Biochemical characterisation of ornithine carbamoyltransferase from Pyrococcus furiosus

European Journal of Biochemistry

Volumn 247, Issue 3, 1997, Pages 1046-1055

  Legrain, Christianne ^a   Villeret, Vincent ^b,c   Roovers, Martine ^d,e   Gigot, Daniel ^f   Dideberg, Otto ^c   Piérard, André ^a,f   Glansdorff, Nicolas ^a,d,e,g  

^a Inst Rech Ctr d'Enseignement R   (Belgium)

^b GHENT UNIVERSITY   (Belgium)

^c INSTITUT DE BIOLOGIE STRUCTURALE   (France)

^d VRIJE UNIVERSITEIT BRUSSEL   (Belgium)

^e DEPARTMENT OF PLANT SYSTEMS BIOLOGY   (Belgium)

^f UNIVERSITÉ LIBRE DE BRUXELLES   (Belgium)

^g Institut de Recherches du CERIA   (Belgium)

Author keywords

Archaea; Hyperthermophiles; Ornithine carbamoyltransferase; Pyrococcus furiosus; Thermostability

Indexed keywords

ORNITHINE CARBAMOYLTRANSFERASE;

ARTICLE; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME PURIFICATION; ESCHERICHIA COLI; GENE EXPRESSION; PRIORITY JOURNAL; SACCHAROMYCES CEREVISIAE; THERMOPHILIC BACTERIUM; THERMOSTABILITY;

ARCHAEA; BACTERIA (MICROORGANISMS); ESCHERICHIA COLI; PSEUDOMONAS; PSEUDOMONAS AERUGINOSA; PYROCOCCUS FURIOSUS; SACCHAROMYCES CEREVISIAE;

EID: 0030839261     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1432-1033.1997.01046.x     Document Type: Article

References (41)

1. Baur, H., Stalon, V., Falmagne, P., Luethi, E. & Haas, D. (1987) Primary and quaternary structure of the catabolic ornithine carbamoyltransferase from Pseudomonas aeruginosa. Extensive sequence homology with the anabolic ornithine carbamoyltransferases of Escherichia coli, Eur. J. Biochem. 166, 111-117.
2. Britton, K. L., Baker, P. J., Borges, K. M. M., Engel, P. C., Pasquo, A., Rice, D. W., Robb, F. T., Scandurra, R., Stillman, T. J. & Yip, K. S. P. (1995) Insights into thermal stability from a comparison of the glutamate dehydrogenase from Pyrococcus furiosus and Thermococcus litoralis, Eur. J. Biochem. 229, 688-695.
3. Brünger, A. T. (1992) X-PLOR: a system for X-ray crystallography and NMR, Yale University Press, New Haven CT.
4. Cunin, R., Glansdorff, N., Piérard, A. & Stalon, V. (1986) Biosynthesis and metabolism of arginine in bacteria, Microbiol. Rev. 50, 314-352.
5. Davis, R. H. (1986) Compartmental and regulatory mechanisms in the arginine pathway of Neurospora crassa and Saccharomyces cerevisiae, Microbiol. Rev. 50, 280-313.
6. Fiala, G. & Stetter, K. O. (1986) Pyrococcus furiosus sp. nov. represents a novel genus of marine heterotrophic archaebacteria growing optimally at 100°C, Arch. Microbiol. 145, 56-61.
7. Fiala, G., Stetter, K. O., Jannasch, H. W., Langworthy, T. A. & Madon, J. (1986) Staphylothermus marinus sp. nov. represents a novel genus of extremely thermophilic submarine heterotrophic archaebacteria growing up to 98°C, Syst. Appl. Microbiol. 8, 106-113.
8. Gaboriaud, C., Bissery, V., Benchetrit, T. & Mornon, J. P. (1987) Hydrophobic cluster analysis: an efficient new way to compare and analyse amino acid sequences, FEBS Lett. 224, 149-155.
9. Glansdorff, N. (1996) Biosynthesis of arginine and polyamines, in Escherichia coli and Salmonella. Cellular and molecular biology (Neidhardt, F., ed. in chief) pp. 408-433, American Society for Microbiology, Washington DC.
10. Gorini, L. & Maas, W. K. (1957) The potential for the formation of a biosynthetic enzyme in Escherichia coli, Biochim. Biophys. Acta 25, 208-209.
11. Guillou, F., Rubino, S. D., Markovitz, R. S., Kinney, D. M. & Lusty, C. J. (1989) Escherichia coli carbamoyl-phosphate synthetase: Domains of glutaminase and synthetase subunit interaction, Proc. Natl Acad. Sci. USA 86, 8304-8308.
12. Kirino, H., Aoki, M., Aoshima, M., Hayashi, Y., Ohba, M., Yamagishi, A., Wakagi, T. & Oshima, T. (1994) Hydrophobic interaction at the subunit interface contributes to the thermostability of 3-isopropylmalate dehydrogenase from an extreme thermophile. Thermus thermophilus, Eur. J. Biochem. 220, 275-281.
13. Korndörfer, I., Steipe, B., Huber, R., Tomschy, A. & Jaenicke, R. (1995) The crystal structure of holo-glyceraldehyde-3-phosphate dehydrogenase from the hyperthermophilic bacterium Thermotoga maritima at 2.5 Å resolution, J. Mol. Biol. 246, 511-521.
14. Kraulis, P. J. (1991) MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures, J. Appl. Crystallogr. 24, 946-950.
15. Kuo, L. C., Herzberg, W. & Lipscomb, W. N. (1985) Substrate specificity and protonation state of ornithine transcarbamoylase as determined by pH studies, Biochemistry 24, 4754-4761.
16. Kuo, L. C., Miller, A. W., Lee, S. & Kozuma, C. (1988) Site-directed mutagenesis of Escherichia coli ornithine transcarbamoylase: role of arginine-57 in substrate binding and catalysis, Biochemistry 27, 8823-8832.
17. 2+ regulation of ornithine transcarbamoylase. II. Metal binding site, J. Mol. Biol. 211, 271-280.
18. Legrain, C. & Stalon, V. (1976) Ornithine carbamoyltransferase from Escherichia coli W. Purification, structure and steady-state kinetic analysis, Eur. J. Biochem. 63, 289-301.
19. Legrain, C., Stalon, V., Noullez, J. P., Mercenier, A., Simon, J. P., Broman, K. & Wiame, J. M. (1977) Structure and function of ornithine carbamoyltransferases, Eur. J. Biochem. 80, 401-409.
20. Legrain, C., Demarez, M., Glansdorff, N. & Piérard, A. (1995) Ammonia-dependent synthesis and metabolic channeling of carbamoylphosphate in the hyperthermophilic archaeon Pyrococcus furiosus, Microbiology 141, 1093-1099.
21. Lerner, C. G. & Switzer, R. L. (1986) Cloning and structure of the Bacillus subtilis aspartate transcarbamylase gene (pyrB), J. Biol. Chem. 261, 11156-11165.
22. Marshall, M. & Cohen, P. P. (1972) Ornithine transcarbamylase from Streptococcus faecalis and bovine liver. I. Isolation and subunit structure, J. Biol. Chem. 247, 1641-1653.
23. Murata, L. B. & Schachman, H. K. (1996) Structural similarity between ornithine and aspartate transcarbamoylases of Escherichia coli: characterization of the active site and evidence for an interdomain carboxy-terminal helix in ornithine transcarbamoylase, Protein Sci. 5, 709-718.
24. Mouz, N., Tricot, C., Ebel, C., Petillot, Y., Stalon, V. & Dideberg, O. (1996) Use of a designed fusion protein dissociates allosteric properties from the dodecameric state of Pseudomonas aeruginosa catabolic ornithine carbamoyltransferase, Proc. Natl Acad. Sci. USA 93, 9414-9419.
25. Penninckx, M. & Gigot, D. (1978) Synthesis and interaction with Escherichia coli L-ornithine carbamoyltransferase of two potential transition-state analogues, FEBS Lett. 88, 94-96.
26. Purcarea, C., Simon, V., Prieur, D. & Hervé, G. (1996) Purification and characterization of carbamoyl-phosphate synthetase from the deep-sea hyperthermophilic archaebacterium Pyrcoccus abyssi, Eur. J. Biochem. 236, 189-199.
27. Rice, D. W., Yip, K. S. P., Stillman, T. J., Britton, K. L., Fuentes, A., Connerton, I., Pasquo, A., Scandurra, R. & Engel, P. C. (1996) Insights into the molecular basis of thermal stability from the structure determination of Pyrococcus furiosus glutamate dehydrogenase, FEMS Microbiol. Rev. 18, 105-117.
28. Roovers, M., Hethke, C., Thomm, M. & Glansdorff, N. (1997) Isolation of the gene encoding Pyrococcus furiosus ornithine carbamoyltransferase and study of its expression profile in vivo and in vitro, Eur. J. Biochem. 247, 1038-1045.
29. Roussel, A. & Cambillau, C. (1989) Silicon graphics geometry partner directory, pp. 77-78, Silicon Graphics, Mountain View CA.
30. Ruepp, A., Muller, H. N., Lottspeich, F. & Soppa, J. (1995) Catabolic ornithine carbamoyltransferase of Halobacteirum halobium (salinarium): purification, characterization, sequence determination, and evolution, J. Bacteriol. 177, 1129-1136.
31. Scholz, S., Sonnenbichler, J., Schafer, W. & Hensel, R. (1992) Di-myo-inositol-1,1′-phosphate: a new inositol phosphate isolated from Pyrococcus woesei, FEBS Lett. 306, 239-242.
32. Snodgrass, P. J. (1968) The effects of pH on the kinetics of human liver ornithine carbamylphosphate transferase, Biochemists 7, 3047-3051.
33. Stalon, V., Ramos, F., Piérard, A. & Wiame, J. M. (1972) Regulation of the catabolic ornithine carbamoyltransferase of Pseudomonas fluorescens. A comparison with the anabolic transferase and with a mutationally modified catabolic transferase, Eur. J. Biochem. 29, 25-35.
34. Summers, N. L., Carlson, W. D. & Karplus, M. (1987) Analysis of side-chain orientations in homologous proteins, J. Mol. Biol. 196, 175-198.
35. Van de Casteele, M., Demarez, M., Legrain, C., Glansdorff, N. & Piérard, A. (1990) Pathways of arginine biosynthesis in extreme thermophilic archaeo- and eubacteria, J. Gen. Microbiol. 136, 1177-1183.
36. Van de Casteele, M., Desmarez, L., Legrain, C., Chen, P. G., Van Lierde, K., Piérard, A. & Glansdorff, N. (1994) Genes encoding thermophilic aspartate carbamoyltransterases of Thermus aquaticus ZO5 and Thermotoga maritima MSB8: modes of expression in E. coli and properties of their products, Biocatalysis 112, 165-179.
37. Van de Casteele, M., Legrain, C., Desmarez, L., Chen, P. G., Piérard, A. & Glansdorff, N. (1997) Molecular physiology of carbamoylation under extreme conditions: what can we learn from extreme thermophilic microorganisms? Comp. Physiol. Biochem., in the press.
38. Villeret, V. (1994) Etudes structurales de l'ornithine carbamoyltransférase catabolique de Pseudomonas aeruginosa, PhD thesis, Université de Liège.
39. Villeret, V., Tricot, C., Stalon, V. & Dideberg, O. (1995) Crystal structure of Pseudomonas aeruginosa catabolic ornithine transcarbamoylase at 3.0-Å resolution: a different oligomeric organization in the transcarbamoylase family, Proc. Natl Acad. Sci. USA 92, 10762-10766.
40. Waxdal, M. J., Konigsberg, W. H., Henley, W. L. & Edelman, G. M. (1968) The covalent structure of a human γ G-immunoglobulin. II. Isolation and characterization of the cyanogen bromide fragments, Biochemists 7, 1959-1966.
41. Yip, K. S. P., Stillman, T. J., Britton, K. L., Artymiuk, P. J., Baker, P. J., Sedelnikova, S. E., Engel, P. C., Pasquo, A., Chiaraluce, R., Consalvi, V., Scandurra, R. & Rice, D. W. (1995) The structure of Pyrococcus furiosus glutamate dehydrogenase reveals a key role for ion-pair networks in maintaining enzyme stability at extreme temperatures, Structure 3, 1147-1158.