Multicopper oxidase
| Multicopper oxidase (type 1) | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 crystal structures of e. coli laccase cueo under different copper binding situations | |||||||||
| Identifiers | |||||||||
| Symbol | Cu-oxidase | ||||||||
| Pfam | PF00394 | ||||||||
| Pfam clan | CL0026 | ||||||||
| InterPro | IPR001117 | ||||||||
| PROSITE | PDOC00076 | ||||||||
| SCOP | 1aoz | ||||||||
| SUPERFAMILY | 1aoz | ||||||||
| |||||||||
| Multicopper oxidase (type 2) | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 active laccase from trametes versicolor complexed with 2,5-xylidine | |||||||||
| Identifiers | |||||||||
| Symbol | Cu-oxidase_2 | ||||||||
| Pfam | PF07731 | ||||||||
| Pfam clan | CL0026 | ||||||||
| InterPro | IPR011706 | ||||||||
| SCOP | 1aoz | ||||||||
| SUPERFAMILY | 1aoz | ||||||||
| |||||||||
| Multicopper oxidase (type 3) | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 crystal structures of e. coli laccase cueo under different copper binding situations | |||||||||
| Identifiers | |||||||||
| Symbol | Cu-oxidase_3 | ||||||||
| Pfam | PF07732 | ||||||||
| Pfam clan | CL0026 | ||||||||
| InterPro | IPR011707 | ||||||||
| SCOP | 1aoz | ||||||||
| SUPERFAMILY | 1aoz | ||||||||
| |||||||||
| CMulti-copper polyphenol oxidoreductase laccase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 crystal structure of protein cc_0490 from caulobacter crescentus, pfam duf152 | |||||||||
| Identifiers | |||||||||
| Symbol | Cu-oxidase_4 | ||||||||
| Pfam | PF02578 | ||||||||
| InterPro | IPR003730 | ||||||||
| |||||||||
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]
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
- ↑ 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. PMID 16234932. doi:10.1039/b504806k.
- ↑ 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. PMID 2404764. doi:10.1111/j.1432-1033.1990.tb15311.x.
- ↑ 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. PMID 1995346. doi:10.1016/0014-5793(91)80254-Z.
- 1 2 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. PMC 122422
. PMID 11867755. doi:10.1073/pnas.052710499. - ↑ 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. PMID 14572631. doi:10.1016/S0014-5793(03)01000-7.
- ↑ Suzuki S, Kataoka K, Yamaguchi K (October 2000). "Metal coordination and mechanism of multicopper nitrite reductase". Acc. Chem. Res. 33 (10): 728–35. PMID 11041837. doi:10.1021/ar9900257.
- ↑ 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. PMID 3052293. doi:10.1146/annurev.bi.57.070188.004411.
- ↑ 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. PMID 8293473. doi:10.1016/0092-8674(94)90346-8.
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