| 词条 | Multicopper oxidase |
| 释义 |
| Symbol = Cu-oxidase | Name = Multicopper oxidase (type 1) | image = PDB 2fqg EBI.jpg | width = | caption = crystal structures of e. coli laccase cueo under different copper binding situations | Pfam = PF00394 | Pfam_clan = CL0026 | InterPro = IPR001117 | SMART = | PROSITE = PDOC00076 | MEROPS = | SCOP = 1aoz | TCDB = | OPM family = | OPM protein = | CAZy = | CDD = |Membranome superfamily = 253 }}{{Infobox protein family | Symbol = Cu-oxidase_2 | Name = Multicopper oxidase (type 2) | image = PDB 1kya EBI.jpg | width = | caption = active laccase from trametes versicolor complexed with 2,5-xylidine | Pfam = PF07731 | Pfam_clan = CL0026 | InterPro = IPR011706 | SMART = | PROSITE = | MEROPS = | SCOP = 1aoz | TCDB = | OPM family = | OPM protein = | CAZy = | CDD = }}{{Infobox protein family | Symbol = Cu-oxidase_3 | Name = Multicopper oxidase (type 3) | image = PDB 2fqe EBI.jpg | width = | caption = crystal structures of e. coli laccase cueo under different copper binding situations | Pfam = PF07732 | Pfam_clan = CL0026 | InterPro = IPR011707 | SMART = | PROSITE = | MEROPS = | SCOP = 1aoz | TCDB = | OPM family = | OPM protein = | CAZy = | CDD = }}{{Infobox protein family | Symbol = Cu-oxidase_4 | Name = CMulti-copper polyphenol oxidoreductase laccase | image = PDB 1xfj EBI.jpg | width = | caption = crystal structure of protein cc_0490 from caulobacter crescentus, pfam duf152 | Pfam = PF02578 | Pfam_clan = | InterPro = IPR003730 | SMART = | PROSITE = | MEROPS = | SCOP = | TCDB = | OPM family = | OPM protein = | CAZy = | CDD = }} In molecular biology, multicopper oxidases are enzymes which oxidise their substrate by accepting electrons at a mononuclear copper centre and transferring them to a trinuclear copper centre; dioxygen binds to the trinuclear centre and, following the transfer of four electrons, is reduced to two molecules of water.[1] There are three spectroscopically different copper centres found in multicopper oxidases: type 1 (or blue), type 2 (or normal) and type 3 (or coupled binuclear).[2][3] Multicopper oxidases consist of 2, 3 or 6 of these homologous domains, which also share homology with the cupredoxins azurin and plastocyanin. Structurally, these domains consist of a cupredoxin-like fold, a beta-sandwich consisting of 7 strands in 2 beta-sheets, arranged in a Greek-key beta-barrel.[4] Multicopper oxidases include:
In addition to the above enzymes there are a number of other proteins that are similar to the multi-copper oxidases in terms of structure and sequence, some of which have lost the ability to bind copper. These include: copper resistance protein A (copA) from a plasmid in Pseudomonas syringae; domain A of (non-copper binding) blood coagulation factors V (Fa V) and VIII (Fa VIII);[7] yeast Fet3p (FET3) required for ferrous iron uptake;[8] yeast hypothetical protein YFL041w; and the fission yeast homologue SpAC1F7.08. References1. ^{{cite journal | vauthors = Bento I, Martins LO, Gato Lopes G, Arménia Carrondo M, Lindley PF | title = Dioxygen reduction by multi-copper oxidases; a structural perspective | journal = Dalton Transactions | volume = | issue = 21 | pages = 3507–13 |date=November 2005 | pmid = 16234932 | doi = 10.1039/b504806k | url = }} {{InterPro content|IPR001117}}{{InterPro content|IPR011706}}{{InterPro content|IPR011707}}{{InterPro content|IPR003730}}2. ^{{cite journal | vauthors = Messerschmidt A, Huber R | title = The blue oxidases, ascorbate oxidase, laccase and ceruloplasmin. Modelling and structural relationships | journal = Eur. J. Biochem. | volume = 187 | issue = 2 | pages = 341–52 |date=January 1990 | pmid = 2404764 | doi = 10.1111/j.1432-1033.1990.tb15311.x | url = }} 3. ^{{cite journal | vauthors = Ouzounis C, Sander C | title = A structure-derived sequence pattern for the detection of type I copper binding domains in distantly related proteins | journal = FEBS Lett. | volume = 279 | issue = 1 | pages = 73–8 |date=February 1991 | pmid = 1995346 | doi = 10.1016/0014-5793(91)80254-Z| url = }} 4. ^1 {{cite journal | vauthors = Roberts SA, Weichsel A, Grass G, Thakali K, Hazzard JT, Tollin G, Rensing C, Montfort WR | title = Crystal structure and electron transfer kinetics of CueO, a multicopper oxidase required for copper homeostasis in Escherichia coli | journal = Proc. Natl. Acad. Sci. U.S.A. | volume = 99 | issue = 5 | pages = 2766–71 |date=March 2002 | pmid = 11867755 | pmc = 122422 | doi = 10.1073/pnas.052710499 | url = }} 5. ^{{cite journal | vauthors = Nakamura K, Kawabata T, Yura K, Go N | title = Novel types of two-domain multi-copper oxidases: possible missing links in the evolution | journal = FEBS Lett. | volume = 553 | issue = 3 | pages = 239–44 |date=October 2003 | pmid = 14572631 | doi = 10.1016/S0014-5793(03)01000-7| url = }} 6. ^{{cite journal | vauthors = Suzuki S, Kataoka K, Yamaguchi K | title = Metal coordination and mechanism of multicopper nitrite reductase | journal = Acc. Chem. Res. | volume = 33 | issue = 10 | pages = 728–35 |date=October 2000 | pmid = 11041837 | doi = 10.1021/ar9900257| url = }} 7. ^{{cite journal | vauthors = Mann KG, Jenny RJ, Krishnaswamy S | title = Cofactor proteins in the assembly and expression of blood clotting enzyme complexes | journal = Annu. Rev. Biochem. | volume = 57 | issue = | pages = 915–56 | year = 1988 | pmid = 3052293 | doi = 10.1146/annurev.bi.57.070188.004411 | url = }} 8. ^{{cite journal | vauthors = Askwith C, Eide D, Van Ho A, Bernard PS, Li L, Davis-Kaplan S, Sipe DM, Kaplan J | title = The FET3 gene of S. cerevisiae encodes a multicopper oxidase required for ferrous iron uptake | journal = Cell | volume = 76 | issue = 2 | pages = 403–10 |date=January 1994 | pmid = 8293473 | doi = 10.1016/0092-8674(94)90346-8| url = }} 1 : Protein domains |
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