Abstract
The genestrpEandtrpGof the hyperthermophilic archaeonSulfolobus solfataricus,encoding the components I and II of anthranilate synthase, were cloned and co-expressed inEscherichia coli.The properties of the recombinant protein were determined and compared to those of the wild type complex. Gel filtration chromatography revealed an α2β2composition. The heteromeric enzyme is fully active above 85°C and can be considered to be an “extremozyme” according to Adamset al.[1].Sulfolobus solfataricusanthranilate synthase is subject to feedback inhibition by L-tryptophan even if it lacks the co-operativity that has been observed for all the other tetrameric anthranilate synthases.
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