2. Academic Validation
  3. Characterization of Aminopeptidase P from the Unicellular Cyanobacterium Synechocystis sp. PCC6803

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

  • Dokl Biochem Biophys. 2018 Jul;481(1):190-194. doi: 10.1134/S1607672918040038.
A S Baik 1,  K S Mironov 2,  D V Arkhipov 2,  M S Piotrovskii 2,  E S Pojidaeva 2
Affiliations

Affiliations

  • 1 Timiryazev Institute of Plant Physiology, Russian Academy of Sciences, Moscow, 127276, Russia. [email protected].
  • 2 Timiryazev Institute of Plant Physiology, Russian Academy of Sciences, Moscow, 127276, Russia.
PMID: 30168056 DOI: 10.1134/S1607672918040038
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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