The genes trpE and trpG of the hyperthermophilic archaeon Sulfolobus solfataricus, encoding the components I and II of anthranilate synthase, were cloned and co-expressed in Escherichia coli. The properties of the recombinant protein were determined and compared to those of the wild type complex. Gel filtration chromatography revealed an alpha(2) beta(2) composition. The heteromeric enzyme is fully active above 85 degrees C and can be considered to be an ''extremozyme'' according to Adams et al.[1]. Sulfolobus solfataricus anthranilate 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. (C) 1997 Academic Press
Expression of Sulfolobus solfataricus trpE and trpG genes in E-coli / Tutino, M.L., A., T., G., M., Sannia, G.. - In: BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS. - ISSN 0006-291X. - STAMPA. - 230:2(1997), pp. 306-310. [10.1006/bbrc.1996.5951]
Expression of Sulfolobus solfataricus trpE and trpG genes in E-coli
TUTINO, MARIA LUISA;SANNIA, GIOVANNI
1997
Abstract
The genes trpE and trpG of the hyperthermophilic archaeon Sulfolobus solfataricus, encoding the components I and II of anthranilate synthase, were cloned and co-expressed in Escherichia coli. The properties of the recombinant protein were determined and compared to those of the wild type complex. Gel filtration chromatography revealed an alpha(2) beta(2) composition. The heteromeric enzyme is fully active above 85 degrees C and can be considered to be an ''extremozyme'' according to Adams et al.[1]. Sulfolobus solfataricus anthranilate 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. (C) 1997 Academic PressI documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
