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Characterization of an Arabidopsis thaliana cDNA encoding an S‐adenosylmethionine‐sensitive threonine synthase Threonine synthase from higher plants
Author(s) -
Curien Gilles,
Dumas Renaud,
Ravanel Stéphane,
Douce Roland
Publication year - 1996
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(96)00633-3
Subject(s) - threonine , atp synthase , biochemistry , arabidopsis thaliana , complementation , complementary dna , biology , protein fragment complementation assay , akt3 , serine , microbiology and biotechnology , enzyme , mutant , gene
An Arabidopsis thaliana cDNA encoding an Sadenosylmethionine‐sensitive threonine synthase (EC 4.2.99.2) has been isolated by functional complementation of an Escherichia coli mutant devoid of threonine synthase activity. Threonine synthase from A. thaliana was shown to be synthesized with a transit peptide. The recombinant protein is activated by Sadenosylmethionine in the same range as the plant threonine synthase and evidence is presented for an involvement of the N‐terminal part of the mature enzyme in the sensitivity to Sadenosylmethionine.