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

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

doi:10.1134/S1607672918040038

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

Autores: Baik A.S.¹, Mironov K.S.¹, Arkhipov D.V.¹, Piotrovskii M.S.¹, Pojidaeva E.S.¹
Afiliações:
1. Timiryazev Institute of Plant Physiology
Edição: Volume 481, Nº 1 (2018)
Páginas: 190-194
Seção: Biochemistry, Biophysics, and Molecular Biology
URL: https://journals.rcsi.science/1607-6729/article/view/212345
DOI: https://doi.org/10.1134/S1607672918040038
ID: 212345

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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.