Characterization of Aminopeptidase P from the Unicellular Cyanobacterium Synechocystis sp. PCC6803
- Авторы: Baik A.S.1, Mironov K.S.1, Arkhipov D.V.1, Piotrovskii M.S.1, Pojidaeva E.S.1
-
Учреждения:
- Timiryazev Institute of Plant Physiology
- Выпуск: Том 481, № 1 (2018)
- Страницы: 190-194
- Раздел: Biochemistry, Biophysics, and Molecular Biology
- URL: https://journals.rcsi.science/1607-6729/article/view/212345
- DOI: https://doi.org/10.1134/S1607672918040038
- ID: 212345
Цитировать
Аннотация
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.
Об авторах
A. Baik
Timiryazev Institute of Plant Physiology
Автор, ответственный за переписку.
Email: a_baik@mail.ru
Россия, Moscow, 127276
K. Mironov
Timiryazev Institute of Plant Physiology
Email: a_baik@mail.ru
Россия, Moscow, 127276
D. Arkhipov
Timiryazev Institute of Plant Physiology
Email: a_baik@mail.ru
Россия, Moscow, 127276
M. Piotrovskii
Timiryazev Institute of Plant Physiology
Email: a_baik@mail.ru
Россия, Moscow, 127276
E. Pojidaeva
Timiryazev Institute of Plant Physiology
Email: a_baik@mail.ru
Россия, Moscow, 127276
Дополнительные файлы
