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Peroxidase stability related to its calcium and glycans

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Abstract

Peroxidases are known to be very stable enzymes. The reasons for such have not yet been fully investigated. Cationic peroxidase from cultured peanut peroxidase can be obtained in substantial amounts and can easily be purified. It is thus an ideal enzyme for study. Through immunological assays its site in the cell has been found and a function determined. With crystals and X-ray diffraction thereof, a 3-D structure of the protein is available. The sites of the heme as well as the 2 calcium ions have been located. With the cDNA it was possible to determine the sites for three glycan chains on the protein. Good progress is being made on the elucidation of the structure of these glycan chains. While both calcium and glycans influence the stability of the protein, the search for how the glycans control the folding pattern is harder than to define the role of calcium. Site-directed mutagenesis has been carried out in each of the three binding sites in turn to determine the role of each glycan. Further work with Mass Spectroscopy. using Electron Spin Ionization tandem Mass Spectroscopy (ESI MS/MS) is underway.

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Authors and Affiliations

  1. Department of Biology, The University of Western Ontario, London, Ontario, N6A 5B7, Canada

    Robert B. van Huystee

  2. Departamento de Quimica Fisica, Facultad de Ciencias Quimicas, Universidad de Salamanca, 37008, Spain

    Manuel G. Roig

  3. Departamento de Bioquimica y Biologia Molecular, Facultad de Biologia, Universidad de Salamanca, 37007, Salamanca, Spain

    Valery L. Shnyrov

  4. Department of Chemical Enzymology, Faculty of Chemistry, Moscow State University, Moscow, 119899, Russia

    Ivan Y. Sakharov

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van Huystee, R.B., Roig, M.G., Shnyrov, V.L. et al. Peroxidase stability related to its calcium and glycans. Phytochemistry Reviews 3, 19–28 (2004). https://doi.org/10.1023/B:PHYT.0000047802.79211.32

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