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X-ray diffraction study of Penicillium Vitale catalase in the complex with aminotriazole

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Abstract

The three-dimensional structure of the enzyme catalase from Penicillium vitale in a complex with the inhibitor aminotriazole was solved and refined by protein X-ray crystallography methods. An analysis of the three-dimensional structure of the complex showed that the inhibition of the enzyme occurs as a result of the covalent binding of aminotriazole to the amino-acid residue His64 in the active site of the enzyme. An investigation of the three-dimensional structure of the complex resulted in the amino-acid residues being more precisely identified. The binding sites of saccharide residues and calcium ions in the protein molecule were found.

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Authors and Affiliations

  1. Shubnikov Institute of Crystallography, Russian Academy of Sciences, Leninskii pr. 59, Moscow, 119333, Russia

    A. A. Borovik, A. I. Grebenko & V. R. Melik-Adamyan

Authors
  1. A. A. Borovik
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  2. A. I. Grebenko
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  3. V. R. Melik-Adamyan
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Correspondence to V. R. Melik-Adamyan.

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Dedicated to the memory of B.K. Vainshtein

Original Russian Text © A.A. Borovik, A.I. Grebenko, V.R. Melik-Adamyan, 2011, published in Kristallografiya, 2011, Vol. 56, No. 4, pp. 635–640.

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Borovik, A.A., Grebenko, A.I. & Melik-Adamyan, V.R. X-ray diffraction study of Penicillium Vitale catalase in the complex with aminotriazole. Crystallogr. Rep. 56, 590–595 (2011). https://doi.org/10.1134/S1063774511030060

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  • DOI: https://doi.org/10.1134/S1063774511030060

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