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Characterization of Aminopeptidase P from the Unicellular Cyanobacterium Synechocystis sp. PCC6803

  • Biochemistry, Biophysics, and Molecular Biology
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Abstract

The PepP protein has been purified in vitro and characterized for the first time. It is encoded by the sll0136 gene of the unicellular cyanobacterium Synechocystis sp. PCC6803. It is established that the PepP protein is a Mn2+-dependent Xaa-Pro-specific aminopeptidase. The protein in the reaction of hydrolysis of the fluorescent peptide Lys(N-Abz)-Pro-Pro-pNA has a maximal activity at pH 7.6 and 32°C.

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Authors and Affiliations

  1. Timiryazev Institute of Plant Physiology, Russian Academy of Sciences, Moscow, 127276, Russia

    A. S. Baik, K. S. Mironov, D. V. Arkhipov, M. S. Piotrovskii & E. S. Pojidaeva

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  1. A. S. Baik
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  2. K. S. Mironov
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  3. D. V. Arkhipov
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  4. M. S. Piotrovskii
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  5. E. S. Pojidaeva
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Correspondence to A. S. Baik.

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Original Russian Text © A.S. Baik, K.S. Mironov, D.V. Arkhipov, M.S. Piotrovskii, E.S. Pojidaeva, 2018, published in Doklady Akademii Nauk, 2018, Vol. 481, No. 2.

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Baik, A.S., Mironov, K.S., Arkhipov, D.V. et al. Characterization of Aminopeptidase P from the Unicellular Cyanobacterium Synechocystis sp. PCC6803. Dokl Biochem Biophys 481, 190–194 (2018). https://doi.org/10.1134/S1607672918040038

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  • DOI: https://doi.org/10.1134/S1607672918040038

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