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Structure of the allosteric regulatory enzyme of purine biosynthesis.
Multi-wavelength anomalous diffraction (MAD) has been used to determine the structure of the regulatory enzyme of de novo synthesis of purine nucleotides, glutamine 5-phosphoribosyl-1-pyrophosphate…
Regulation of Pyrimidine Biosynthetic Gene Expression in Bacteria: Repression without Repressors
SUMMARY DNA-binding repressor proteins that govern transcription initiation in response to end products generally regulate bacterial biosynthetic genes, but this is rarely true for the pyrimidine…
Purification and properties of phosphoribosyl-diphosphate synthetase from Bacillus subtilis.
- K. Arnvig, B. Hove-Jensen, R. Switzer
- Biology, ChemistryEuropean journal of biochemistry
- 1 August 1990
Of several end products tested, only ADP was strongly inhibitory; GDP was a weak inhibitor; these observations strongly suggest a specific allosteric site for ADP binding.
Phosphoribosylpyrophosphate synthetase of Escherichia coli. Properties of the purified enzyme and primary structure of the prs gene.
Regulation of the Bacillus subtilis pyrimidine biosynthetic (pyr) gene cluster by an autogenous transcriptional attenuation mechanism
Northern (RNA) blot analysis has identified transcripts of lengths which coincide with termination at these proposed attenuation sites and whose relative abundances vary in the expected pyrimidine-dependent manner.
The genetic and functional basis of purine nucleotide feedback-resistant phosphoribosylpyrophosphate synthetase superactivity.
- M. Becker, P. Smith, W. Taylor, R. Mustafi, R. Switzer
- BiologyThe Journal of clinical investigation
- 1 November 1995
Kinetic analysis of recombinant mutant PRS1s showed that widely dispersed point mutations in the X chromosome-linked PRPS1 gene encoding thePRS1 isoform result in alteration of the allosteric mechanisms regulating both enzyme inhibition by purine nucleotides and activation by inorganic phosphate.
Phosphoribosyl Diphosphate (PRPP): Biosynthesis, Enzymology, Utilization, and Metabolic Significance
- B. Hove-Jensen, K. Andersen, M. Kilstrup, J. Martinussen, R. Switzer, M. Willemoës
- Biology, ChemistryMicrobiology and Molecular Biology Reviews
- 28 December 2016
The results of these analyses are unified with recent progress in molecular enzymology and the elucidation of the three-dimensional structures of PRPP synthases from eubacteria, archaea, and humans.
Molecular recognition of pyr mRNA by the Bacillus subtilis attenuation regulatory protein PyrR.
- E. R. Bonner, J. D'Elia, B. Billips, R. Switzer
- Biology, ChemistryNucleic acids research
- 1 December 2001
The pyrimidine nucleotide biosynthesis (pyr) operon in Bacillus subtilis is regulated by transcriptional attenuation, and PyrR likely recognizes conserved RNA sequences, but only if they are properly positioned in the correct secondary structure.
Purification and Characterization of Bacillus subtilis PyrR, a Bifunctional pyr mRNA-binding Attenuation Protein/Uracil Phosphoribosyltransferase*
- R. Turner, E. R. Bonner, G. K. Grabner, R. Switzer
- Biology, ChemistryThe Journal of Biological Chemistry
- 6 March 1998
The results support a model for the regulation of Pyr transcription whereby termination is governed by the UMP-dependent binding of PyrR to pyr RNA and provide purified and characterized PyrR for detailed biochemical studies of RNA binding and transcriptional attenuation.
Aspartokinase III, a new isozyme in Bacillus subtilis 168
A previously undetected Bacillus subtilis aspartokinase isozyme has been characterized and it was found to be synergistically inhibited by lysine and threonine, and declined rapidly in B. subtilIS cells that were starved for glucose.