@entity30116 synthetase of XXXX . Properties of the purified enzyme and primary structure of the prs gene.

@entity17457 @entity2036 @entity535 @entity34778 @entity377 @entity855 @entity30116 @entity1391 @entity30975 @entity857 @entity526 @entity1760
@entity30116 ( @entity34778 ) synthetase of @entity526 has been purified to near homogeneity from a strain harboring the prs gene, encoding P-Rib-PP synthetase, on a multicopy plasmid. Analysis of the enzyme showed that it required inorganic @entity1391 for activity and for stability. @entity1760 ions were required both as a complex with the substrate @entity855 and as a free cation. P- @entity30975 -PP synthetase activity was inhibited strongly by @entity857 . Kinetic analysis indicated multiple sites of action of @entity857 . In addition apparent substrate inhibition was exerted by @entity17457 in the presence of @entity857 . The @entity377 sequence of the @entity526 prs gene has been determined and the coding segment established. The deduced @entity535 sequence of P-Rib-PP synthetase contained 314 @entity535 residues and the molecular weight was calculated as 34,060. The initiation site of transcription was determined. This site was preceded by well conserved -10 and -35 consensus sequences (pdT-dA-dG-dA-dA-dT and pdT-dT-dG-dA-dT-dG, respectively). The transcription initiation site preceded the potential translation initiation site by 302 nucleotides. Transcription terminated approximately 35 @entity2036 downstream from the UAA translation stop codon, within a Thy-rich region following an inverted repeat sequence, indicative of an rho-independent transcription terminator.
