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

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 Mn 2+ -dependent Xaa-Pro -specific aminopeptidase. The protein in the reaction...

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Bibliographic Details
Published in:Doklady. Biochemistry and biophysics 2018-07, Vol.481 (1), p.190-194
Main Authors: Baik, A. S., Mironov, K. S., Arkhipov, D. V., Piotrovskii, M. S., Pojidaeva, E. S.
Format: Article
Language:English
Subjects:
Aminopeptidase
Aminopeptidases - chemistry
Aminopeptidases - metabolism
Biochemistry
Biological and Medical Physics
Biomedical and Life Sciences
Biophysics
Hydrolysis
Kinetics
Life Sciences
Metals - pharmacology
Models, Molecular
Molecular Biology
Protein Conformation
Proteins
Substrate Specificity
Synechocystis
Synechocystis - enzymology
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Summary: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 Mn 2+ -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.
ISSN:1607-6729
1608-3091
DOI:10.1134/S1607672918040038