Gene Review:
pyrB - aspartate carbamoyltransferase
Escherichia coli O157:H7 str. Sakai
- Genetic characterization of the folding domains of the catalytic chains in aspartate transcarbamoylase. Jenness, D.D., Schachman, H.K. J. Biol. Chem. (1983)
- 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)
- Cloning, nucleotide sequence and expression of the pyrBI operon of Salmonella typhimurium LT2. Michaels, G., Kelln, R.A., Nargang, F.E. Eur. J. Biochem. (1987)
- Molecular cloning and characterization of the pyrB gene of Lactobacillus leichmannii encoding aspartate transcarbamylase. Becker, J., Brendel, M. Biochimie (1996)
- Molecular structure of Bacillus subtilis aspartate transcarbamoylase at 3.0 A resolution. Stevens, R.C., Reinisch, K.M., Lipscomb, W.N. Proc. Natl. Acad. Sci. U.S.A. (1991)
- The effect of pH on the cooperative behavior of aspartate transcarbamylase from Escherichia coli. Pastra-Landis, S.C., Evans, D.R., Lipscomb, W.N. J. Biol. Chem. (1978)
- Still looking for the Ivory Tower. Schachman, H.K. Annu. Rev. Biochem. (2000)
- Reconstruction of an enzyme by domain substitution effectively switches substrate specificity. Houghton, J.E., O'Donovan, G.A., Wild, J.R. Nature (1989)
- Substitutions in the aspartate transcarbamoylase domain of hamster CAD disrupt oligomeric structure. Qiu, Y., Davidson, J.N. Proc. Natl. Acad. Sci. U.S.A. (2000)
- Binding of bisubstrate analog promotes large structural changes in the unregulated catalytic trimer of aspartate transcarbamoylase: implications for allosteric regulation induced cell migration. Endrizzi, J.A., Beernink, P.T., Alber, T., Schachman, H.K. Proc. Natl. Acad. Sci. U.S.A. (2000)
- Interaction of tetraiodofluorescein with a modified form of aspartate transcarbamylase. Kantrowitz, E.R., Jacobsberg, L.B., Landfear, S.M., Lipscomb, W.N. Proc. Natl. Acad. Sci. U.S.A. (1977)
- Determination of ligand binding: partial and full saturation of aspartate transcarbamylase. Applicability of a filter assay to weakly binding ligands. Suter, P., Rosenbusch, J.P. J. Biol. Chem. (1976)
- Aquifex aeolicus aspartate transcarbamoylase, an enzyme specialized for the efficient utilization of unstable carbamoyl phosphate at elevated temperature. Purcarea, C., Ahuja, A., Lu, T., Kovari, L., Guy, H.I., Evans, D.R. J. Biol. Chem. (2003)
- Superproduction and rapid purification of Escherichia coli aspartate transcarbamylase and its catalytic subunit under extreme derepression of the pyrimidine pathway. Nowlan, S.F., Kantrowitz, E.R. J. Biol. Chem. (1985)
- Assembly of the aspartate transcarbamoylase holoenzyme from transcriptionally independent catalytic and regulatory cistrons. Foltermann, K.F., Shanley, M.S., Wild, J.R. J. Bacteriol. (1984)
- Molecular characterization of pyrimidine biosynthesis genes from the thermophile Bacillus caldolyticus. Ghim, S.Y., Nielsen, P., Neuhard, J. Microbiology (Reading, Engl.) (1994)
- Crystal structure of Pseudomonas aeruginosa catabolic ornithine transcarbamoylase at 3.0-A resolution: a different oligomeric organization in the transcarbamoylase family. Villeret, V., Tricot, C., Stalon, V., Dideberg, O. Proc. Natl. Acad. Sci. U.S.A. (1995)
- Elimination of cooperativity in aspartate transcarbamylase by nitration of a single tyrosine residue. Landfear, S.M., Evans, D.R., Lipscomb, W.N. Proc. Natl. Acad. Sci. U.S.A. (1978)
- Changes in stability and allosteric properties of aspartate transcarbamoylase resulting from amino acid substitutions in the zinc-binding domain of the regulatory chains. Eisenstein, E., Markby, D.W., Schachman, H.K. Proc. Natl. Acad. Sci. U.S.A. (1989)
- Aquifex aeolicus dihydroorotase: association with aspartate transcarbamoylase switches on catalytic activity. Ahuja, A., Purcarea, C., Ebert, R., Sadecki, S., Guy, H.I., Evans, D.R. J. Biol. Chem. (2004)
- Effect of amino acid substitutions on the catalytic and regulatory properties of aspartate transcarbamoylase. Robey, E.A., Wente, S.R., Markby, D.W., Flint, A., Yang, Y.R., Schachman, H.K. Proc. Natl. Acad. Sci. U.S.A. (1986)
- Genes encoding Escherichia coli aspartate transcarbamoylase: the pyrB-pyrI operon. Pauza, C.D., Karels, M.J., Navre, M., Schachman, H.K. Proc. Natl. Acad. Sci. U.S.A. (1982)
- Mercurial-promoted Zn2+ release from Escherichia coli aspartate transcarbamoylase. Hunt, J.B., Neece, S.H., Schachman, H.K., Ginsburg, A. J. Biol. Chem. (1984)
- An aspartate transcarbamylase lacking catalytic subunit interactions. Study of conformational changes by ultraviolet absorbance and circular dichroism spectroscopy. Kerbiriou, D., Hervé, G. J. Biol. Chem. (1977)