Enzymatic properties of chorismate synthase isozymes of tomato (Lycopersicon esculentum Mill.) View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1996-09

AUTHORS

Martin Braun, John M. Henstrand, Jörn Görlach, Nikolaus Amrhein, Jürg Schmid

ABSTRACT

Three plastidic chorismate synthase isozymes (CS1, CS2 and CS2Δ) of tomato were identified by isolation of the corresponding cDNAs. These three cDNAs are derived from only two genes (LeCS1 and LeCS2). This additional complexity results from differential splicing of the primary transcript of one of the genes (LeCS2) giving rise to two different transcripts (CS2 and CS2Δ transcripts). All three isozymes were individually expressed in Escherichia coli both as precursor proteins with N-terminal transit peptides and as mature proteins. Only the mature but not the precursor isozymes CS1 and CS2 were enzymatically active. The enzyme CS2Δ was unstable in E. coli. Both CS1 and CS2 were purified to near homogeneity and their enzymatic properties were analyzed. They differ substantially in their Km values for the substrate 5-enol-pyruvylshikimate 3-phosphate (11 and 80 μM for the mature forms of CS1 and CS2, respectively). The two isozymes appear to be active only as oligomers, and the potential physiological implications of this result are discussed. More... »

PAGES

64-70

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/bf00196650

DOI

http://dx.doi.org/10.1007/bf00196650

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1020116528

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/8987618


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