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Gene Review

purF  -  amidophosphoribosyltransferase

Escherichia coli str. K-12 substr. MG1655

Synonyms: ECK2306, JW2309, ade, purC
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Disease relevance of purF


High impact information on purF


Chemical compound and disease context of purF


Biological context of purF


Associations of purF with chemical compounds

  • Mutations in apbC block function of the APB pathway since they prevent growth of a purF mutant in the absence of thiamine [11].
  • The Cys-His-Asp catalytic triad is implicated in the glutamine amide transfer function of purF-type amidotransferases [12].
  • Apparent dissociation constants of 3.4 nM were determined for binding of holorepressor to purF operator and of 1.7 and 7.1 microM were determined for aporepressor interaction with guanine and hypoxanthine, respectively [13].
  • Enzyme specific activity, immunological reactivity, in vitro lability to O2, Fe-S content, and NH2-terminal processing were virtually identical with amidophosphoribosyltransferase purified from B. subtilis [2].
  • The NH2-terminal cysteine of amidophosphoribosyltransferase was determined to be the residue alkylated by [6-14C]DON [8].

Other interactions of purF


  1. The hisT-purF region of the Escherichia coli K-12 chromosome. Identification of additional genes of the hisT and purF operons. Nonet, M.L., Marvel, C.C., Tolan, D.R. J. Biol. Chem. (1987) [Pubmed]
  2. Cloning of the Bacillus subtilis glutamine phosphoribosylpyrophosphate amidotransferase gene in Escherichia coli. Nucleotide sequence determination and properties of the plasmid-encoded enzyme. Makaroff, C.A., Zalkin, H., Switzer, R.L., Vollmer, S.J. J. Biol. Chem. (1983) [Pubmed]
  3. Arginine 30 and asparagine 74 have functional roles in the glutamine dependent activities of Escherichia coli asparagine synthetase B. Boehlein, S.K., Richards, N.G., Walworth, E.S., Schuster, S.M. J. Biol. Chem. (1994) [Pubmed]
  4. Nucleotide sequence of Escherichia coli asnB and deduced amino acid sequence of asparagine synthetase B. Scofield, M.A., Lewis, W.S., Schuster, S.M. J. Biol. Chem. (1990) [Pubmed]
  5. Interaction of a putative repressor protein with an extended control region of the Bacillus subtilis pur operon. Ebbole, D.J., Zalkin, H. J. Biol. Chem. (1989) [Pubmed]
  6. Regulation of Escherichia coli purF. Mutations that define the promoter, operator, and purine repressor gene. Rolfes, R.J., Zalkin, H. J. Biol. Chem. (1988) [Pubmed]
  7. Nucleotide sequence of Escherichia coli purF and deduced amino acid sequence of glutamine phosphoribosylpyrophosphate amidotransferase. Tso, J.Y., Zalkin, H., van Cleemput, M., Yanofsky, C., Smith, J.M. J. Biol. Chem. (1982) [Pubmed]
  8. Glutamine phosphoribosylpyrophosphate amidotransferase from cloned Escherichia coli purF. NH2-terminal amino acid sequence, identification of the glutamine site, and trace metal analysis. Tso, J.Y., Hermodson, M.A., Zalkin, H. J. Biol. Chem. (1982) [Pubmed]
  9. Amino-terminal deletions define a glutamine amide transfer domain in glutamine phosphoribosylpyrophosphate amidotransferase and other PurF-type amidotransferases. Mei, B.G., Zalkin, H. J. Bacteriol. (1990) [Pubmed]
  10. Structure, function, and regulation of amidophosphoribosyltransferase from prokaryotes. Zalkin, H. Adv. Enzyme Regul. (1983) [Pubmed]
  11. Mutations in apbC (mrp) prevent function of the alternative pyrimidine biosynthetic pathway in Salmonella typhimurium. Petersen, L., Downs, D.M. J. Bacteriol. (1996) [Pubmed]
  12. A cysteine-histidine-aspartate catalytic triad is involved in glutamine amide transfer function in purF-type glutamine amidotransferases. Mei, B., Zalkin, H. J. Biol. Chem. (1989) [Pubmed]
  13. Purification of the Escherichia coli purine regulon repressor and identification of corepressors. Rolfes, R.J., Zalkin, H. J. Bacteriol. (1990) [Pubmed]
  14. Genes of the Escherichia coli pur regulon are negatively controlled by a repressor-operator interaction. He, B., Shiau, A., Choi, K.Y., Zalkin, H., Smith, J.M. J. Bacteriol. (1990) [Pubmed]
  15. Primary structure of the Escherichia coli folC gene and its folylpolyglutamate synthetase-dihydrofolate synthetase product and regulation of expression by an upstream gene. Bognar, A.L., Osborne, C., Shane, B. J. Biol. Chem. (1987) [Pubmed]
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