Aspartate transcarbamylase from the hyperthermophilic archaeon Pyrococcus abyssi: Insights into cooperative and allosteric mechanisms

FEBS Journal

Volumn 272, Issue 11, 2005, Pages 2670-2683

  Van Boxstael, Sigrid ^a   Maes, Dominique ^a,b   Cunin, Raymond ^a  

^a VRIJE UNIVERSITEIT BRUSSEL   (Belgium)

^b DEPARTMENT OF PLANT SYSTEMS BIOLOGY   (Belgium)

Author keywords

Allostery; Aspartate transcarbamylase; Cooperativity; Inhibition by analogues; Pyrococcus abyssi

Indexed keywords

ADENOSINE TRIPHOSPHATE; ASPARTATE CARBAMOYLTRANSFERASE; BACTERIAL ENZYME; CARBAMOYL PHOSPHATE; CYTIDINE TRIPHOSPHATE; SPARFOSIC ACID;

ALLOSTERISM; ARTICLE; BACTERIAL CELL; CONTROLLED STUDY; ENZYME ACTIVITY; ESCHERICHIA COLI; HIGH TEMPERATURE; NONHUMAN; PHASE TRANSITION; PRIORITY JOURNAL; PYROCOCCUS ABYSSI; THERMOSTABILITY; ULTRACENTRIFUGATION;

ADENOSINE TRIPHOSPHATE; ALLOSTERIC REGULATION; ALLOSTERIC SITE; ASPARTATE CARBAMOYLTRANSFERASE; CARBAMOYL-PHOSPHATE SYNTHASE (AMMONIA); CARBAMYL PHOSPHATE; CATALYSIS; CYTIDINE TRIPHOSPHATE; ESCHERICHIA COLI; PHOSPHONOACETIC ACID; PYROCOCCUS ABYSSI; RECOMBINANT PROTEINS; URIDINE TRIPHOSPHATE;

ARCHAEA; ESCHERICHIA COLI; PYROCOCCUS ABYSSI;

EID: 20444469673     PISSN: 1742464X     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1742-4658.2005.04678.x     Document Type: Article

References (54)

1. Helmstaedt K, Krappmann S & Braus GH (2001) Allosteric regulation of catalytic activity: Escherichia coli aspartate transcarbamoylase versus yeast chorismate mutase. Microbiol Mol Biol Rev 65, 404-421.
2. Hervé G. (1989) Aspartate transcarbamylase from Escherichia coli. In Allosteric Enzymes (Hervé G, ed.). pp. 61-79. CRC Press, Boca Raton, FL.
3. Kantrowitz ER & Lipscomb WN (1988) Escherichia coli aspartate transcarbamylase: the relations between structure and function. Science 241, 669-674.
4. Lipscomb W (1994) Aspartate transcarbamylase from Escherichia coli: activity and regulation. Adv Enzymol 68, 67-152.
5. Lipscomb WN (1995) Activity and allosteric regulation in mammalian fructose-1,6-biphosphatase and E. coli aspartate transcarbamylase. Biopolymers and Bioproducts. Proceedings of the 11th FAOBMB Symposium, pp. 327-335. Samakkishan Public Company Ltd., Bangkok.
6. Van Boxstael S, Cunin R, Khan S & Maes D (2003) Aspartate transcarbamylase from the hyperthermophilic archaeon Pyrococcus abyssi: thermostability and 1.8 Å resolution crystal structure of the catalytic subunit complexed with the bisubstrate analogue N-phopsphonacetyl-L-aspartate. J Mol Biol 326, 203-216.
7. Purcarea C (1995) Enzymes involved in carbamoyl phosphate metabolism from the hyperthermophilic and barophilic marine archaebacterium Pyrococcus abyssi, PhD Thesis, Université de Paris-Sud, France.
8. Purcarea C, Hervé G, Ladjimi MM & Cunin R (1997) Aspartate transcarbamylase from the deep-sea hyperthermophilic archaeon Pyrococcus abyssi: genetic organization, structure and expression in Escherichia coli. J Bacteriol 179, 4143-4157.
9. Purcarea C, Evans DR & Hervé G (1999) Channeling of carbamoyl phosphate to the pyrimidine and arginine biosynthetic pathways in the deep sea hyperthermophilic Archaeon Pyrococcus abyssi. J Biol Chem 274, 6122-6129.
10. Legrain C, Demarez M, Glansdorff N & Piérard A (1995) Ammonia-dependent synthesis and metabolic channelling of carbamoyl phosphate in the hyperthermophilic archaeon Pyrococcus furiosus. Microbiology 141, 1093-1099.
11. Massant J, Verstreken P, Durbecq V, Kholti A, Legrain C, Beeckmans S, Cornelis P & Glansdorff N (2002) Metabolic channeling of carbamoyl phosphate, a thermolabile intermediate. J Biol Chem 277, 18517-18522.
12. Cornish-Bowden A (1995) Fundamentals of Enzyme Kinetics. Portland Press, London.
13. England P, Leconte C, Tauc P & Hervé G (1994) Apparent cooperativity for carbamoylphosphate in Escherichia coli aspartate transcarbamoylase only reflects cooperativity for aspartate. Eur J Biochem 222, 775-780.
14. Collins KD & Stark GR (1971) Aspartate transcarbamylase. Interaction with the transition state analog N-phosphonacetyl-L-aspartate. J Biol Chem 246, 6599-6605.
15. Jacobsen GR & Stark GR (1973) Aspartate transcarbamylase: a study of possible roles for the sulfhydryl group at the active site. J Biol Chem 248, 8003-8014.
16. Kerbiriou D, Hervé G & Griffin JH (1977) An aspartate transcarbamylase lacking catalytic subunit interactions. Study of conformational changes by ultraviolet and cirucular dichroism spectroscopy. J Biol Chem 252, 2881.
17. Purcarea C, Erauso G, Prieur D & Hervé G (1994) The catalytic and regulatory properties of aspartate transcarbamoylase from Pyrococcus abyssi, a new deep-sea hyperthermophilic archaeobacterium. Microbiology 140, 1967-1975.
18. Porter RW, Modebe MO & Stark GR (1969) Aspartate transcarbamylase. Kinetic studies of the catalytic subunit. J Biol Chem 214, 1846-1859.
19. Beernink PT, Yang YR, Graf R, King DS, Shah SS & Schachman HK (2001) Random circular permutation leading to chain disruption within and near α helices in the catalytic chains of aspartate transcarbamoylase: effects on assembly, stability and function. Protein Sci 10, 528-537.
20. Howlett GJ & Schachman HK (1977) Allosteric regulation of aspartate transcarbamoylase. Changes in the sedimentation coefficient promoted by the bisubstrate analogue N-(phosphonacetyl)-L-aspartate. Biochemistry 16, 5077-5083.
21. Xinhai X & Schachman HK (2001) In vivo assembly of aspartate transcarbamylase from fragmented and circularly permuted catalytic polypeptide chains. Protein Sci 10, 519-527.
22. England P & Hervé G (1992) Synergistic inhibition of Escherichia coli aspartate transcarbamylase by CTP and UTP: binding studies using continuous-flow dialysis. Biochemistry 31, 9725-9732.
23. Matsumoto S & Hammes GG (1973) An equilibrium binding study of the interaction of aspartate transcarbamylase with cytidine 5′-triphosphate and adenosine-5′-triphosphate. Biochemistry 12, 1388-1394.
24. 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.
25. Webb JL (1963) General principles of inhibition. In Enzyme and Metabolic Inhibitors, Vol. 1. pp. 949-959. Academic Press, New York.
26. Bethell MR & Jones ME (1969) Molecular size and feedback regulation characteristics of bacterial aspartate transcarbamylase. Arch Biochem Biophys 134, 352-365.
27. Wild JR & Wales M (1990) Molecular evolution and genetic engineering of protein domains involving aspartate transcarbamoylase. Annu Rev Microbiol 44, 193-218.
28. Xu Y & Glansdorff N (2002) Was our ancestor a hyperthermophilic procaryote? Comp Biochem Physiol A 133, 677-688.
29. Labedan B & Boyen A (1998) The evolutionary history of carbamoyltranseferase: insights on the early evolution of the last universal common ancestor. In Thermophiles: the keys to molecular evolution and the origin of Life (Wiegel J, Adams MWW, eds), pp. 231-240. Taylor & Francis, Philadelphia.
30. Labedan B, Boyen A, Baetens M et al. (1999) The evolutionary history of carbamyltransferases: a complex set of paralogous genes was already present in the last universal common ancestor. J Mol Evol 49, 461-473.
31. Labedan B, Xu Y, Naumoff DG & Glansdorff N (2004) Using quaternary structures to assess the evolutionary history of proteins: the case of the aspartate carbamoyltransferase. Mol Biol Evol 21, 364-373.
32. Durbecq V, Thia-Toong T-L, Charlier D. Villeret V, Roovers M, Wattiez R, Legrain C & Glansdorff N (1999) Aspartate carbamoyltransferase from the thermoacidophilic archaeon Sulfolobus acidocaldarius. Cloning, sequence analysis, enzyme purification and characterization. Eur J Biochem 264, 233-241.
33. Jin L, Stec B, Lipscomb WN & Kantrowitz ER (1999) 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-phosphon-acetyl-L-aspartate at 2.1 Å. Proteins 37, 729-742.
34. Fetler L, Vachette P, Hervé G & Ladjimi MM (1995) Unlike the quaternary structure transition, the tertiary structure change of the 240S loop in allosteric aspartate transcarbamylase requires active site saturation by substrate for completion. Biochemistry 34, 15654-15660.
35. Fetler L, Taue P, Hervé G, Moody MF & Vachette P (1995) X-Ray scattering titration of the quaternary structure transition of aspartate transcarbamylase with a bisubstrate analogue: influence of nucleotide effectors. J Mol Biol 251, 243-255.
36. Fetler L & Vachette P (2001) The allosteric activator Mg-ATP modifies the quaternary structure of the R-state of Escherichia coli aspartate transcarbamylase without altering the T ? R equilibrium. J Mol Biol 309, 817-832.
37. Gerhart JC & Schachman HK (1968) Allosteric interactions in aspartate transcarbamylase. II. Evidence for different conformational states of the protein in the presence and abscence of specific ligands. Biochemistry 7. 538-552.
38. Allison R & Purich D (1983) Practical considerations in the design of initial velocity enzyme rate assays. In Contemporary Enzyme Kinetics and Mechanism, pp. 33-52. Academic Press, London.
39. Purcarea C (2001) Aspartate transcarbamoylase from Pyrococcus abyssi. Methods Enzymol 331, 248-270.
40. Cunin R, Swarupa Rani C, Van Vliet F, Wild JR & Wales M (1999) Intramolecular signal transmission in enterobacterial aspartate transcarbamylases II. Engineering co-operativity and allosteric regulation in the aspartate transcarbamylase of Erwinia herbicola. J Mol Biol 294, 1401-1411.
41. De Staercke C, Van Vliet F, Xi XG, Rani CS, Ladjimi MM, Jacobs A, Triniolles F, Hervé G & Cunin R (1995) Intramolecular transmission of the ATP regulatory signal in Escherichia coli aspartate transcarbamylase. Specfic involvement of a clustered set of amino acid interactions at an interface between regulatory and catalytic subunits. J Mol Biol 246, 132-143.
42. Liu L, Wales M & Wild J (1997) Conversion of the allosteric regulatory patterns of aspartate transcarbamylase by exchange of a single β-strand between diverged regulatory chains. Biochemistry 36, 3126-3132.
43. Van Vliet F, Xi XG, De Staercke C, De Wannemaeker B, Jacobs A, Cherfils J, Ladjimi MM, Hervé G & Cunin R (1991) Heterotropic interactions in aspartate transarbamoylase: turning allosteric ATP activation into inhibition as a consequence of a single tyrosine to phenylalanine mutation. Proc Natl Acad Sci USA 88, 9180-9183.
44. Stevens RC & Lipscomb WN (1992) A molecular mechanism for pyrimidine and purine nucleotide control of aspartate transcarbamylase. Proc Natl Acad Sci USA 89, 5281-5285.
45. Xi XG, Van Vliet F, Ladjimi MM, De Wannemaecker B, De Staercke C, Glansdorff N, Piérard A, Cunin R & Hervé G (1991) Heterotropic interactions in Escherichia coli aspartate transcarbamylase. J Mol Biol 220, 789-799.
46. Kim R, Sandler SJ, Yokota H, Clark AJ & Kim SH (1998) Overexpression of Archaeal proteins in Escherichia coli. Biotechnol Lett 20, 207-210.
47. Glansdorff N (1965) Topography of co-transducible arginine mutations in E. coli K-12. Genetics 51, 167-179.
48. Pace CN, Vajdos F, Fee L, Grimsley G & Gray T (1995) How to measure and predict the molar absorption coefficient of a protein. Protein Sci 4, 2411-2423.
49. Prescott LM & Jones ME (1969) Modified methods for the determination of carbamylaspartate. Anal Biochem 32, 408-419.
50. Dutta M & Kantrowitz ER (1998) The influence of the regulatory chain amino acids Glu-62 and Ile-12 on the heterotropic properties of Escherichia coli aspartate transcarbamoylase. Biochemistry 37, 8653-8658.
51. Sakash JB & Kantrowitz ER (1998) The N-terminus of the regulatory chain of Escherichia coli aspartate transcarbamoylase is important for both nucleotide binding and heterotropic effects. Biochemistry 37, 281-288.
52. Kelly L & Holladay LA (1990) A comparative study of the unfolding thermodynamics of vertebrate metmyoglobins. Biochemistry 29, 5062-5069.
53. Stafford WF III (1992) Boundary analysis in sedimentation transport experiments: a procedure for obtaining sedimentation coefficient distributions using the time derivative of the concentration profile. Anal Biochem 203, 295-301.
54. Shire SJ, Holladay LA & Rinderknecht E (1991) Self association of human and porcine relaxin as assessed by analytical ultracentrifugation and circular dichroism. Biochemistry 30, 7703-7711.