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J. Biol. Chem., Vol. 261, Issue 15, 6765-6771, May, 1986
B Hove-Jensen, KW Harlow, CJ King and RL Switzer
Phosphoribosylpyrophosphate (P-Rib-PP) synthetase of Escherichia coli 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 phosphate for activity and for
stability. Magnesium ions were required both as a complex with the
substrate ATP and as a free cation. P-Rib-PP synthetase activity was
inhibited strongly by ADP. Kinetic analysis indicated multiple sites of
action of ADP. In addition apparent substrate inhibition was exerted by
ribose 5-phosphate in the presence of ADP. The nucleotide sequence of the
E. coli prs gene has been determined and the coding segment established.
The deduced amino acid sequence of P-Rib-PP synthetase contained 314 amino
acid 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 nucleotides downstream from the
UAA translation stop codon, within a Thy-rich region following an inverted
repeat sequence, indicative of an rho-independent transcription terminator.
Phosphoribosylpyrophosphate synthetase of Escherichia coli. Properties of the purified enzyme and primary structure of the prs gene
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