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

 
PIIS086956520001207-0-1
DOI10.31857/S086956520001207-0
Publication type Article
Status Published
Authors
Affiliation: K.A. Timiryazev Institute of Plant Physiology of the Russian Academy of Science
Affiliation: K.A. Timiryazev Institute of Plant Physiology of the Russian Academy of Science
Affiliation: K.A. Timiryazev Institute of Plant Physiology of the Russian Academy of Science
Affiliation: K.A. Timiryazev Institute of Plant Physiology of the Russian Academy of Science
Affiliation: K.A. Timiryazev Institute of Plant Physiology of the Russian Academy of Science
Journal nameDoklady Akademii nauk
EditionVolume 481 Issue 2
Pages211-215
Abstract

It is the first time the PepP protein has been purified in vitro and characterized. 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. Its activity optimum in a reaction of hydrolysis of the fluorescent peptide Lys(N-Abz)-Pro-Pro-pNA is at pH 7,6 and at 32°C.

Keywords
Received13.10.2018
Publication date14.10.2018
Number of characters291
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