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Aspartate carbamoyltransferase

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Springer Handbook of Enzymes

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References

  1. Sheperdson, M.; Pardee, A.B.: Production and crystallization of aspartate transcarbamylase. J. Biol. Chem., 235, 3233–3237 (1960)

    Google Scholar 

  2. Lowenstein, J.M.; Cohen, P.P.: Studies on the biosynthesis of carbamylaspartic acid. J. Biol. Chem., 220, 57–70 (1956)

    PubMed  CAS  Google Scholar 

  3. Jacobson, G.R.; Stark, G.R.: Aspartate transcarbamylases. The Enzymes, 3rd Ed. (Boyer, P.D., ed.), 9, 225–308 (1973)

    Google Scholar 

  4. Allewell, N.M.: Escherichia coli aspartate transcarbamoylase: structure, energetics, and catalytic and regulatory mechanisms. Annu. Rev. Biophys. Biophys. Chem., 18, 71–92 (1989)

    Article  PubMed  CAS  Google Scholar 

  5. Kantrowitz, E.R.; Lipscomb, W.N.: Escherichia coli aspartate transcarbamoylase: the molecular basis for a concerted allosteric transition. Trends Biochem. Sci., 15, 53–59 (1990)

    Article  PubMed  CAS  Google Scholar 

  6. England, P.; Herve, G.: Synergistic inhibition of Escherichia coli aspartate transcarbamylase by CTP and UTP: binding studies using continuous-flow dialysis. Biochemistry, 31, 9725–9732 (1992)

    Article  PubMed  CAS  Google Scholar 

  7. Mort, J.S.; Chan, W.W.C.: Subunit interactions in aspartate transcarbamylase. Characterization of a complex between the catalytic and the regulatory subunits. J. Biol. Chem., 250, 653–660 (1975)

    PubMed  CAS  Google Scholar 

  8. Zhang, Y.; Kantrowitz, E.R.: The synergistic inhibition of Escherichia coli aspartate carbamoyltransferase by UTP in the presence of CTP is due to the binding of UTP to the low affinity CTP sites. J. Biol. Chem., 266, 22154–22158 (1991)

    PubMed  CAS  Google Scholar 

  9. Laing, N.; Chan, W.W.C.; Hutchinson, D.W.; Íberg, B.: Phosphorus-containing inhibitors of aspartate transcarbamoylase from Escherichia coli. FEBS Lett., 260, 206–208 (1990)

    Article  PubMed  CAS  Google Scholar 

  10. Nowlan, S.C.; Kantrowitz, E.R.: Superproduction and rapid purification of Escherichia coli aspartate transcarbamylase and its catalytic subunit under extreme derepression of the pyrimidine pathway. J. Biol. Chem., 260, 14712–14716 (1985)

    PubMed  CAS  Google Scholar 

  11. Swyryd, E.A.; Seaver, S.S.; Stark, G.R.: N-(phosphonacetyl)-L-aspartate, a potent transition state analog inhibitor of aspartate transcarbamylase, blocks proliferation of mammalian cells in culture. J. Biol. Chem., 249, 6945–6950 (1974)

    PubMed  CAS  Google Scholar 

  12. Enns, C.A.; Chan, W.W.C.: Chemical stabilization of conformational states of aspartate transcarbamoylase. Methods Enzymol., 135, 569–577 (1987)

    PubMed  CAS  Google Scholar 

  13. Yon, R.J.: Wheat-germ aspartate transcarbamoylase: potentiation of end-product inhibition in vitro by deoxycholate. Biochem. Soc. Trans., 1, 676–678 (1973)

    CAS  Google Scholar 

  14. Rao, G.S.J.; Savithri, H.S.; Seethalakshmi, S.; Rao, N.A.: Plant aspartate transcarbamylase: an affinity chromatographic method for the purification of the enzyme from germinated seedings. Anal. Biochem., 95, 401–405 (1979)

    Article  CAS  Google Scholar 

  15. Brabson, J.S.; Switzer, R.L.: Purification and properties of Bacillus subtilis aspartate transcarbamylase. J. Biol. Chem., 250, 8664–8669 (1975)

    PubMed  CAS  Google Scholar 

  16. Yon, R.J.: Versatility of mixed-function adsorbents in biospecific protein desorption: accidental affinity and an improved purification of aspartate transcarbamoylase from wheat germ. Anal. Biochem., 113, 219–228 (1981)

    Article  PubMed  CAS  Google Scholar 

  17. Grayson, J.E.; Yon, R.J.; Butterworth, P.J.: Wheat-germ aspartate transcarbamoylase. Purification and cold-lability. Biochem. J., 183, 239–245 (1979)

    PubMed  CAS  Google Scholar 

  18. Grayson, D.R.; Evans, D.R.: The isolation and characterization of the aspartate transcarbamylase domain of the multifunctional protein, CAD. J. Biol. Chem., 258, 4123–4129 (1983)

    PubMed  CAS  Google Scholar 

  19. Jacobson, G.R.; Stark, G.R.: Aspartate transcarbamylase of Escherichia coli. Mechanisms of inhibition and activation by dicarboxylic acids and other anions. J. Biol. Chem., 250, 6852–6860 (1975)

    PubMed  CAS  Google Scholar 

  20. Mathieu, M.: Partial characterization of aspartate transcarbamylase from the mantle of the mussel Mytilus edulis. Comp. Biochem. Physiol. B Comp. Biochem., 82, 667–674 (1985)

    Article  CAS  Google Scholar 

  21. Prasad, P.V.; Rao, N.A.: Purification and regulation of aspartate transcarba-mylase from germinated mung bean (Vigna radiata) seedlings. J. Biosci., 6, 233–248 (1984)

    Article  CAS  Google Scholar 

  22. Savithri, H.S.; Vaidyanathan, C.S.; Rao, N.A.: Plant aspartate transcarbamyl-ase: kinetic properies of the enzyme from mung bean (Phaseolus aureus) seedlings. Proc. Indian Acad. Sci. Sect. B, 87B, 81–94 (1978)

    CAS  Google Scholar 

  23. Brabson, J.S.; Maurizi, M.R.; Switzer, R.L.: Aspartate transcarbamylase from Bacillus subtilis. Methods Enzymol., 113, 627–635 (1985)

    PubMed  CAS  Google Scholar 

  24. Chang, T.Y.; Prescott, L.M.; Jones, M.E.: Aspartate carbamyltransferase (Streptococcus faecalis). Methods Enzymol., 51, 41–50 (1978)

    PubMed  CAS  Google Scholar 

  25. Adair, L.B.; Jones, M.E.: Aspartate carbamyltransferase (Pseudomonas fluorescens). Methods Enzymol., 51, 51–58 (1978)

    PubMed  CAS  Google Scholar 

  26. Chang, T.Y.; Jones, M.E.: Aspartate transcarbamylase from Streptococcus faecalis. Purification, properties, and nature of an allosteric activator site. Biochemistry, 13, 629–638 (1974)

    Article  PubMed  CAS  Google Scholar 

  27. Chang, T.Y.; Jones, M.E.: Aspartate transcarbamylase from Streptococcus faecalis. Steady-state kinetic analysis. Biochemistry, 13, 638–645 (1974)

    Article  PubMed  CAS  Google Scholar 

  28. Achar, B.S.; Savithri, H.S.; Vaidyanathan, C.S.; Rao, N. A.: Studies on plant aspartate transcarbamylase. Purification and properties of the enzyme from mung-bean (Phaseolus aureus) seedlings. Eur. J. Biochem., 47, 15–22 (1974)

    Article  PubMed  CAS  Google Scholar 

  29. Ong, B.L.; Jackson, J.F.: Aspartate transcarbmoylase from Phaseolus aureus. Biochem. J., 129, 571–581 (1972)

    PubMed  CAS  Google Scholar 

  30. Jarry, B.P.: Purification of aspartate transcarbamylase from Drosophila mel-anogaster. Eur. J. Biochem., 87, 533–540 (1978)

    Article  PubMed  CAS  Google Scholar 

  31. Adair, L.B.; Jones, M.E.: Purification and characteristics of aspartate transcarbamylase from Pseudomonas fluorescens. J. Biol. Chem., 247, 2308–2315 (1972)

    PubMed  CAS  Google Scholar 

  32. Masood, R.; Venkitasubramanian, T.A.: Purification and properties of aspartate transcarbamylase from Mycobacterium smegmatis. Biochim. Biophys. Acta, 953, 106–113 (1988)

    PubMed  CAS  Google Scholar 

  33. Mori, M.; Tatibana, M.: A multienzyme complex of carbamoyl-phosphate synthase (glutamine):aspartate carbamoyltransferase:dihydroorotase (rat ascites hepatoma cells and rat liver). Methods Enzymol., 51, 111–121 (1978)

    Article  PubMed  CAS  Google Scholar 

  34. Coleman, RE; Suttle, D.P.; Stark, G.R.: Purification of a multifunctional protein bearing carbamyl-phosphate synthase, aspartate transcarbamylase, and dihydroorotase enzyme activities from mutant hamster cells. Methods Enzymol., 51, 121–134 (1978)

    PubMed  CAS  Google Scholar 

  35. Purcarea, C; Erauso, G.; Prieur, D.; Herve, G.: The catalytic and regulatory properties of aspartate transcarbamoylase from Pyrococcus abyssi, a new deep-sea hyperthermophilic archaeobacterium. Microbiology, 140, 1967–1975 (1994)

    CAS  Google Scholar 

  36. Xi, X.G.; De Staercke, C; Van Vliet, E; Triniolles, E; Jacobs, A.; Stas, P.P.; Ladjimi, M.M.; Simon, V; Cunin, R.; Herve, G.: The activation of Escheri-chia coli aspartate transcarbamylase by ATP. Specific involvement of helix H2’ at the hydrophobic interface between the two domains of the regulatory chains. J. Mol. Biol., 242, 139–149 (1994)

    Article  PubMed  CAS  Google Scholar 

  37. Lee, B.H.; Ley, B.W.; Kantrowitz, E.R.; O’Leary, M.H.; Wedler, F.C.: Domain closure in the catalytic chains of Escherichia coli aspartate transcarbamoyl-ase influences the kinetic mechanism. J. Biol. Chem., 270, 15620–15627 (1995)

    Article  PubMed  CAS  Google Scholar 

  38. Baker, D.R; Aucoin, J.M.; Williams, M.K.; DeMello, L.A.; Kantrowitz, E.R.: Overexpression and purification of the trimeric aspartate transcarbamoyl-ase from Bacillus subtilis. Protein Expr. Purif., 6, 679–684 (1995)

    Article  PubMed  CAS  Google Scholar 

  39. Khan, A.; Chowdhry, B.Z.; Yon, R.J.: Effects of lipids on nucleotide inhibition of wheat-germ aspartate transcarbamoylase: evidence of an additional level of control?. Biochem. J., 313, 669–673 (1996)

    PubMed  CAS  Google Scholar 

  40. Yuan, X.; LiCata, V.J.; Allewell, N.M.: Effects of assembly and mutations outside the active site on the functional pH dependence of Escherichia coli aspartate transcarbamylase. J. Biol. Chem., 271, 1285–1294 (1996)

    Article  PubMed  CAS  Google Scholar 

  41. Burns, B.P.; Mendz, G.L.; Hazell, S.L.: In situ properties of Helicobacter pylori aspartate carbamoyltransferase. Arch. Biochem. Biophys., 347, 119–125 (1997)

    Article  PubMed  CAS  Google Scholar 

  42. Xu, Y; Zhang, Y; Liang, Z.; Van de Casteele, M.; Legrain, C; Glansdorff, N.: Aspartate carbamoyltransferase from a psychrophilic deep-sea bacterium, Vibrio strain 2693: properties of the enzyme, genetic organization and synthesis in Escherichia coli. Microbiology, 144, 1435–1441 (1998)

    Article  PubMed  CAS  Google Scholar 

  43. Liu, L.; Wales, M.E.; Wild, J.R.: Temperature effects on the allosteric responses of native and chimeric aspartate transcarbamoylases. J. Mol. Biol., 282, 891–901 (1998)

    Article  PubMed  CAS  Google Scholar 

  44. Khan, A.I.; Chowdhry, B.Z.; Yon, R.J.: Wheat germ aspartate transcarbamoylase: revised purification, stability and re-evaluation of regulatory kinetics in terms of the Monod-Wyman-Changeux model. Eur. J. Biochem., 259, 71–78 (1999)

    Article  PubMed  CAS  Google Scholar 

  45. Durbecq, V; Thia-Toong, T.L.; Charlier, D.; Villeret, V; Roovers, M.; Wat-tiez, R.; Legrain, C; Glansdorff, N.: Aspartate carbamoyltransferase from the thermoacidophilic archaeon Sulfolobus acidocaldarius cloning, sequence analysis, enzyme purification and characterization. Eur. J. Biochem., 264, 233–241 (1999)

    Article  PubMed  CAS  Google Scholar 

  46. Vorisek, J.; Noaillac-Depeyre, J.; Denis-Duphil, M.: Life-cycle-dependent changes of aspartate carbamoyltransferase localization in membranes of Saccharomyces cerevisiae-centrifugal elutriation and ultracytochemical study. Folia Microbiol., 44, 289–294 (1999)

    Article  CAS  Google Scholar 

  47. Jin, L.; Stec, B.; Lipscomb, W.N.; Kantrowitz, E.R.: Insights into the mechanisms of catalysis and heterotropic regulation of Escherichia coli aspartate transcarbamoylase based upon a structure of the enzyme complexed with the bisubstrate analogue N-phosphonacetyl-L-aspartate at 2.1 A Proteins Struct. Funct. Genet., 37, 729–742 (1999)

    Article  CAS  Google Scholar 

  48. Hack, E.S.; Vorobyova, T.; Sakash, J.B.; West, J.M.; Macol, C.P.; Herve, G.; Williams, M.K.; Kantrowitz, E.R.: Characterization of the aspartate transcarbamoylase from Methanococcus jannaschii. J. Biol. Chem., 275, 15820–15827 (2000)

    Article  PubMed  CAS  Google Scholar 

  49. Endrizzi, J.A.; Beernink, P.T.; Alber, T.; Schachman, H.K.: Binding of bisubstrate analog promotes large structural changes in the unregulated catalytic trimer of aspartate transcarbamoylase: implications for allosteric regulation. Proc. Natl. Acad. Sci. USA, 97, 5077–5082 (2000)

    Article  PubMed  CAS  Google Scholar 

  50. Fetler, L.; Tauc, P.; Baker, D.P.; Macol, C.P.; Kantrowitz, E.R.; Vachette, P.: Replacement of Asp-162 by Ala prevents the cooperative transition by the substrates while enhancing the effect of the allosteric activator ATP on E. coli aspartate transcarbamoylase. Protein Sci., 11, 1074–1081 (2002)

    Article  PubMed  CAS  Google Scholar 

  51. West, J.M.; Tsuruta, H.; Kantrowitz, E.R.: Stabilization of the R allosteric structure of Escherichia coli aspartate transcarbamoylase by disulfide bond formation. J. Biol. Chem., 277, 47300–47304 (2002)

    Article  PubMed  CAS  Google Scholar 

  52. Vickrey, J.F.; Herve, G.; Evans, D.R.: Pseudomonas aeruginosa aspartate transcarbamoylase. Characterization of its catalytic and regulatory properties. J. Biol. Chem., 277, 24490–24498 (2002)

    Article  PubMed  CAS  Google Scholar 

  53. Van Boxstael, S.; Cunin, R.; Khan, S.; Maes, D.: Aspartate transcarbamylase from the hyperthermophilic archaeon Pyrococcus abyssi: thermostability and 1.8 A resolution crystal structure of the catalytic subunit complexed with the bisubstrate analogue N-phosphonacetyl-L-aspartate. J. Mol. Biol., 326, 203–216 (2003)

    Google Scholar 

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(2006). Aspartate carbamoyltransferase. In: Schomburg, D., Schomburg, I., Chang, A. (eds) Springer Handbook of Enzymes. Springer Handbook of Enzymes, vol 29. Springer, Berlin, Heidelberg. https://doi.org/10.1007/3-540-37716-6_13

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