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Updated: Feb 5, 2026

Spectrophotometric Determination of Phycobiliprotein Content in Cyanobacterium Synechocystis
Published on: September 11, 2018
Characterization of Aminopeptidase P from the Unicellular Cyanobacterium Synechocystis sp. PCC6803
A S Baik1, K S Mironov2, D V Arkhipov2
1Timiryazev Institute of Plant Physiology, Russian Academy of Sciences, Moscow, 127276, Russia. a_baik@mail.ru.
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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