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; dioxygenbinds 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:
LaccaseEC 1.10.3.2 (urishiol oxidase), a 3-domain enzyme found in fungi and plants, which oxidizes different phenols and diamines. CueO is a laccase found in Escherichia coli that is involved in copper-resistance.[4]
^Bento I, Martins LO, Gato Lopes G, Arménia Carrondo M, Lindley PF (November 2005). "Dioxygen reduction by multi-copper oxidases; a structural perspective". Dalton Transactions (21): 3507–13. doi:10.1039/b504806k. PMID 16234932.
^Messerschmidt A, Huber R (January 1990). "The blue oxidases, ascorbate oxidase, laccase and ceruloplasmin. Modelling and structural relationships". Eur. J. Biochem. 187 (2): 341–52. doi:10.1111/j.1432-1033.1990.tb15311.x. PMID 2404764.
^Ouzounis C, Sander C (February 1991). "A structure-derived sequence pattern for the detection of type I copper binding domains in distantly related proteins". FEBS Lett. 279 (1): 73–8. doi:10.1016/0014-5793(91)80254-Z. PMID 1995346. S2CID 10299194.
^ abRoberts SA, Weichsel A, Grass G, Thakali K, Hazzard JT, Tollin G, Rensing C, Montfort WR (March 2002). "Crystal structure and electron transfer kinetics of CueO, a multicopper oxidase required for copper homeostasis in Escherichia coli". Proc. Natl. Acad. Sci. U.S.A. 99 (5): 2766–71. doi:10.1073/pnas.052710499. PMC122422. PMID 11867755.
^Nakamura K, Kawabata T, Yura K, Go N (October 2003). "Novel types of two-domain multi-copper oxidases: possible missing links in the evolution". FEBS Lett. 553 (3): 239–44. doi:10.1016/S0014-5793(03)01000-7. PMID 14572631. S2CID 85060706.
^Suzuki S, Kataoka K, Yamaguchi K (October 2000). "Metal coordination and mechanism of multicopper nitrite reductase". Acc. Chem. Res. 33 (10): 728–35. doi:10.1021/ar9900257. PMID 11041837.
^Mann KG, Jenny RJ, Krishnaswamy S (1988). "Cofactor proteins in the assembly and expression of blood clotting enzyme complexes". Annu. Rev. Biochem. 57: 915–56. doi:10.1146/annurev.bi.57.070188.004411. PMID 3052293.
^Askwith C, Eide D, Van Ho A, Bernard PS, Li L, Davis-Kaplan S, Sipe DM, Kaplan J (January 1994). "The FET3 gene of S. cerevisiae encodes a multicopper oxidase required for ferrous iron uptake". Cell. 76 (2): 403–10. doi:10.1016/0092-8674(94)90346-8. PMID 8293473. S2CID 27473253.
This article incorporates text from the public domain Pfam and InterPro: IPR001117
This article incorporates text from the public domain Pfam and InterPro: IPR011706
This article incorporates text from the public domain Pfam and InterPro: IPR011707
This article incorporates text from the public domain Pfam and InterPro: IPR003730
^Lawton, Thomas J.; Sayavedra-Soto, Luis A.; Arp, Daniel J.; Rosenzweig, Amy C. (2009-04-10). "Crystal Structure of a Two-domain Multicopper Oxidase *". Journal of Biological Chemistry. 284 (15): 10174–10180. doi:10.1074/jbc.M900179200. ISSN 0021-9258. PMID 19224923.
January 13, 2023
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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 Ceruloplasmin EC 1 16 3 1 ferroxidase a 6 domain enzyme found in the serum of mammals and birds that oxidizes different inorganic and organic substances exhibits internal sequence homology that appears to have evolved from the triplication of a Cu binding domain similar to that of laccase and ascorbate oxidase Laccase EC 1 10 3 2 urishiol oxidase a 3 domain enzyme found in fungi and plants which oxidizes different phenols and diamines CueO is a laccase found in Escherichia coli that is involved in copper resistance 4 Ascorbate oxidase EC 1 10 3 3 a 3 domain enzyme found in higher plants Nitrite reductase EC 1 7 2 1 a 2 domain enzyme containing type 1 and type 2 copper centres 5 6 Multicopper oxidase type 1 crystal structures of e coli laccase cueo under different copper binding situationsIdentifiersSymbolCu oxidasePfamPF00394Pfam clanCL0026InterProIPR001117PROSITEPDOC00076SCOP21aoz SCOPe SUPFAMMembranome253Available protein structures Pfam structures ECOD PDBRCSB PDB PDBe PDBjPDBsumstructure summaryMulticopper oxidase type 2 active laccase from trametes versicolor complexed with 2 5 xylidineIdentifiersSymbolCu oxidase 2PfamPF07731Pfam clanCL0026InterProIPR011706SCOP21aoz SCOPe SUPFAMAvailable protein structures Pfam structures ECOD PDBRCSB PDB PDBe PDBjPDBsumstructure summaryMulticopper oxidase type 3 crystal structures of e coli laccase cueo under different copper binding situationsIdentifiersSymbolCu oxidase 3PfamPF07732Pfam clanCL0026InterProIPR011707SCOP21aoz SCOPe SUPFAMAvailable protein structures Pfam structures ECOD PDBRCSB PDB PDBe PDBjPDBsumstructure summaryCMulti copper polyphenol oxidoreductase laccasecrystal structure of protein cc 0490 from caulobacter crescentus pfam duf152IdentifiersSymbolCu oxidase 4PfamPF02578InterProIPR003730Available protein structures Pfam structures ECOD PDBRCSB PDB PDBe PDBjPDBsumstructure summary 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 References Edit Bento I Martins LO Gato Lopes G Armenia Carrondo M Lindley PF November 2005 Dioxygen reduction by multi copper oxidases a structural perspective Dalton Transactions 21 3507 13 doi 10 1039 b504806k PMID 16234932 Messerschmidt A Huber R January 1990 The blue oxidases ascorbate oxidase laccase and ceruloplasmin Modelling and structural relationships Eur J Biochem 187 2 341 52 doi 10 1111 j 1432 1033 1990 tb15311 x PMID 2404764 Ouzounis C Sander C February 1991 A structure derived sequence pattern for the detection of type I copper binding domains in distantly related proteins FEBS Lett 279 1 73 8 doi 10 1016 0014 5793 91 80254 Z PMID 1995346 S2CID 10299194 a b Roberts SA Weichsel A Grass G Thakali K Hazzard JT Tollin G Rensing C Montfort WR March 2002 Crystal structure and electron transfer kinetics of CueO a multicopper oxidase required for copper homeostasis in Escherichia coli Proc Natl Acad Sci U S A 99 5 2766 71 doi 10 1073 pnas 052710499 PMC 122422 PMID 11867755 Nakamura K Kawabata T Yura K Go N October 2003 Novel types of two domain multi copper oxidases possible missing links in the evolution FEBS Lett 553 3 239 44 doi 10 1016 S0014 5793 03 01000 7 PMID 14572631 S2CID 85060706 Suzuki S Kataoka K Yamaguchi K October 2000 Metal coordination and mechanism of multicopper nitrite reductase Acc Chem Res 33 10 728 35 doi 10 1021 ar9900257 PMID 11041837 Mann KG Jenny RJ Krishnaswamy S 1988 Cofactor proteins in the assembly and expression of blood clotting enzyme complexes Annu Rev Biochem 57 915 56 doi 10 1146 annurev bi 57 070188 004411 PMID 3052293 Askwith C Eide D Van Ho A Bernard PS Li L Davis Kaplan S Sipe DM Kaplan J January 1994 The FET3 gene of S cerevisiae encodes a multicopper oxidase required for ferrous iron uptake Cell 76 2 403 10 doi 10 1016 0092 8674 94 90346 8 PMID 8293473 S2CID 27473253 1 This article incorporates text from the public domain Pfam and InterPro IPR001117 This article incorporates text from the public domain Pfam and InterPro IPR011706 This article incorporates text from the public domain Pfam and InterPro IPR011707 This article incorporates text from the public domain Pfam and InterPro IPR003730 Lawton Thomas J Sayavedra Soto Luis A Arp Daniel J Rosenzweig Amy C 2009 04 10 Crystal Structure of a Two domain Multicopper Oxidase Journal of Biological Chemistry 284 15 10174 10180 doi 10 1074 jbc M900179200 ISSN 0021 9258 PMID 19224923 Retrieved from https en wikipedia org w index php title Multicopper oxidase amp oldid 1113330552, wikipedia, wiki, book, books, library,
