메뉴 건너뛰기




Volumn 179, Issue 13, 1997, Pages 4143-4157

Aspartate transcarbamylase from the deep-sea hyperthermophilic archaeon Pyrococcus abyssi: Genetic organization, structure, and expression in Escherichia coli

Author keywords

[No Author keywords available]

Indexed keywords

ASPARTATE CARBAMOYLTRANSFERASE;

EID: 0030873134     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/jb.179.13.4143-4157.1997     Document Type: Article
Times cited : (33)

References (86)
  • 1
    • 0024386126 scopus 로고
    • Effects of salts on the aspartate transcarbamylase of a halophilic eubacterium, Vibrio costicola
    • Ahonkhai, I., M. Kamekura, and D. J. Kushner. 1989. Effects of salts on the aspartate transcarbamylase of a halophilic eubacterium, Vibrio costicola. Biochem. Cell. Biol. 67:666-669.
    • (1989) Biochem. Cell. Biol. , vol.67 , pp. 666-669
    • Ahonkhai, I.1    Kamekura, M.2    Kushner, D.J.3
  • 2
    • 0001289443 scopus 로고
    • Decomposition of carbamylphosphate in aqueous solutions
    • Allen, C. M. J., and M. E. Jones. 1964. Decomposition of carbamylphosphate in aqueous solutions. Biochemistry 3:1238-1247.
    • (1964) Biochemistry , vol.3 , pp. 1238-1247
    • Allen, C.M.J.1    Jones, M.E.2
  • 3
    • 0024490181 scopus 로고
    • Escherichia coli aspartate transcarbamoylase: Structure, energetics, and catalytic and regulatory mechanisms
    • Allewell, N. M. 1989. Escherichia coli aspartate transcarbamoylase: structure, energetics, and catalytic and regulatory mechanisms. Annu. Rev. Biophys. Biochem. Chem. 18:71-92.
    • (1989) Annu. Rev. Biophys. Biochem. Chem. , vol.18 , pp. 71-92
    • Allewell, N.M.1
  • 4
    • 0024437869 scopus 로고
    • Comparison of the aspartate transcarbamoylases from Serratia marcescens and Escherichia coli
    • Beck, D., K. M. Kedzie, and J. R. Wild. 1989. Comparison of the aspartate transcarbamoylases from Serratia marcescens and Escherichia coli. J. Biol. Chem. 264:16629-16637.
    • (1989) J. Biol. Chem. , vol.264 , pp. 16629-16637
    • Beck, D.1    Kedzie, K.M.2    Wild, J.R.3
  • 5
    • 0024530633 scopus 로고
    • Gene structure, organization, and expression in archaebacteria
    • Brown, J. W., C. J. Daniels, and J. N. Reeve. 1989. Gene structure, organization, and expression in archaebacteria. Crit. Rev. Microbiol. 16:287-338.
    • (1989) Crit. Rev. Microbiol. , vol.16 , pp. 287-338
    • Brown, J.W.1    Daniels, C.J.2    Reeve, J.N.3
  • 7
    • 0026775677 scopus 로고
    • Evidence that a plasmid from a hyperthermophilic archaebacterium is relaxed at physiological temperatures
    • Charbonnier, F., G. Erauso, T. Barbeyron, D. Prieur, and P. Forterre. 1992. Evidence that a plasmid from a hyperthermophilic archaebacterium is relaxed at physiological temperatures. J. Bacteriol. 174:6103-6108.
    • (1992) J. Bacteriol. , vol.174 , pp. 6103-6108
    • Charbonnier, F.1    Erauso, G.2    Barbeyron, T.3    Prieur, D.4    Forterre, P.5
  • 8
    • 0015528760 scopus 로고
    • Structure and arrangement of the regulatory subunits in aspartate transcarbamoylase
    • Cohlberg, J. A., V. P. Pigiet, Jr., and H. K. Schachman. 1972. Structure and arrangement of the regulatory subunits in aspartate transcarbamoylase. Biochemistry 11:3396-3411.
    • (1972) Biochemistry , vol.11 , pp. 3396-3411
    • Cohlberg, J.A.1    Pigiet Jr., V.P.2    Schachman, H.K.3
  • 9
    • 0030595363 scopus 로고    scopus 로고
    • Allosteric regulation in a family of enterobacterial aspartate transcarbamylases: Intramolecular transmission of regulatory signals in chimeric enzymes
    • Cunin, R., M. E. Wales, F. Van Vliet, C. De Staercke, L. Scapozza, C. Swarupa Rani, and J. R. Wild. 1996. Allosteric regulation in a family of enterobacterial aspartate transcarbamylases: intramolecular transmission of regulatory signals in chimeric enzymes. J. Mol. Biol. 262:258-269.
    • (1996) J. Mol. Biol. , vol.262 , pp. 258-269
    • Cunin, R.1    Wales, M.E.2    Van Vliet, F.3    De Staercke, C.4    Scapozza, L.5    Swarupa Rani, C.6    Wild, J.R.7
  • 10
    • 0027564279 scopus 로고
    • The evolutionary history of the 1st 3 enzymes in pyrimidine biosynthesis
    • Davidson, J. N., K. C. Chen, R. S. Jamison, L. A. Musmanno, and C. B. Kern. 1993. The evolutionary history of the 1st 3 enzymes in pyrimidine biosynthesis. Bioessays 15:157-164.
    • (1993) Bioessays , vol.15 , pp. 157-164
    • Davidson, J.N.1    Chen, K.C.2    Jamison, R.S.3    Musmanno, L.A.4    Kern, C.B.5
  • 11
    • 1842382601 scopus 로고    scopus 로고
    • Alignment of aspartate transcarbamylase sequences
    • Davidson, J. N., and M. E. Wales. 1996. Alignment of aspartate transcarbamylase sequences. Paths Pyrimidines 4:11-17.
    • (1996) Paths Pyrimidines , vol.4 , pp. 11-17
    • Davidson, J.N.1    Wales, M.E.2
  • 12
    • 0028951425 scopus 로고
    • Intramolecular transmission of the ATP regulatory signal in Escherichia coli aspartate transcarbamylase: Specific involvement of a clustered set of amino acid interactions at an interface between regulatory and catalytic subunits
    • De Staercke, C., F. Van Vliet, X. G. Xi, C. Rani, M. Ladjimi, A. Jacobs, F. Triniolles, G. Hervé, and R. Cunin. 1995. Intramolecular transmission of the ATP regulatory signal in Escherichia coli aspartate transcarbamylase: specific involvement of a clustered set of amino acid interactions at an interface between regulatory and catalytic subunits. J. Mol. Biol. 246:132-143.
    • (1995) J. Mol. Biol. , vol.246 , pp. 132-143
    • De Staercke, C.1    Van Vliet, F.2    Xi, X.G.3    Rani, C.4    Ladjimi, M.5    Jacobs, A.6    Triniolles, F.7    Hervé, G.8    Cunin, R.9
  • 13
    • 85036482427 scopus 로고    scopus 로고
    • Unpublished data
    • 12a. Durbecq, V., et al. Unpublished data.
    • Durbecq, V.1
  • 14
    • 0026792903 scopus 로고
    • Synergistic inhibition of Escherichia coli aspartate transcarbamylase by CTP and UTP: Binding studies using continuous-flow dialysis
    • England, P., and G. Hervé. 1992. Synergistic inhibition of Escherichia coli aspartate transcarbamylase by CTP and UTP: binding studies using continuous-flow dialysis. Biochemistry 31:9725-9732.
    • (1992) Biochemistry , vol.31 , pp. 9725-9732
    • England, P.1    Hervé, G.2
  • 15
    • 0028334284 scopus 로고
    • Apparent cooperativity for carbamylphosphate in Escherichia coli aspartate transcarbamoylase only reflects cooperativity for aspartate
    • England, P., C. Leconte, P. Tauc, and G. Hervé. 1994. Apparent cooperativity for carbamylphosphate in Escherichia coli aspartate transcarbamoylase only reflects cooperativity for aspartate. Eur. J. Biochem. 222:775-780.
    • (1994) Eur. J. Biochem. , vol.222 , pp. 775-780
    • England, P.1    Leconte, C.2    Tauc, P.3    Hervé, G.4
  • 16
    • 0026514577 scopus 로고
    • Preliminary characterization of a hyperthermophilic archaebacterium with a plasmid, isolated from a North Fiji basin hydrothermal vent
    • Erauso, G., F. Charbonnier, T. Barbeyron, P. Forterre, and D. Prieur. 1992. Preliminary characterization of a hyperthermophilic archaebacterium with a plasmid, isolated from a North Fiji basin hydrothermal vent. C. R. Acad. Sci. Paris Ser. III Sciences Vie 314:387-393.
    • (1992) C. R. Acad. Sci. Paris Ser. III Sciences Vie , vol.314 , pp. 387-393
    • Erauso, G.1    Charbonnier, F.2    Barbeyron, T.3    Forterre, P.4    Prieur, D.5
  • 18
    • 0027516939 scopus 로고
    • CAD gene sequence and the domain structure of the mammalian multifunctional protein CAD
    • Evans, D., K. Bein, H. I. Guy, X. Liu, J. A. Molina, and B. H. Zimmermann. 1993. CAD gene sequence and the domain structure of the mammalian multifunctional protein CAD. Biochem. Soc. Trans. 21:186-191.
    • (1993) Biochem. Soc. Trans. , vol.21 , pp. 186-191
    • Evans, D.1    Bein, K.2    Guy, H.I.3    Liu, X.4    Molina, J.A.5    Zimmermann, B.H.6
  • 19
    • 0024614164 scopus 로고
    • Molecular characterization of a Dictyostelium discoideum gene encoding a multifunctional enzyme of the pyrimidine pathway
    • Faure, M., J. H. Camonis, and M. Jacquet. 1989. Molecular characterization of a Dictyostelium discoideum gene encoding a multifunctional enzyme of the pyrimidine pathway. Eur. J. Biochem. 179:345-358.
    • (1989) Eur. J. Biochem. , vol.179 , pp. 345-358
    • Faure, M.1    Camonis, J.H.2    Jacquet, M.3
  • 20
    • 0023042239 scopus 로고
    • Molecular organization of the rudimentary gene of Drosophila melanogaster
    • Erratum, 191:727
    • Freund, J. N., W. Zerges, P. Scheld, B. P. Jarry, and W. Vergis. 1986. Molecular organization of the rudimentary gene of Drosophila melanogaster. J. Mol. Biol. 189:25-36. (Erratum, 191:727.)
    • (1986) J. Mol. Biol. , vol.189 , pp. 25-36
    • Freund, J.N.1    Zerges, W.2    Scheld, P.3    Jarry, B.P.4    Vergis, W.5
  • 21
    • 0023657949 scopus 로고
    • Hydrophobic cluster analysis: An efficient new way to compare and analyse amino acid sequences
    • Gaboriaud, C., V. Bissery, T. Benchetrit, and J. P. Mornon. 1987. Hydrophobic cluster analysis: an efficient new way to compare and analyse amino acid sequences. FEBS Lett. 224:149-155.
    • (1987) FEBS Lett. , vol.224 , pp. 149-155
    • Gaboriaud, C.1    Bissery, V.2    Benchetrit, T.3    Mornon, J.P.4
  • 22
    • 0025065382 scopus 로고
    • Glycine to alanine substitutions in helices of glyceraldehyde-3-phosphate dehydrogenase: Effects on stability
    • Ganter, C., and A. Plückthun. 1990. Glycine to alanine substitutions in helices of glyceraldehyde-3-phosphate dehydrogenase: effects on stability. Biochemistry 29:9395-9402.
    • (1990) Biochemistry , vol.29 , pp. 9395-9402
    • Ganter, C.1    Plückthun, A.2
  • 23
    • 0001572474 scopus 로고
    • Topography of cotransducible arginine mutations in Escherichia coli K-12
    • Glansdorff, N. 1965. Topography of cotransducible arginine mutations in Escherichia coli K-12. Genetics 51:167-179.
    • (1965) Genetics , vol.51 , pp. 167-179
    • Glansdorff, N.1
  • 24
    • 0024021799 scopus 로고
    • Three-dimensional structure of carbamoyl phosphate and succinate bound to aspartate carbamoyltransferase
    • Gouaux, J. E., and W. N. Lipscomb. 1988. Three-dimensional structure of carbamoyl phosphate and succinate bound to aspartate carbamoyltransferase. Proc. Natl. Acad. Sci. USA 85:4205-4208.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 4205-4208
    • Gouaux, J.E.1    Lipscomb, W.N.2
  • 25
    • 0015523783 scopus 로고
    • Conformational changes in aspartate transcarbamylase. I. Studies of ligand binding and of subunit interactions by circular dichroism spectroscopy
    • Griffin, J. H., J. P. Rosenbusch, K. K. Weber, and E. R. Blout. 1972. Conformational changes in aspartate transcarbamylase. I. Studies of ligand binding and of subunit interactions by circular dichroism spectroscopy. J. Biol. Chem. 247:6482-6490.
    • (1972) J. Biol. Chem. , vol.247 , pp. 6482-6490
    • Griffin, J.H.1    Rosenbusch, J.P.2    Weber, K.K.3    Blout, E.R.4
  • 26
    • 0021253525 scopus 로고
    • Unidirectional digestion with exonuclease III creates targeted breakpoints for DNA sequencing
    • Henikoff, S. 1984. Unidirectional digestion with exonuclease III creates targeted breakpoints for DNA sequencing. Gene 28:351-359.
    • (1984) Gene , vol.28 , pp. 351-359
    • Henikoff, S.1
  • 27
    • 0002135554 scopus 로고
    • Aspartate transcarbamylase from Escherichia coli
    • G. Hervé (ed.), CRC Press, Inc., Boca Raton, Fla.
    • Hervé, G. 1989. Aspartate transcarbamylase from Escherichia coli, p. 62-79. In G. Hervé (ed.), Allosteric enzymes. CRC Press, Inc., Boca Raton, Fla.
    • (1989) Allosteric Enzymes , pp. 62-79
    • Hervé, G.1
  • 28
    • 85036491199 scopus 로고    scopus 로고
    • Unpublished data
    • Hervé, G., et al. Unpublished data.
    • Hervé, G.1
  • 29
    • 0029018738 scopus 로고
    • Nucleotide sequence and tissue-specific expression of the multifunctional protein carbamoyl-phosphate synthetase-aspartate transcarbamoylase-dihydroorotase CAD mRNA in Squalus acanthias
    • Hong, J., W. L. Salo, and P. M. Andersen. 1995. Nucleotide sequence and tissue-specific expression of the multifunctional protein carbamoyl-phosphate synthetase-aspartate transcarbamoylase-dihydroorotase CAD mRNA in Squalus acanthias. J. Biol. Chem. 270:14130-14139.
    • (1995) J. Biol. Chem. , vol.270 , pp. 14130-14139
    • Hong, J.1    Salo, W.L.2    Andersen, P.M.3
  • 30
    • 0020367718 scopus 로고
    • Interactions of phosphate ligands with Escherichia coli aspartate carbamoyltransferase in the crystalline state
    • Honzatko, R. B., and W. N. Lipscomb. 1982. Interactions of phosphate ligands with Escherichia coli aspartate carbamoyltransferase in the crystalline state. J. Mol. Biol. 160:265-286.
    • (1982) J. Mol. Biol. , vol.160 , pp. 265-286
    • Honzatko, R.B.1    Lipscomb, W.N.2
  • 32
    • 0020540661 scopus 로고
    • Nucleotide sequence of the structural gene pyrB that encodes the catalytic polypeptide of aspartate transcarbamoylase of Escherichia coli
    • Hoover, T. A., W. D. Roof, K. F. Foltermann, G. A. O'Donovan, D. A. Bencini, and J. R. Wild. 1983. Nucleotide sequence of the structural gene pyrB that encodes the catalytic polypeptide of aspartate transcarbamoylase of Escherichia coli. Proc. Natl. Acad. Sci. USA 80:2462-2466.
    • (1983) Proc. Natl. Acad. Sci. USA , vol.80 , pp. 2462-2466
    • Hoover, T.A.1    Roof, W.D.2    Foltermann, K.F.3    O'Donovan, G.A.4    Bencini, D.A.5    Wild, J.R.6
  • 33
    • 0025303523 scopus 로고
    • A reactor permitting injection and sampling for steady state studies of enzymatic reactions at high pressure: Tests with aspartate transcarbamylase
    • Hui Bon Hoa, G., G. Hamel, A. Else, G. Weill, and G. Hervé. 1990. A reactor permitting injection and sampling for steady state studies of enzymatic reactions at high pressure: tests with aspartate transcarbamylase. Anal. Biochem. 187:258-261.
    • (1990) Anal. Biochem. , vol.187 , pp. 258-261
    • Hui Bon Hoa, G.1    Hamel, G.2    Else, A.3    Weill, G.4    Hervé, G.5
  • 34
    • 0025058563 scopus 로고
    • Escherichia coli aspartate transcarbamylase: The molecular basis for a concerted allosteric transition
    • Kantrowitz, E. R., and W. N. Lipscomb. 1990. Escherichia coli aspartate transcarbamylase: the molecular basis for a concerted allosteric transition. Trends Biochem. Sci. 15:53-59.
    • (1990) Trends Biochem. Sci. , vol.15 , pp. 53-59
    • Kantrowitz, E.R.1    Lipscomb, W.N.2
  • 35
    • 0024231301 scopus 로고
    • Complex of N-phosphonacetyl-L-aspartate with aspartate carbamoyltransferase from Escherichia coli
    • Ke, H., W. N. Lipscomb, Y. Cho, and R. B. Honzatko. 1988. Complex of N-phosphonacetyl-L-aspartate with aspartate carbamoyltransferase from Escherichia coli. J. Mol. Biol. 204:725-747.
    • (1988) J. Mol. Biol. , vol.204 , pp. 725-747
    • Ke, H.1    Lipscomb, W.N.2    Cho, Y.3    Honzatko, R.B.4
  • 36
    • 0015505467 scopus 로고
    • An aspartate transcarbamylase lacking catalytic subunit interactions. I. Disconnection of homotropic and heterotropic interactions under the influence of 2-thiouracil
    • Kerbiriou, D., and G. Hervé. 1972. An aspartate transcarbamylase lacking catalytic subunit interactions. I. Disconnection of homotropic and heterotropic interactions under the influence of 2-thiouracil. J. Mol. Biol. 64:379-392.
    • (1972) J. Mol. Biol. , vol.64 , pp. 379-392
    • Kerbiriou, D.1    Hervé, G.2
  • 37
    • 0027399487 scopus 로고
    • Crystal structure of CTP-ligated T-state aspartate transcarbamoylase at 2.5 angstrom resolution: Implications for ATCase mutants and the mechanism of negative cooperativity
    • Kosman, R. P., J. E. Gouaux, and W. N. Lipscomb. 1993. Crystal structure of CTP-ligated T-state aspartate transcarbamoylase at 2.5 angstrom resolution: implications for ATCase mutants and the mechanism of negative cooperativity. Proteins Struct. Funct. Genet. 15:147-176.
    • (1993) Proteins Struct. Funct. Genet. , vol.15 , pp. 147-176
    • Kosman, R.P.1    Gouaux, J.E.2    Lipscomb, W.N.3
  • 38
    • 0023160005 scopus 로고
    • The 2.5 Å structure of aspartate carbamoyltransferase complexed with the bisubstrate analogue N-phosphonacetyl-L-aspartate
    • Krause, K. L., K. W. Volz, and W. N. Lipscomb. 1987. The 2.5 Å structure of aspartate carbamoyltransferase complexed with the bisubstrate analogue N-phosphonacetyl-L-aspartate. J. Mol. Biol. 193:527.
    • (1987) J. Mol. Biol. , vol.193 , pp. 527
    • Krause, K.L.1    Volz, K.W.2    Lipscomb, W.N.3
  • 39
    • 0029000244 scopus 로고
    • Ammonia-dependent synthesis and metabolic channelling of carbamoyl phosphate in the hyperthermophilic archaeon Pyrococcus furiosus
    • Legrain, C., M. Demarez, N. Glansdorff, and A. Piérard. 1995. Ammonia-dependent synthesis and metabolic channelling of carbamoyl phosphate in the hyperthermophilic archaeon Pyrococcus furiosus. Microbiology 141:1093-1099.
    • (1995) Microbiology , vol.141 , pp. 1093-1099
    • Legrain, C.1    Demarez, M.2    Glansdorff, N.3    Piérard, A.4
  • 40
    • 0025129872 scopus 로고
    • Hydrophobic cluster analysis: Procedures to derive structural and functional information from 2-D-representation of protein sequences
    • Lemesle-Varloot, L., B. Henrissat, C. Gaboriaud, V. Bissery, A. Morgat, and J. P. Mornon. 1990. Hydrophobic cluster analysis: procedures to derive structural and functional information from 2-D-representation of protein sequences. Biochimie 72:555-574.
    • (1990) Biochimie , vol.72 , pp. 555-574
    • Lemesle-Varloot, L.1    Henrissat, B.2    Gaboriaud, C.3    Bissery, V.4    Morgat, A.5    Mornon, J.P.6
  • 41
    • 0023025283 scopus 로고
    • Cloning and structure of the Bacillus subtilis aspartate transcarbamylase gene pyrB
    • Lerner, G. C., and R. L. Switzer. 1986. Cloning and structure of the Bacillus subtilis aspartate transcarbamylase gene pyrB. J. Biol. Chem. 261:11156-11165.
    • (1986) J. Biol. Chem. , vol.261 , pp. 11156-11165
    • Lerner, G.C.1    Switzer, R.L.2
  • 42
    • 0028144138 scopus 로고
    • Aspartate transcarbamylase from Escherichia coli: Activity and regulation
    • Lipscomb, W. N. 1994. Aspartate transcarbamylase from Escherichia coli: activity and regulation. Adv. Enzymol. Relat. Areas Mol. Biol. 68:67-151.
    • (1994) Adv. Enzymol. Relat. Areas Mol. Biol. , vol.68 , pp. 67-151
    • Lipscomb, W.N.1
  • 43
    • 0029129081 scopus 로고
    • As in Saccharomyces cerevisiae, aspartate transcarbamoylase is assembled on a multifunctional protein including a dihydroorotase-like cryptic domain in Schizosaccharomyces pombe
    • Lollier, M., L. Jaquet, T. Nedeva, F. Lacroute, S. Potier, and J. L. Souciet. 1995. As in Saccharomyces cerevisiae, aspartate transcarbamoylase is assembled on a multifunctional protein including a dihydroorotase-like cryptic domain in Schizosaccharomyces pombe. Curr. Genet. 28:138-149.
    • (1995) Curr. Genet. , vol.28 , pp. 138-149
    • Lollier, M.1    Jaquet, L.2    Nedeva, T.3    Lacroute, F.4    Potier, S.5    Souciet, J.L.6
  • 44
    • 0024553087 scopus 로고
    • Molecular evolution of enzyme structure: Construction of a hybrid hamster/Escherichia coli aspartate transcarbamoylase
    • Major, J. G., M. E. Wales, J. E. Houghton, J. A. Maley, J. N. Davidson, and J. R. Wild. 1989. Molecular evolution of enzyme structure: construction of a hybrid hamster/Escherichia coli aspartate transcarbamoylase. J. Mol. Evol. 28:442-450.
    • (1989) J. Mol. Evol. , vol.28 , pp. 442-450
    • Major, J.G.1    Wales, M.E.2    Houghton, J.E.3    Maley, J.A.4    Davidson, J.N.5    Wild, J.R.6
  • 45
    • 0027255479 scopus 로고
    • Structural and genetic analysis of protein stability
    • Matthews, B. W. 1993. Structural and genetic analysis of protein stability. Annu. Rev. Biochem. 62:139-160.
    • (1993) Annu. Rev. Biochem. , vol.62 , pp. 139-160
    • Matthews, B.W.1
  • 46
    • 0014707511 scopus 로고
    • Hybridization of native and chemically modified enzymes, III: The catalytic subunits of aspartate transcarbamylase
    • Meighen, E. A., V. Pigiet, and H. K. Schachman. 1970. Hybridization of native and chemically modified enzymes, III: the catalytic subunits of aspartate transcarbamylase. Proc. Natl. Acad. Sci. USA 67:234-241.
    • (1970) Proc. Natl. Acad. Sci. USA , vol.67 , pp. 234-241
    • Meighen, E.A.1    Pigiet, V.2    Schachman, H.K.3
  • 47
    • 0020362615 scopus 로고
    • A new pair of M13 vectors for selecting either DNA strand of double-digest restriction fragments
    • Messing, J., and J. Vieira. 1982. A new pair of M13 vectors for selecting either DNA strand of double-digest restriction fragments. Gene 19:269-276.
    • (1982) Gene , vol.19 , pp. 269-276
    • Messing, J.1    Vieira, J.2
  • 48
    • 0023261180 scopus 로고
    • Cloning, nucleotide sequence and expression of the pyrBI operon of Salmonella typhimurium LT2
    • Michaels, G., R. A. Kelln, and F. E. Nargang. 1987. Cloning, nucleotide sequence and expression of the pyrBI operon of Salmonella typhimurium LT2. Eur. J. Biochem. 166:55-61.
    • (1987) Eur. J. Biochem. , vol.166 , pp. 55-61
    • Michaels, G.1    Kelln, R.A.2    Nargang, F.E.3
  • 49
    • 0024371505 scopus 로고
    • The primary structure of the aspartate transcarbamylase region of the URA2 gene product in Saccharomyces cerevisiae. Features involved in activities and in nuclear localization
    • Nagy, M., M. Le Gouar, S. Potier, J. L. Souciet, and G. Hervé. 1989. The primary structure of the aspartate transcarbamylase region of the URA2 gene product in Saccharomyces cerevisiae. Features involved in activities and in nuclear localization. J. Biol. Chem. 264:8366-8374.
    • (1989) J. Biol. Chem. , vol.264 , pp. 8366-8374
    • Nagy, M.1    Le Gouar, M.2    Potier, S.3    Souciet, J.L.4    Hervé, G.5
  • 50
    • 0028342548 scopus 로고
    • Heterospecific cloning of Arabidopsis thaliana cDNAs by direct complementation of pyrimidine auxotrophic mutants of Saccharomyces cerevisiae. I. Cloning and sequence analysis of two cDNAs catalysing the second, fifth and sixth steps of the de novo pyrimidine biosynthesis pathway
    • Nasr, F., N. Bertauche, M. E. Dufour, M. Minet, and F. Lacroute. 1994. Heterospecific cloning of Arabidopsis thaliana cDNAs by direct complementation of pyrimidine auxotrophic mutants of Saccharomyces cerevisiae. I. Cloning and sequence analysis of two cDNAs catalysing the second, fifth and sixth steps of the de novo pyrimidine biosynthesis pathway. Mol. Gen. Genet. 244:23-32.
    • (1994) Mol. Gen. Genet. , vol.244 , pp. 23-32
    • Nasr, F.1    Bertauche, N.2    Dufour, M.E.3    Minet, M.4    Lacroute, F.5
  • 51
    • 0014757386 scopus 로고
    • A general method applicable to the search for similarities in the amino acid sequence of two proteins
    • Needleman, S. B., and C. D. Wunsch. 1970. A general method applicable to the search for similarities in the amino acid sequence of two proteins. J. Mol. Biol. 48:443-453.
    • (1970) J. Mol. Biol. , vol.48 , pp. 443-453
    • Needleman, S.B.1    Wunsch, C.D.2
  • 52
    • 0026010011 scopus 로고
    • Analysis of the interaction between charged side chains and the α-helix dipole using designed thermostable mutants of phage T4 lysozyme
    • Nicholson, H., D. E. Anderson, S. Dao-Pin, and B. W. Matthews. 1991. Analysis of the interaction between charged side chains and the α-helix dipole using designed thermostable mutants of phage T4 lysozyme. Biochemistry 30:9816-9828.
    • (1991) Biochemistry , vol.30 , pp. 9816-9828
    • Nicholson, H.1    Anderson, D.E.2    Dao-Pin, S.3    Matthews, B.W.4
  • 53
    • 0024273441 scopus 로고
    • Enhanced protein thermostability from designed mutations that interact with α-helix dipoles
    • Nicholson, H., W. J. Becktel, and B. W. Matthews. 1988. Enhanced protein thermostability from designed mutations that interact with α-helix dipoles. Nature 336:651-656.
    • (1988) Nature , vol.336 , pp. 651-656
    • Nicholson, H.1    Becktel, W.J.2    Matthews, B.W.3
  • 54
    • 0015580688 scopus 로고
    • Kinetics and regulation of the salt-dependent aspartate transcarbamylase of Halobacterium cutirubrum
    • Norberg, P., J. G. Kaplan, and D. J. Kuschner. 1973. Kinetics and regulation of the salt-dependent aspartate transcarbamylase of Halobacterium cutirubrum. J. Bacteriol. 113:680-686.
    • (1973) J. Bacteriol. , vol.113 , pp. 680-686
    • Norberg, P.1    Kaplan, J.G.2    Kuschner, D.J.3
  • 55
    • 0022382162 scopus 로고
    • Superproduction and rapid purification of Escherichia coli aspartate transcarbamylase and its catalytic subunit under extreme derepression of the pyrimidine pathway
    • Nowlan, S. F., and E. R. Kantrowitz. 1985. 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) J. Biol. Chem. , vol.260 , pp. 14712-14716
    • Nowlan, S.F.1    Kantrowitz, E.R.2
  • 56
    • 0027248124 scopus 로고
    • The Asc locus for resistance to Alternaria stem canker in tomato does not encode the enzyme aspartate carbamoyltransferase
    • Overduin, B., S. A. Hogenhout, E. A. Vanderbiezen, M. A. Haring, H. J. J. Nijkamp, and J. Hille. 1993. The Asc locus for resistance to Alternaria stem canker in tomato does not encode the enzyme aspartate carbamoyltransferase. Mol. Gen. Genet. 240:43-48.
    • (1993) Mol. Gen. Genet. , vol.240 , pp. 43-48
    • Overduin, B.1    Hogenhout, S.A.2    Vanderbiezen, E.A.3    Haring, M.A.4    Nijkamp, H.J.J.5    Hille, J.6
  • 57
    • 0029004590 scopus 로고
    • Protein modeling by E-mail
    • Peitsch, M. C. 1995. Protein modeling by E-mail. Biotechnology 13:658-660.
    • (1995) Biotechnology , vol.13 , pp. 658-660
    • Peitsch, M.C.1
  • 58
    • 0030053370 scopus 로고    scopus 로고
    • PpoMod and Swiss-Model: Internet-based tools for automated comparative protein modeling
    • Peitsch, M. C. 1996. PpoMod and Swiss-Model: Internet-based tools for automated comparative protein modeling. Biochem. Soc. Trans. 24:274-279.
    • (1996) Biochem. Soc. Trans. , vol.24 , pp. 274-279
    • Peitsch, M.C.1
  • 59
    • 0015506189 scopus 로고
    • Biosynthesis of Escherichia coli aspartate transcarbamylase. I. Parameters of gene expression and sequential biosynthesis of the subunits
    • Perbal, B., and G. Hervé. 1972. Biosynthesis of Escherichia coli aspartate transcarbamylase. I. Parameters of gene expression and sequential biosynthesis of the subunits. J. Mol. Biol. 70:511-529.
    • (1972) J. Mol. Biol. , vol.70 , pp. 511-529
    • Perbal, B.1    Hervé, G.2
  • 61
    • 0028146899 scopus 로고
    • The catalytic and regulatory properties of aspartate transcarbamoylase from Pyrococcus abyssi, a new deep-sea hyperthermophilic archaebacterium
    • Purcarea, C., G. Erauso, D. Prieur, and G. Hervé. 1994. The catalytic and regulatory properties of aspartate transcarbamoylase from Pyrococcus abyssi, a new deep-sea hyperthermophilic archaebacterium. Microbiology 140:1967-1975.
    • (1994) Microbiology , vol.140 , pp. 1967-1975
    • Purcarea, C.1    Erauso, G.2    Prieur, D.3    Hervé, G.4
  • 62
    • 0024290472 scopus 로고
    • Amino acid preferences for specific locations at the ends of a helices
    • Richardson, J. S., and D. C. Richardson. 1988. Amino acid preferences for specific locations at the ends of a helices. Science 240:1648-1652.
    • (1988) Science , vol.240 , pp. 1648-1652
    • Richardson, J.S.1    Richardson, D.C.2
  • 63
    • 0027291015 scopus 로고
    • Prediction of protein secondary structure at better than 70% accuracy
    • Rost, B., and C. Sander. 1993. Prediction of protein secondary structure at better than 70% accuracy. J. Mol. Biol. 232:584-599.
    • (1993) J. Mol. Biol. , vol.232 , pp. 584-599
    • Rost, B.1    Sander, C.2
  • 64
    • 0028300741 scopus 로고
    • Combining evolutionary information and neutral networks to predict protein secondary structure
    • Rost, B., and C. Sander. 1994. Combining evolutionary information and neutral networks to predict protein secondary structure. Proteins 19:55-77.
    • (1994) Proteins , vol.19 , pp. 55-77
    • Rost, B.1    Sander, C.2
  • 65
    • 0028158628 scopus 로고
    • PHD - A mail server for protein secondary structure prediction
    • Rost, B., C. Sander, and R. Schneider. 1994. PHD - a mail server for protein secondary structure prediction. CABIOS 10:53-60.
    • (1994) CABIOS , vol.10 , pp. 53-60
    • Rost, B.1    Sander, C.2    Schneider, R.3
  • 66
    • 0026030641 scopus 로고
    • Database of homology-derived structures and the structural meaning of sequence alignement
    • Sander, C., and R. Schneider. 1991. Database of homology-derived structures and the structural meaning of sequence alignement. Proteins 9:56-68.
    • (1991) Proteins , vol.9 , pp. 56-68
    • Sander, C.1    Schneider, R.2
  • 68
    • 0342416706 scopus 로고
    • Location of amino acid alterations in mutants of aspartate transcarbamoylase: Structural aspects of interallelic complementation
    • Schachman, H. K., C. D. Pauza, M. Navre, M. J. Karels, L. Wu, and Y. R. Yang. 1984. Location of amino acid alterations in mutants of aspartate transcarbamoylase: structural aspects of interallelic complementation. Proc. Natl. Acad. Sci. USA 81:115-119.
    • (1984) Proc. Natl. Acad. Sci. USA , vol.81 , pp. 115-119
    • Schachman, H.K.1    Pauza, C.D.2    Navre, M.3    Karels, M.J.4    Wu, L.5    Yang, Y.R.6
  • 69
    • 0028969125 scopus 로고
    • Aspartate transcarbamoylase genes of Pseudomonas putida: Requirement for an inactive dihydroorotase for assembly into the dodecameric holoenzyme
    • Schurr, M. J., J. F. Vickrey, A. P. Kumar, A. L. Campbell, R. Cunin, R. C. Benjamin, M. S. Shanley, and G. A. O'Donovan. 1995. Aspartate transcarbamoylase genes of Pseudomonas putida: requirement for an inactive dihydroorotase for assembly into the dodecameric holoenzyme. J. Bacteriol. 177:1751-1759.
    • (1995) J. Bacteriol. , vol.177 , pp. 1751-1759
    • Schurr, M.J.1    Vickrey, J.F.2    Kumar, A.P.3    Campbell, A.L.4    Cunin, R.5    Benjamin, R.C.6    Shanley, M.S.7    O'Donovan, G.A.8
  • 70
    • 1842466357 scopus 로고
    • Mammalian aspartate transcarbamylase ATCase: Sequence of the ATCase domain and interdomain linker in the CAD multifunctional polypeptide and properties of the isolated domain
    • Simmer, J. P., R. E. Kelly, J. L. Scully, D. R. Grayson, A. G. Rinker, Jr., S. T. Bergh, and D. R. Evans. 1989. Mammalian aspartate transcarbamylase ATCase: sequence of the ATCase domain and interdomain linker in the CAD multifunctional polypeptide and properties of the isolated domain. Proc. Natl. Acad. Sci. USA 86:4382-4386.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 4382-4386
    • Simmer, J.P.1    Kelly, R.E.2    Scully, J.L.3    Grayson, D.R.4    Rinker Jr., A.G.5    Bergh, S.T.6    Evans, D.R.7
  • 71
    • 0024339081 scopus 로고
    • Organization of the yeast URA2 gene: Identification of a defective dihydroorotase like domain in the multifunctional complex carbamylphosphate synthetase-aspartate transcarbamylase
    • Souciet, J. L., M. Nagy, M. Le Gouar, F. Lacroute, and S. Potier. 1989. Organization of the yeast URA2 gene: identification of a defective dihydroorotase like domain in the multifunctional complex carbamylphosphate synthetase-aspartate transcarbamylase. Gene 79:59-70.
    • (1989) Gene , vol.79 , pp. 59-70
    • Souciet, J.L.1    Nagy, M.2    Le Gouar, M.3    Lacroute, F.4    Potier, S.5
  • 72
    • 0025852356 scopus 로고
    • Escherichia coli aspartate carbamoyltransferase: The probing of crystal structure analysis via site-specific mutagenesis
    • Stevens, R. C., Y. M. Chook, C. Y. Cho, W. N. Lipscomb, and E. R. Kantrowitz. 1991. Escherichia coli aspartate carbamoyltransferase: the probing of crystal structure analysis via site-specific mutagenesis. Protein Eng. 4:391-408.
    • (1991) Protein Eng. , vol.4 , pp. 391-408
    • Stevens, R.C.1    Chook, Y.M.2    Cho, C.Y.3    Lipscomb, W.N.4    Kantrowitz, E.R.5
  • 73
    • 0025002987 scopus 로고
    • Structural consequences of effector binding to the T-state of aspartate carbamoyltransferase: Crystal structures of the unligated and ATP- and CTP-complexed enzymes at 2.6 a resolution
    • Stevens, R. C., J. E. Gouaux, and W. N. Lipscomb. 1990. Structural consequences of effector binding to the T-state of aspartate carbamoyltransferase: crystal structures of the unligated and ATP-and CTP-complexed enzymes at 2.6 A resolution. Biochemistry 29:7691-7701.
    • (1990) Biochemistry , vol.29 , pp. 7691-7701
    • Stevens, R.C.1    Gouaux, J.E.2    Lipscomb, W.N.3
  • 74
    • 0026729135 scopus 로고
    • A molecular mechanism for pyrimidine and purine nucleotide control of aspartate transcarbamoylase
    • Stevens, R. C., and W. N. Lipscomb. 1992. A molecular mechanism for pyrimidine and purine nucleotide control of aspartate transcarbamoylase. Proc. Natl. Acad. Sci. USA 89:5281-5285.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 5281-5285
    • Stevens, R.C.1    Lipscomb, W.N.2
  • 76
    • 84907034779 scopus 로고
    • Genes encoding thermophilic aspartate carbamoyltransferases of Thermus aquaticus ZO5 and Thermotoga maritima MSB8: Modes of expression in E. coli and properties of their products
    • Van de Casteele, M., M. Demarez, C. Legrain, C. Chen, P. G. Van Lierde, A. Piérard, and N. Glansdorff. 1994. Genes encoding thermophilic aspartate carbamoyltransferases of Thermus aquaticus ZO5 and Thermotoga maritima MSB8: modes of expression in E. coli and properties of their products. Biocatalysis 11:165-179.
    • (1994) Biocatalysis , vol.11 , pp. 165-179
    • Van De Casteele, M.1    Demarez, M.2    Legrain, C.3    Chen, C.4    Van Lierde, P.G.5    Piérard, A.6    Glansdorff, N.7
  • 78
    • 0019036679 scopus 로고
    • Heat stability of a tetrameric enzyme, D-glyceraldehyde-3-phosphate dehydrogenase
    • Walker, J. E., A. J. Wonacott, and J. I. Harris. 1980. Heat stability of a tetrameric enzyme, D-glyceraldehyde-3-phosphate dehydrogenase. Eur. J. Biochem. 108:581-586.
    • (1980) Eur. J. Biochem. , vol.108 , pp. 581-586
    • Walker, J.E.1    Wonacott, A.J.2    Harris, J.I.3
  • 79
    • 0025104532 scopus 로고
    • Molecular evolution and genetic engineering of protein domains involving aspartate transcarbamoylase
    • Wild, J. R., and M. E. Wales. 1990. Molecular evolution and genetic engineering of protein domains involving aspartate transcarbamoylase. Annu. Rev. Microbiol. 44:193-218.
    • (1990) Annu. Rev. Microbiol. , vol.44 , pp. 193-218
    • Wild, J.R.1    Wales, M.E.2
  • 80
    • 0014426672 scopus 로고
    • Crystallographic determination of symmetry of aspartate transcarbamylase
    • Wiley, D. C., and W. N. Lipscomb. 1968. Crystallographic determination of symmetry of aspartate transcarbamylase. Nature (London) New Biol. 218: 1119-1121.
    • (1968) Nature (London) New Biol. , vol.218 , pp. 1119-1121
    • Wiley, D.C.1    Lipscomb, W.N.2
  • 81
    • 0027623005 scopus 로고
    • Characterization of an aspartate transcarbamoylase cDNA from pea Pisum salivum 1
    • Williamson, C. L., and R. D. Slocum. 1993. Characterization of an aspartate transcarbamoylase cDNA from pea Pisum salivum 1. Plant Physiol. 102: 1055-1056.
    • (1993) Plant Physiol. , vol.102 , pp. 1055-1056
    • Williamson, C.L.1    Slocum, R.D.2
  • 82
    • 0028357717 scopus 로고
    • Isolation of cDNA clones by complementation of E. coli mutants with infective pBluescript phagemid libraries
    • Williamson, C. L., and R. D. Slocum. 1994. Isolation of cDNA clones by complementation of E. coli mutants with infective pBluescript phagemid libraries. BioTechniques 16:986-987.
    • (1994) BioTechniques , vol.16 , pp. 986-987
    • Williamson, C.L.1    Slocum, R.D.2
  • 84
    • 0028108702 scopus 로고
    • The activation of Escherichia coli aspartate transcarbamylase by ATP. Specific involvement of helix H2′ at the hydrophobic interface between the two domains of the regulatory chains
    • Xi, X. G., C. De Staercke, F. Van Vliet, F. Triniolles, A. Jacobs, P. P. Stas, M. M. Ladjimi, V. Simon, R. Cunin, and G. Hervé. 1994. The activation of Escherichia 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) J. Mol. Biol. , vol.242 , pp. 139-149
    • Xi, X.G.1    De Staercke, C.2    Van Vliet, F.3    Triniolles, F.4    Jacobs, A.5    Stas, P.P.6    Ladjimi, M.M.7    Simon, V.8    Cunin, R.9    Hervé, G.10
  • 85
    • 0025861489 scopus 로고
    • The cooperative interactions between the catalytic sites in Escherichia coli aspartate transcarbamylase: Role of the C-terminal region of the regulatory chains
    • Xi, X. G., F. Van Vliet, M. M. Ladjimi, B. De Wannedmaeker, C. De Staercke, N. Glansdorff, A. Piérard, R. Cunin, and G. Hervé. 1991. The cooperative interactions between the catalytic sites in Escherichia coli aspartate transcarbamylase: role of the C-terminal region of the regulatory chains. J. Mol. Biol. 220:789-799.
    • (1991) J. Mol. Biol. , vol.220 , pp. 789-799
    • Xi, X.G.1    Van Vliet, F.2    Ladjimi, M.M.3    De Wannedmaeker, B.4    De Staercke, C.5    Glansdorff, N.6    Piérard, A.7    Cunin, R.8    Hervé, G.9
  • 86
    • 0020370144 scopus 로고
    • Effect of single amino acid substitutions at the same position on stability of a two-domain protein
    • Yutani, K., K. Ogasahara, A. Kimura, and Y. Sugino. 1982. Effect of single amino acid substitutions at the same position on stability of a two-domain protein. J. Mol. Biol. 160:387-390.
    • (1982) J. Mol. Biol. , vol.160 , pp. 387-390
    • Yutani, K.1    Ogasahara, K.2    Kimura, A.3    Sugino, Y.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.