Competitive inhibition analysis of the enzyme‐substrate interaction in the carboxy‐terminal processing of the precursor D1 protein of photosystem II reaction center using substituted oligopeptides

FEBS Letters

Yamamoto, Yumiko¹  Satoh, Kimiyuki¹ 

[1] Department of Biology, Okayama University, Okayama 700-8530, Japan

关键词: C-terminal processing;    Competitive inhibition;    D1 protein;    Photosystem II;    Processing protease;    Synthetic oligopeptide;   

DOI  :  10.1016/S0014-5793(98)00671-1

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

A clear parallelism was demonstrated between the efficiency as substrate of the substituted oligopeptides corresponding to the carboxy-terminal (C-terminal) sequence of the precursor D1 protein (pD1) in the in vitro enzymatic assay and their competitive inhibitory capacity toward the proteolytic C-terminal processing of the full-length pD1 integrated in the intact photosystem II complex embedded in the thylakoid membrane of Scenedesmus obliquus LF-1 mutant, as shown e.g. by the influence of L343A, A345G and A345V substitutions and the effect of C-terminal fragments. This suggests that the basic mechanism for substrate recognition by the processing protease elucidated in the enzymatic analysis using synthetic oligopeptides is also effective in vivo, although it can sometimes be difficult to detect the consequence of amino acid substitution in the integrated systems.

【 授权许可】

Unknown