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

Baik, A S; Mironov, K S; Arkhipov, D V; Piotrovskii, M S; Pojidaeva, E S

Baik, A S; Mironov, K S; Arkhipov, D V; Piotrovskii, M S; Pojidaeva, E S.

Baik AS; Timiryazev Institute of Plant Physiology, Russian Academy of Sciences, Moscow, 127276, Russia. a_baik@mail.ru.
Mironov KS; Timiryazev Institute of Plant Physiology, Russian Academy of Sciences, Moscow, 127276, Russia.
Arkhipov DV; Timiryazev Institute of Plant Physiology, Russian Academy of Sciences, Moscow, 127276, Russia.
Piotrovskii MS; Timiryazev Institute of Plant Physiology, Russian Academy of Sciences, Moscow, 127276, Russia.
Pojidaeva ES; Timiryazev Institute of Plant Physiology, Russian Academy of Sciences, Moscow, 127276, Russia.

Dokl Biochem Biophys ; 481(1): 190-194, 2018 Jul.

Article en En | MEDLINE | ID: mdl-30168056

RESUMEN

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.

Asunto(s)

Aminopeptidasas/química; Aminopeptidasas/metabolismo; Synechocystis/enzimología; Hidrólisis; Cinética; Metales/farmacología; Modelos Moleculares; Conformación Proteica; Especificidad por Sustrato

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Texto completo: 1 Banco de datos: MEDLINE Asunto principal: Synechocystis / Aminopeptidasas Idioma: En Año: 2018 Tipo del documento: Article

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Texto completo: 1 Banco de datos: MEDLINE Asunto principal: Synechocystis / Aminopeptidasas Idioma: En Año: 2018 Tipo del documento: Article