Inhibition by penem of processing peptidases from cyanobacteria and chloroplast thylakoids

被引:11
作者
Barbrook, AC
Packer, JCL
Howe, CJ
机构
[1] UNIV CAMBRIDGE,DEPT BIOCHEM,CAMBRIDGE CB2 1QW,ENGLAND
[2] UNIV CAMBRIDGE,CAMBRIDGE CTR MOL RECOGNIT,CAMBRIDGE CB2 1QW,ENGLAND
基金
英国生物技术与生命科学研究理事会;
关键词
thylakoid processing peptidase; signal peptidase; penem; Phormidium laminosum; Pisum sativum;
D O I
10.1016/S0014-5793(96)01239-2
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
Proteins targeted to the thylakoid lumen of plants and cyanobacteria and the periplasmic space of cyanobacteria are synthesised with N-terminal presequences which are removed following translocation across the membrane, These presequences are thought to direct translocation of the preprotein by a sec-type pathway. Detergent extracts of cyanobacterial and chloroplast membranes contain enzymes which are capable of processing precursors to the mature size. We show that the processing of a range of precursors by both cyanobacterial and chloroplast enzymes is inhibited by the penem SB216357. This is the first report of an inhibitor of these enzymes and indicates that they are type 1 signal peptidases.
引用
收藏
页码:198 / 200
页数:3
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