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Kinetics of Thermoinactivation of D-Amino Acid Oxidase OPADAAO1 from the Ogataea parapolymorpha DL-1 Yeast

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Moscow University Chemistry Bulletin Aims and scope

Abstract

Our earlier annotation of the genome of the yeast Ogataea parapolymorpha DL-1 made it possible to identify five genes of potential D-amino acids oxidases. All opadaao1–opadaao5 genes were cloned and expressed in E. coli. Four OpaDAAO1-OpaDAAO4 enzymes were obtained in highly purified form and their catalytic properties were studied. It was found that among all DAAO described in the literature, the enzyme OpaDAAOl has the highest catalytic constant kcat with D-Ala, which makes it promising for practical applications. However, in addition to good catalytic parameters, effective application of the enzyme in practice requires stability and knowledge of the inactivation mechanism, including at elevated temperatures. In this paper, we study the effect of elevated temperatures on the stability of OpaDAAOl. The enzyme is shown to have higher thermal stability than the majority of other D-amino acid oxidases. The kinetics of OpaDAAOl inactivation at different temperatures, at the initial concentrations of the enzyme, and in the presence of exogenous FAD are studied. A possible kinetic scheme of inactivation is proposed based on the data obtained.

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Funding

Thermal inactivation experiments were carried out with the financial support of a grant of the President of the Russian Federation for the state support of young Russian scientists—candidates of sciences and doctors of sciences. The equation for the inactivation scheme was derived and the constants were analyzed as part of the state research program.

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Authors and Affiliations

  1. Department of Chemistry, Moscow State University, 119234, Moscow, Russia

    M. K. Koshkina, E. P. Sergeyev, T. A. Fedorov, M. D. Shelomov, A. A. Pometun, S. S. Savin, V. I. Tishkov & D. L. Atroshenko

  2. Bach Institute of Biochemistry, Federal Research Center “Fundamentals of Biotechnology”, Russian Academy of Sciences, 119071, Moscow, Russia

    A. A. Pometun, V. I. Tishkov & D. L. Atroshenko

Authors
  1. M. K. Koshkina
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  2. E. P. Sergeyev
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  3. T. A. Fedorov
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  4. M. D. Shelomov
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  5. A. A. Pometun
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  6. S. S. Savin
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  7. V. I. Tishkov
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  8. D. L. Atroshenko
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Contributions

All authors contributed equally to the preparation of the publication.

Corresponding authors

Correspondence to V. I. Tishkov or D. L. Atroshenko.

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The authors declare that they have no conflicts of interest.

Additional information

Translated by V. Mittova

Abbreviations: DAAO, D-amino acid oxidase; OpaDAAOl, amino acid oxidase D from yeast Ogataea parapolymorpha DL-1; FAD, flavinadenindinucleotide.

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Koshkina, M.K., Sergeyev, E.P., Fedorov, T.A. et al. Kinetics of Thermoinactivation of D-Amino Acid Oxidase OPADAAO1 from the Ogataea parapolymorpha DL-1 Yeast. Moscow Univ. Chem. Bull. 78, 69–75 (2023). https://doi.org/10.3103/S0027131423020049

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  • DOI: https://doi.org/10.3103/S0027131423020049

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