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单细胞蓝藻聚球藻属6803菌株中氨肽酶P的特性研究

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

作者信息

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

机构信息

Timiryazev Institute of Plant Physiology, Russian Academy of Sciences, Moscow, 127276, Russia.

出版信息

Dokl Biochem Biophys. 2018 Jul;481(1):190-194. doi: 10.1134/S1607672918040038. Epub 2018 Aug 31.

DOI:10.1134/S1607672918040038
PMID:30168056
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 Mn-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.

摘要

PepP蛋白已在体外得到纯化并首次进行了特性鉴定。它由单细胞蓝藻集胞藻PCC6803的sll0136基因编码。现已确定PepP蛋白是一种依赖锰的Xaa-Pro特异性氨肽酶。该蛋白在水解荧光肽Lys(N-Abz)-Pro-Pro-pNA的反应中,于pH 7.6和32°C时具有最大活性。

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本文引用的文献

1
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Biochem J. 2016 Oct 1;473(19):3189-204. doi: 10.1042/BCJ20160550. Epub 2016 Jul 26.
2
INTERMEDIATE CLEAVAGE PEPTIDASE55 Modifies Enzyme Amino Termini and Alters Protein Stability in Arabidopsis Mitochondria.中间切割肽酶55修饰酶的氨基末端并改变拟南芥线粒体中的蛋白质稳定性。
Plant Physiol. 2015 Jun;168(2):415-27. doi: 10.1104/pp.15.00300. Epub 2015 Apr 10.
3
Identification of cleavage sites and substrate proteins for two mitochondrial intermediate peptidases in Arabidopsis thaliana.
拟南芥中两种线粒体中间肽酶的切割位点和底物蛋白的鉴定
J Exp Bot. 2015 May;66(9):2691-708. doi: 10.1093/jxb/erv064. Epub 2015 Mar 1.
4
Cloning, expression, and characterization of aminopeptidase P from the hyperthermophilic archaeon Thermococcus sp. strain NA1.嗜热古菌嗜热栖热菌NA1菌株氨肽酶P的克隆、表达及特性分析
Appl Environ Microbiol. 2006 Mar;72(3):1886-90. doi: 10.1128/AEM.72.3.1886-1890.2006.
5
A continuous fluorimetric assay for aminopeptidase P detailed analysis of product inhibition.
Anal Biochem. 2003 Nov 1;322(1):60-7. doi: 10.1016/S0003-2697(03)00464-0.
6
The gene complement for proteolysis in the cyanobacterium Synechocystis sp. PCC 6803 and Arabidopsis thaliana chloroplasts.集胞藻6803和拟南芥叶绿体中蛋白水解的基因互补情况。
Curr Genet. 2002 Aug;41(5):291-310. doi: 10.1007/s00294-002-0309-8. Epub 2002 Jul 18.
7
Cloning, expression, and characterization of tomato (Lycopersicon esculentum) aminopeptidase P.番茄(Lycopersicon esculentum)氨肽酶P的克隆、表达及特性分析
J Biol Chem. 2001 Aug 24;276(34):31732-7. doi: 10.1074/jbc.M103179200. Epub 2001 Jun 22.
8
Structure and mechanism of a proline-specific aminopeptidase from Escherichia coli.来自大肠杆菌的脯氨酸特异性氨肽酶的结构与机制
Proc Natl Acad Sci U S A. 1998 Mar 31;95(7):3472-7. doi: 10.1073/pnas.95.7.3472.
9
Proline specific peptidases.脯氨酸特异性肽酶
Biochim Biophys Acta. 1997 Dec 5;1343(2):160-86. doi: 10.1016/s0167-4838(97)00134-9.
10
Inhibition and metal ion activation of pig kidney aminopeptidase P. Dependence on nature of substrate.猪肾氨肽酶P的抑制作用和金属离子激活。对底物性质的依赖性。
Biochem Pharmacol. 1996 Jul 26;52(2):229-36. doi: 10.1016/0006-2952(96)00180-3.