Characterization of Aminopeptidase P from the Unicellular Cyanobacterium Synechocystis sp PCC6803

被引：2
|
作者：
Baik, A. S. [1 ]
Mironov, K. S. [1 ]
Arkhipov, D. V. [1 ]
Piotrovskii, M. S. [1 ]
Pojidaeva, E. S. [1 ]
机构：
[1] Russian Acad Sci, Timiryazev Inst Plant Physiol, Moscow 127276, Russia
来源：
DOKLADY BIOCHEMISTRY AND BIOPHYSICS | 2018年 / 481卷 / 01期
基金：
俄罗斯科学基金会; 俄罗斯基础研究基金会;
关键词：
ARABIDOPSIS-THALIANA; ESCHERICHIA-COLI; SUBSTRATE; CLEAVAGE; INHIBITION; PEPTIDASES; EXPRESSION; PROTEINS; CLONING; ENZYME;
D O I：
10.1134/S1607672918040038
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
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 degrees C.
引用
收藏
页码：190 / 194
页数：5
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