A functional tomato ACC synthase expressed in Escherichia coli demonstrates suicidal inactivation by its substrate S‐adenosylmethionine

FEBS Letters

Li, Ning¹  Liu, Derong¹  Mattoo, Autar K.¹  Wiesman, Zeev¹ 

[1] Plant Molecular Biology Laboratory, Building 006, United States Department of Agriculture/Agricultural Research Service, Beltsville, Agricultural Research Center (W), Beltsville, MD 20705-2350, USA

关键词: ACC synthase;    Gene expression;    Lycopersicon esculentum;    Enzyme inactivation;    ACC;    1-aminocyclopropane-1-carboxylic acid;    EPPS;    N-(2-hydroxyethyl)piperazine-N′-3-propanesulfonic acid;    PCR;    polymerase chain reaction;    PLP;    pyridoxal-5′-phosphate;    SAM;    S-adenosylmethionine;    SDS-PAGE;    sodium dodecyl sulfate-polyacrylamide gel electrophoresis;   

DOI  :  10.1016/0014-5793(92)80978-P

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

1-Aminocyclopropane-1-carboxylate (ACC) synthase is a key enzyme in the biosynthesis of the plant hormone, ethylene. We have isolated, sequenced and expressed a functional tomato (cy Pik-Red) ACC synthase gene in Escherichia coli. ACC synthase expressed in E. coli was inactivated by incubation with S-adenosylmethionine (SAM), the half—time of which was concentration dependent. Mixing the tomato fruit protein extract with the cell-free extract from transformed E. coli did not affect SAM-dependent inactivation of ACC synthase activity. Thus, single isoforms of the ACC synthase enzyme, which demonstrate the biochemical features expected of the tomato fruit enzyme, can be expressed in E. coli and their structure—function relationships investigated.

【 授权许可】

Unknown