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Characterization of a prolyl endopeptidase from spinach thylakoids
Author(s) -
Kuwabara Tomohiko
Publication year - 1992
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(92)80179-k
Subject(s) - proteolysis , protease , diisopropyl fluorophosphate , photosystem ii , biochemistry , spinach , chemistry , enzyme , prolyl endopeptidase , endopeptidase , substrate (aquarium) , photosystem i , biology , photosynthesis , ecology
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 CuCl 2 , 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.