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

Dokl Biochem Biophys. 2018 Jul;481(1):190-194. doi: 10.1134/S1607672918040038. Epub 2018 Aug 31.

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.

MeSH terms

  • Aminopeptidases / chemistry*
  • Aminopeptidases / metabolism*
  • Hydrolysis
  • Kinetics
  • Metals / pharmacology
  • Models, Molecular
  • Protein Conformation
  • Substrate Specificity
  • Synechocystis / enzymology*

Substances

  • Metals
  • Aminopeptidases
  • X-Pro aminopeptidase