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Gene Review

pyrC  -  dihydro-orotase

Escherichia coli str. K-12 substr. MG1655

Synonyms: ECK1047, JW1049
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Disease relevance of pyrC


High impact information on pyrC


Chemical compound and disease context of pyrC


Biological context of pyrC

  • An open reading frame encoding a 348-amino acid polypeptide (Mr = 38,827) was identified as the pyrC structural gene by comparing the amino acid composition predicted from the DNA sequence with that previously determined for the dihydroorotase subunit [1].
  • Transcriptional initiation was shown to occur within a region located 36 to 39 base pairs upstream of the pyrC structural gene [1].
  • Nuclease Bal31-deletion derivatives of pyrC plasmids indicate that this gene does not affect the expression of pyrC [10].
  • Mutational analysis of this regulatory region showed that the formation of a hairpin at the 5' end of the pyrC transcript, which overlaps the pyrC ribosome binding site, is required for repression of pyrC expression [11].
  • To define the mechanism of this regulation, an essential regulatory region between the pyrC promoter and the initial codons of the pyrC structural gene was identified [11].

Associations of pyrC with chemical compounds


Other interactions of pyrC


Analytical, diagnostic and therapeutic context of pyrC


  1. Nucleotide sequence and expression of the pyrC gene of Escherichia coli K-12. Wilson, H.R., Chan, P.T., Turnbough, C.L. J. Bacteriol. (1987) [Pubmed]
  2. Cloning, sequencing, and characterizing the Lactobacillus leichmannii pyrC gene encoding dihydroorotase. Schenk-Gröninger, R., Becker, J., Brendel, M. Biochimie (1995) [Pubmed]
  3. Structure and expression of a pyrimidine gene cluster from the extreme thermophile Thermus strain ZO5. Van de Casteele, M., Chen, P., Roovers, M., Legrain, C., Glansdorff, N. J. Bacteriol. (1997) [Pubmed]
  4. Aspartate transcarbamoylase genes of Pseudomonas putida: requirement for an inactive dihydroorotase for assembly into the dodecameric holoenzyme. Schurr, M.J., Vickrey, J.F., Kumar, A.P., Campbell, A.L., Cunin, R., Benjamin, R.C., Shanley, M.S., O'Donovan, G.A. J. Bacteriol. (1995) [Pubmed]
  5. Mammalian dihydroorotase: nucleotide sequence, peptide sequences, and evolution of the dihydroorotase domain of the multifunctional protein CAD. Simmer, J.P., Kelly, R.E., Rinker, A.G., Zimmermann, B.H., Scully, J.L., Kim, H., Evans, D.R. Proc. Natl. Acad. Sci. U.S.A. (1990) [Pubmed]
  6. Mass spectrometric determination of the cleavage sites in Escherichia coli dihydroorotase induced by a cysteine-specific reagent. Daniel, R., Caminade, E., Martel, A., Le Goffic, F., Canosa, D., Carrascal, M., Abian, J. J. Biol. Chem. (1997) [Pubmed]
  7. Cloning and expression of the mammalian multifunctional protein CAD in Escherichia coli. Characterization of the recombinant protein and a deletion mutant lacking the major interdomain linker. Guy, H.I., Evans, D.R. J. Biol. Chem. (1994) [Pubmed]
  8. Dihydroorotase from Escherichia coli. Substitution of Co(II) for the active site Zn(II). Brown, D.C., Collins, K.D. J. Biol. Chem. (1991) [Pubmed]
  9. Dihydroorotase from Escherichia coli: loop movement and cooperativity between subunits. Lee, M., Chan, C.W., Mitchell Guss, J., Christopherson, R.I., Maher, M.J. J. Mol. Biol. (2005) [Pubmed]
  10. Nucleotide sequence of the structural gene for dihydroorotase of Escherichia coli K12. Bäckström, D., Sjöberg, R.M., Lundberg, L.G. Eur. J. Biochem. (1986) [Pubmed]
  11. Translational control of pyrC expression mediated by nucleotide-sensitive selection of transcriptional start sites in Escherichia coli. Wilson, H.R., Archer, C.D., Liu, J.K., Turnbough, C.L. J. Bacteriol. (1992) [Pubmed]
  12. Molecular structure of dihydroorotase: a paradigm for catalysis through the use of a binuclear metal center. Thoden, J.B., Phillips, G.N., Neal, T.M., Raushel, F.M., Holden, H.M. Biochemistry (2001) [Pubmed]
  13. Function of conserved histidine residues in mammalian dihydroorotase. Zimmermann, B.H., Kemling, N.M., Evans, D.R. Biochemistry (1995) [Pubmed]
  14. Synthesis and enzymic evaluation of 4-mercapto-6-oxo-1, 4-azaphosphinane-2-carboxylic acid 4-oxide as an inhibitor of mammalian dihydroorotase. Manthey, M.K., Huang, D.T., Bubb, W.A., Christopherson, R.I. J. Med. Chem. (1998) [Pubmed]
  15. Functional expression and characterization of the two cyclic amidohydrolase enzymes, allantoinase and a novel phenylhydantoinase, from Escherichia coli. Kim, G.J., Lee, D.E., Kim, H.S. J. Bacteriol. (2000) [Pubmed]
  16. Crystallization of hamster dihydroorotase: involvement of a disulfide-linked tetrameric form. Maher, M.J., Huang, D.T., Guss, J.M., Collyer, C.A., Christopherson, R.I. Acta Crystallogr. D Biol. Crystallogr. (2003) [Pubmed]
  17. Assay of Escherichia coli dihydroorotase with enantiomeric substrate: practical preparation of carbamyl L-aspartate and high-performance liquid chromatography analysis of catalysis product. Daniel, R., Kokel, B., Caminade, E., Martel, A., Le Goffic, F. Anal. Biochem. (1996) [Pubmed]
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