CHARACTERIZATION OF A PROLYL ENDOPEPTIDASE FROM SPINACH THYLAKOIDS

被引：33

作者：

KUWABARA, T

机构：

[1] Institute of Biological Sciences, University of Tsukuba, Tsukuba, Ibaraki

来源：

FEBS LETTERS | 1992年 / 300卷 / 02期

关键词：

PROLYL ENDOPEPTIDASE; PHOTOSYSTEM II MEMBRANE; MEMBRANE-BOUND PROTEASE; DESTRUCTIVE PROCESSING; CHLOROPLAST PROTEASE; SPINACH;

D O I：

10.1016/0014-5793(92)80179-K

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：

A prolyl endopeptidase (PEPase, EC 3.4.21.26) that specifically cleaves the 18-kDa protein of photosystem II was extracted from photosystem II membranes with 1 M NaCl. Proteolytic activity measured with artificial substrates was less than a quarter of that with the protein. Studies on inhibition of the proteolysis by an artificial substrate suggested that the protease recognizes the scissile prolyl bond. The protease was inhibited by CuCl2, but not by diisopropyl fluorophosphate or p-chloromercuriphenylsulfonic acid. These findings suggest that the protease represents a new class of PEPase. The specificity of the enzyme is discussed in relation to the structure of the 18-kDa protein.

引用

页码：127 / 130

页数：4

共 22 条

[1] BIOSYNTHESIS OF THE LIGHT-HARVESTING CHLOROPHYLL A-B PROTEIN - POLYPEPTIDE TURNOVER IN DARKNESS [J].