzymes involved in copper homeostasis. Copper as many metal ions is used in multiple biological processes such as detoxification of oxygen free radicals and pigmentation. However copper present in a cell bot bounded to a protein if harmfull and can cause cellular damage. It need to be regulated.
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Multicopper oxidases are enzymes involved in copper homeostasis. Copper as many metal ions is used in multiple biological processes such as detoxification of oxygen free radicals and pigmentation. However copper present in a cell not bounded to a protein is harmful and can cause cellular damage. It need to be regulated.
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Multicopper oxidase act probably for the detoxification of copper present in the periplasmic space. It oxidize the Cu+ into Cu2+ and prevent its uptake by the cytoplasm. It also possesses a phenoloxidase and ferroxidase activities which can be involved in the prevention of oxidative damage.<ref><span class='plainlinks'>[https://www.uniprot.org/uniprot/P36649 UniProtKB]</span></ref>
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Multicopper oxidase acts probably for the detoxification of copper present in the periplasmic space. It oxidizes the Cu+ into Cu2+ and prevents its uptake by the cytoplasm. It also possesses a phenoloxidase and ferroxidase activities which can be involved in the prevention of oxidative damage.<ref><span class='plainlinks'>[https://www.uniprot.org/uniprot/P36649 UniProtKB]</span></ref>
Multicopper oxidase might also be involved in the regulation of metal transport.
Multicopper oxidase might also be involved in the regulation of metal transport.
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<tr><td>I</td><td>P</td><td>P</td><td>G</td><td>G</td><td>K</td><td>R</td><td>S</td><td>V</td><td>T</td><td>L</td><td>N</td><td>V</td><td>D</td><td>Q</td><td>P</td><td>A</td><td>A</td><td>T</td><td>C</td><td>W</td><td>F</td><td class="sblockLbl">H</td><td>P</td><td color="FFC0CB">H</td><td>Q</td><td>H</td><td>G</td><td>K</td><td>T</td></tr>
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Revision as of 16:07, 11 January 2019

Multicopper Oxidase CueO (4e9s)

4e9s, resolution 1.06Å

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References

  1. ↑ EMBL-EBI, Family: Cu-oxidase (PF00394), Summary: Multicopper oxidase, http://pfam.xfam.org/family/Cu-oxidase
  2. ↑ UniProtKB
  3. ↑ Bento I, Martins LO, Gato Lopes G, Arménia Carrondo M, Lindley PF, Dioxygen reduction by multi-copper oxidases; a structural perspective, November 2005
  4. ↑ Messerschmidt A, Huber R, The blue oxidases, ascorbate oxidase, laccase and ceruloplasmin. Modelling and structural relationships, Eur. J. Biochem. 187, January 1990
  5. ↑ Ouzounis C, Sander C, A structure-derived sequence pattern for the detection of type I copper binding domains in distantly related proteins, FEBS Lett. volume 279, February 1991
  6. ↑ Hirofumi Komori, Ryosuke Sugiyama, Kunishige Kataoka, Kentaro Miyazaki, Yoshiki Higuchib, and Takeshi Sakurai, New insights into the catalytic active-site structure of multicopper oxidases, Biological Crystallography, 6 December 2013 doi:10.1107/S1399004713033051
  7. ↑ RCBS PDB
  8. ↑ RCBS PDB
  9. ↑ RCBS PDB
  10. ↑ RCBS PDB
  11. ↑ RCBS PDB
  12. ↑ RCBS PDB
  13. ↑ Kataoka K, Komori H, Ueki Y, Konno Y, Kamitaka Y, Kurose S, Tsujimura S, Higuchi Y, Kano K, Seo D, Sakurai T. Structure and function of the engineered multicopper oxidase CueO from Escherichia coli--deletion of the methionine-rich helical region covering the substrate-binding site. J Mol Biol. 2007 Oct 12;373(1):141-52. Epub 2007 Aug 2. PMID:17804014 doi:10.1016/j.jmb.2007.07.041

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