From feedback inhibition to allostery: The enduring example of aspartate transcarbamoylase

FEBS Journal

Volumn 281, Issue 2, 2014, Pages 612-620

  Gerhart, John ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

allosteric transition; aspartate transcarbamoylase; cooperativity; feedback inhibition; regulatory sites

Indexed keywords

ASPARTATE CARBAMOYLTRANSFERASE; BETA GALACTOSIDASE; CARBON 14; CYTIDINE TRIPHOSPHATE; PURINE NUCLEOTIDE; THREONINE DEHYDRATASE; URIDINE TRIPHOSPHATE;

ALLOSTERISM; BACTERIAL GENETICS; BIOSYNTHESIS; CATALYSIS; CONFORMATIONAL TRANSITION; ENZYME ACTIVATION; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME INDUCTION; ENZYME INHIBITION; ENZYME KINETICS; ENZYME METABOLISM; ENZYME REGULATION; ENZYME REPRESSION; ENZYME STRUCTURE; ENZYME SUBSTRATE; ENZYME SUBSTRATE COMPLEX; ENZYME SYNTHESIS; ESCHERICHIA COLI; IN VIVO STUDY; ISOTOPE LABELING; LIGAND BINDING; MACROMOLECULE; METABOLIC REGULATION; NEGATIVE FEEDBACK; NONHUMAN; NUCLEOTIDE BINDING SITE; OXYGEN SATURATION; PRIORITY JOURNAL; REVIEW;

ESCHERICHIA COLI;

ALLOSTERIC TRANSITION; ASPARTATE TRANSCARBAMOYLASE; COOPERATIVITY; FEEDBACK INHIBITION; REGULATORY SITES;

ALLOSTERIC REGULATION; ALLOSTERIC SITE; ASPARTATE CARBAMOYLTRANSFERASE; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; FEEDBACK, PHYSIOLOGICAL; KINETICS; MODELS, BIOLOGICAL; MODELS, CHEMICAL; PROTEIN BINDING; PROTEIN SUBUNITS;

EID: 84892800241     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/febs.12483     Document Type: Review

References (50)

1. Monod J, Changeux J-P, &, Jacob F, (1963) Allosteric proteins and cellular control systems. J Mol Biol 6, 306-329.
2. Yates R, &, Pardee AB, (1956) Pyrimidine biosynthesis in Escherichia coli. J Biol Chem 221, 743-756.
3. Yates RA, &, Pardee AB, (1956) Control of pyrimidine biosynthesis in Escherichia coli by a feedback mechanism. J Biol Chem 221, 757-770.
4. Monod J, Wyman J, &, Changeux J-P, (1965) On the nature of allosteric transitions: a plausible model. J Mol Biol 12, 88-118.
5. Gerhart JC, (1970) Regulatory properties of aspartate transcarbamoylase from Escherichia coli. Curr Topics Cell Regul 2, 275-325.
6. Wiley DC, &, Lipscomb WN, (1968) Crystallographic determination of the symmetry of aspartate transcarbamoylase. Nature 218, 1119-1121.
7. Lipscomb WN, &, Kantrowitz ER, (2012) Structure and mechanisms of Escherichia coli aspartate transcarbamoylase. Acc Chem Res 45, 444-453.
8. Kantrowitz ER, (2012) Allostery and cooperativity in Escherichia coli aspartate transcarbamoylase. Arch Biochem Biophys 519, 81-90.
9. England P, &, Hervé G, (1992) Synergistic inhibition of Escherichia coli aspartate transcarbamoylase by CTP and UTP: binding studies using continuous-flow dialysis. Biochemistry 31, 9725-9732.
10. Schachman HK, (1988) Can a simple model account for the allosteric transition of aspartate transcarbamoylase? J Biol Chem 263, 18583-18586.
11. Kresge N, Simoni RD, &, Hill RL, (2005) The enzymology of feedback inhibition by Arthur B. Pardee. J Biol Chem 280, e38.
12. Pardee AB, &, Reddy GPV, (2003) Beginnings of feedback inhibition, allostery, and multi-protein complexes. Gene 321, 17-23.
13. Brooke MS, Ushiba D, &, Magasanik B, (1954) Some factors affecting the excretion of orotic acid by mutants of Aerobacter aerogenes. J Bacteriol 68, 534-540.
14. Umbarger HE, (1956) Evidence for a negative-feedback mechanism in the biosynthesis of isoleucine. Science 123, 848.
15. Roberts RB, Abelson PH, Cowie DB, Bolton ET, &, Britten RJ, (1955) Studies of Biosynthesis in Escherichia coli. Carnegie Institution of Washington Publication 607.
16. Novick A, &, Szilard L, (1954) Experiments with the chemostat on the rates of amino acid synthesis in bacteria. In Dynamics of Growth Processes (, Boell EJ, ed.), pp. 21-32. Princeton University Press, Princeton, NJ.
17. Pardee AB, Jacob F, &, Monod J, (1959) The genetic control and cytoplasmic expression of 'inducibility' in the synthesis of β-galactosidase by E. coli. J Mol Biol 1, 165-178.
18. Shepherdson M, &, Pardee AB, (1960) Production and crystallization of aspartate transcarbamoylase. J Biol Chem 235, 3233-3237.
19. Kornberg A, (2000) Ten Commandments: lessons from the enzymology of DNA replication. J Bacteriol 182, 3613-3618.
20. Gerhart JC, &, Holoubek H, (1967) The purification of aspartate transcarbamoylase of Escherichia coli and separation of its protein subunits. J Biol Chem 242, 2886-2892.
21. Nelbach ME, Pigiet VP Jr, Gerhart JC, &, Schachman HK, (1972) A role for zinc in the quaternary structure of aspartate transcarbamoylase from Escherichia coli. Biochemistry 11, 315-327.
22. Markby DW, Zhou B-B, &, Schachman HK, (1991) A 70-amino acid zinc-binding polypeptide from the regulatory chain of aspartate transcarbamoylase forms a stable complex with the catalytic subunit leading to markedly altered enzyme activity. Proc Natl Acad Sci USA 88, 10568-10572.
23. Reichard P, &, Hanshoff G, (1956) Aspartate carbamoyl transferase from Escherichia coli. Acta Chem Scand 10, 548-560.
24. Bethell MR, Smith KE, White JS, &, Jones ME, (1968) Carbamoylphosphate: an allosteric substrate for aspartate transcarbamoylase of Escherichia coli. Proc Natl Acad Sci USA 60, 1442-1449.
25. Wyman J, (1948) Heme proteins. Adv Protein Chem 4, 407-531.
26. Umbarger HE, &, Brown B, (1958) Isoleucine and valine metabolism in Escherichia coli. VII. A negative feedback mechanism controlling isoleucine biosynthesis. J Biol Chem 238, 415-420.
27. Gerhart JC, &, Pardee AB, (1963) The effect of the feedback inhibitor, CTP, on subunit interactions in aspartate transcarbamoylase. Cold Spring Harb Symp Quant Biol 28, 491-496.
28. Haldane JBS, (1912) The dissociation of oxyhemoglobin in human blood during partial CO poisoning. J Physiol (Lond) 45, XXII.
29. Gerhart JC, &, Pardee AB, (1962) The enzymology of control by feedback inhibition. J Biol Chem 237, 891-896.
30. Wild JR, Loughrey-Chen SJ, &, Corder TS, (1989) In the presence of CTP, UTP becomes an allosteric inhibitor of aspartate transcarbamoylase. Proc Natl Acad Sci USA 86, 46-50.
31. Gerhart JC, &, Schachman HK, (1965) Distinct subunits for the regulatory and catalytic activity of aspartate transcarbamoylase. Biochemistry 4, 1054-1062.
32. Gerhart JC, &, Pardee AB, (1961) Separation of feedback inhibition from activity of aspartate transcarbamoylase (ATCase). Fed Proc 20, 224.
33. Changeux JP, (1961) The feedback control mechanism of biosynthetic L-threonine deaminase by L-isoleucine Cold Spring Harbor Symp Quant. Biol 26, 313-318.
34. Monod J, &, Jacob F, (1961) Teleonomic mechanisms in cellular metabolism, growth, and differentiation. Cold Spring Harb Symp Quant Biol 26, 389-401.
35. Weber K, (1968) New structural model of E. coli aspartate transcarbamoylase and the amino-acid sequence of the regulatory polypeptide chain. Nature 218, 1116-1119.
36. Gerhart J, (1964) Subunits for control and catalysis in aspartate transcarbamoylase. Brookhaven Symp Biol 17, 222-231.
37. Gerhart JC, &, Pardee AB, (1964) Aspartate transcarbamoylase, an enzyme designed for feedback inhibition. Fed Proc 23, 727-735.
38. Muirhead H, &, Perutz MF, (1963) Structure of haemoglobin. A three-dimensional Fourier synthesis of reduced human haemoglobin at 5.5 Å resolution. Nature 199, 633-638.
39. Pauling L, (1935) The oxygen equilibrium of hemoglobin and its structural interpretation. Proc Natl Acad Sci USA 21, 186-191.
40. Gerhart JC, &, Schachman HK, (1968) Allosteric interactions in aspartate transcarbamoylase. II. Evidence for different conformational states of the protein in the presence and absence of specific ligands. Biochemistry 7, 538-552.
41. Changeux JP, Gerhart JC, &, Schachman HK, (1968) Allosteric interactions in aspartate transcarbamoylase. I. Binding of specific ligands to the native enzyme and its isolated subunits. Biochemistry 7, 531-538.
42. Changeux JP, &, Rubin MM, (1968) Allosteric interactions in aspartate transcarbamoylase. III. Interpretation of experimental data in terms of the model of Monod, Wyman, and Changeux. Biochemistry 7, 553-560.
43. Koshland DE Jr, Némethy G, &, Filmer D, (1966) Comparison of experimental binding data and theoretical models in proteins containing subunits. Biochemistry 5, 365-368.
44. England P, &, Hervé G, (1994) Involvement of the gamma-phosphate of UTP in the synergistic inhibition of Escherichia coli aspartate transcarbamoylase by CTP and UTP. Biochemistry 33, 3913-3918.
45. Koshland DE, &, Hamadani K, (2002) Proteomics and models for enzyme cooperativity. J Biol Chem 277, 46841-46844.
46. Kosman RP, Gouaux JE, &, Lipscomb WN, (2004) Crystal structure of CTP-ligated T state aspartate transcarbamoylase at 2.5 Å resolution: implications for ATCase mutants and the mechanism of negative cooperativity. Proteins 15, 147-176.
47. Jacob F, &, Monod J, (1961) Genetic regulatory mechanisms in the synthesis of proteins. J Mol Biol 3, 318-356.
48. Britten R, &, Davidson EH, (1969) Gene regulation for higher cells theory. Science 165, 349-357.
49. Wolpert L, (1969) Positional information and the spatial pattern of cellular differentiation. J Theor Biol 25, 1-47.
50. Harland R, &, Gerhart J, (1997) Formation and function of Spemann's organizer. Annu Rev Cell Dev Biol 13, 611-667.