Crystal structure of the copper-containing quercetin 2,3-dioxygenase from Aspergillus japonicus

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Fusetti, Fabrizia; Schröter, Klaus H.; Steiner, Roberto A.; Noort, Paula I. van; Pijning, Tjaard; Rozeboom, Henriëtte J.; Kalk, Kor H.; Egmond, Maarten R.; Dijkstra, Bauke W.;
  • Subject: MODELS | FLAVONOL | DIOXYGENASE | DIFFRACTION DATA | cupin | X-ray structure | X-RAYS | BOND | ANGSTROM RESOLUTION | SEED STORAGE PROTEINS | copper | quercetin | glycoprotein

Quercetin 2,3-dioxygenase is a copper-containing enzyme that catalyzes the insertion of molecular oxygen into polyphenolic flavonols. Dioxygenation catalyzed by iron-containing enzymes has been studied extensively, but dioxygenases employing other metal cofactors are po... View more
  • References (49)
    49 references, page 1 of 5

    1. Que, L., Jr. (1999). Oxygen activation at nonheme iron centers. In Bioinorganic Catalysis, J. Reedijk and E. Bouwman, eds. (New York: Marcel Dekker, Inc.), pp. 269-321.

    2. Oka, T., and Simpson, F.J. (1971). Quercetinase, a dioxygenase containing copper. Biochem. Biophys. Res. Commun. 43, 1-5.

    3. Sharma, H.K., and Vaidyanathan, C.S. (1975). A new mode of ring cleavage of 2,3-dihydroxybenzoic acid in Tecoma stans (L.). Partial purification and properties of 2,3-dihydroxybenzoate 2,3-oxygenase. Eur. J. Biochem. 56, 163-171.

    4. Boldt, Y.R., Sadowski, M.J., Ellis, L.B.M., Que, L., Jr., and Wackett, L.P. (1995). A manganese-dependent dioxygenase from Arthrobacter globiformis CM-2 belongs to the major extradiol dioxygenase family. J. Bacteriol. 177, 1225-1232.

    5. Gibello, A., Ferrer, E., Martin, M., and Garrido-Pertierra, A. (1994). 3,4-Dihydroxyphenylacetate 2,3-dioxygenase from Klebsiella pneumoniae, a Mg(2 )-containing dioxygenase involved in aromatic catabolism. Biochem. J. 301, 145-150.

    6. Abolmaali, B., Taylor, H.V., and Weser, U. (1998). Evolutionary aspects of copper binding centers in copper proteins. Struct. Bond. 91, 91-190.

    7. Holm, R.H., Kennepohl, P., and Solomon, E.I. (1996). Structural and functional aspects of metal sites in biology. Chem. Rev. 96, 2239-2314.

    8. Karlin, S., Zhu, Z.Y., and Karlin, K.D. (1997). The extended environment of mononuclear metal centers in protein structures. Proc. Natl. Acad. Sci. USA 94, 14225-14230.

    9. Hund, H.K., Breuer, J., Lingens, F., Huttermann, J., Kappl, R., and Fetzner, S. (1999). Flavonol 2,4-dioxygenase from Aspergillus niger DSM 821, a type 2 CuII-containing glycoprotein. Eur. J. Biochem. 263, 871-878.

    10. Speier, G. (1991). Quercetin 2,3-dioxygenase mimicking chemistry. In Dioxygen Activation and Homogeneous Catalytic Oxidation, L.I. Sim a´ndi, ed. (Amsterdam: Elsevier Science).

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