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A functional tomato ACC synthase expressed in Escherichia coli demonstrates suicidal inactivation by its substrate S ‐adenosylmethionine
Author(s) -
Li Ning,
Wiesman Zeev,
Liu Derong,
Mattoo Autar K.
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)80978-p
Subject(s) - escherichia coli , atp synthase , substrate (aquarium) , chemistry , biology , biochemistry , enzyme , gene , ecology
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.