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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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Functional expression of Arabidopsis thaliana anthranilate synthase subunit I in Escherichia coli.

Anthranilate synthase is involved in tryptophan (Trp) biosynthesis. Functional expression of subunit I from Arabidopsis (ASA1) was achieved in bacteria as a protein fused with glutathione S-transferase ( GST). The active product was purified in a single step on a glutathione-Sepharose column. The Vmax (45 nmol min-1mg-1), the apparent K(M) for chorismate (180 microM), and the feedback inhibition by Trp (complete inhibition by 10 microM Trp) of the purified fusion product ( GST-ASA1) were comparable to anthranilate synthase purified from plants. Polyclonal antibodies raised against the fusion project and purified by affinity chromatography on a GST-ASA1-Sepharose column cross-reacted with a 61.5-kD protein in a partially purified anthranilate synthase preparation from corn seedlings. GST-ASA1 cleavage by thrombin, as well as site-directed mutagenesis modifications of the Trp allosteric site, inactivated the recombinant protein.[1]

References

  1. Functional expression of Arabidopsis thaliana anthranilate synthase subunit I in Escherichia coli. Bernasconi, P., Walters, E.W., Woodworth, A.R., Siehl, D.L., Stone, T.E., Subramanian, M.V. Plant Physiol. (1994) [Pubmed]
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