메뉴 건너뛰기




Volumn 264, Issue 1, 1999, Pages 233-241

Aspartate carbamoyltransferase from the thermoacidophilic archaeon Sulfolobus acidocaldarius: Cloning, sequence analysis, enzyme purification and characterization

Author keywords

Aspartate carbamoyltransferase; Protein purification; PyrB; PyrI; Sulfolobus acidocaldarius

Indexed keywords

ASPARTATE CARBAMOYLTRANSFERASE;

EID: 0033567285     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1327.1999.00619.x     Document Type: Article
Times cited : (11)

References (51)
  • 1
    • 0025104532 scopus 로고
    • Molecular evolution and genetic engineering of protein domains involving aspartate carbamoylase
    • 1. Wild, J.R. & Wales, M. (1990). Molecular evolution and genetic engineering of protein domains involving aspartate carbamoylase. Annu. Rev. Microbiol. 44, 193-218.
    • (1990) Annu. Rev. Microbiol. , vol.44 , pp. 193-218
    • Wild, J.R.1    Wales, M.2
  • 2
    • 0016752552 scopus 로고
    • Purification and properties of Bacillus subtilis aspartate transcarbamylase
    • 2. Brahson, J.S. & Switzer, R.L. (1975). Purification and properties of Bacillus subtilis aspartate transcarbamylase. J. Biol. Chem. 250, 8664-8669.
    • (1975) J. Biol. Chem. , vol.250 , pp. 8664-8669
    • Brahson, J.S.1    Switzer, R.L.2
  • 3
    • 0025779288 scopus 로고
    • Molecular structure of Bacillus subtilis aspartate transcarbamoylase at 3.0 Å resolution
    • 3. Stevens, R.C., Reinich, K.M. & Lipscomb, W.N. (1991). Molecular structure of Bad/lux suhtilis aspartate transcarbamoylase at 3.0 Å resolution. Proc. Natl Acad. Sci. USA 88, 6087-6091.
    • (1991) Proc. Natl Acad. Sci. USA , vol.88 , pp. 6087-6091
    • Stevens, R.C.1    Reinich, K.M.2    Lipscomb, W.N.3
  • 4
    • 0014602890 scopus 로고
    • Molecular size and feedback regulation characteristics of bacterial aspartate transcarbamylases
    • 4. Bethell, MR. & Jones, M.E. (1969). Molecular size and feedback regulation characteristics of bacterial aspartate transcarbamylases. Arch. Biochem. Biophys. 134, 352-365.
    • (1969) Arch. Biochem. Biophys. , vol.134 , pp. 352-365
    • Bethell, M.R.1    Jones, M.E.2
  • 5
    • 0031280518 scopus 로고    scopus 로고
    • Molecular physiology of carbamoylation under extreme conditions: What can we learn from extreme thermophilic microorganisms?
    • 5. Van de Casteele, M., Legrain, C., Desmarez, M., Chen, P.G., Piérard, A. & Glansdorff, N. (1997). Molecular physiology of carbamoylation under extreme conditions: what can we learn from extreme thermophilic microorganisms? Comp. Biochem. Physiol. 118, 463-473.
    • (1997) Comp. Biochem. Physiol. , vol.118 , pp. 463-473
    • Van De Casteele, M.1    Legrain, C.2    Desmarez, M.3    Chen, P.G.4    Piérard, A.5    Glansdorff, N.6
  • 6
    • 0027373260 scopus 로고
    • Subunit structure of a class A aspartate transcarbamoylase from Pseudomonas fluorescens
    • 6. Bergh, S.T. & Evans, D.R. (1993). Subunit structure of a class A aspartate transcarbamoylase from Pseudomonas fluorescens. Proc. Natl Acad. Sci. USA 90, 9818-9822.
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 9818-9822
    • Bergh, S.T.1    Evans, D.R.2
  • 7
    • 0013784860 scopus 로고
    • Distinct subunits for the regulation and catalytic activity of aspartate transcarbamylase
    • 7. Gerhart, J.C. & Schachman, H.K. (1965). Distinct subunits for the regulation and catalytic activity of aspartate transcarbamylase. Biochemistry 4, 1054-1062.
    • (1965) Biochemistry , vol.4 , pp. 1054-1062
    • Gerhart, J.C.1    Schachman, H.K.2
  • 8
    • 0031750455 scopus 로고    scopus 로고
    • Aspartate carbamoyltransferase from a psychrophilic deep-sea bacterium, Vibrio strain 2693. Properties of the enzyme, genetic organization and synthesis in Escherichia coli
    • 8. Xu, Y., Zhang, Y., Liang, Z., Van de Casteele, M., Legrain, C. & Glansdorff, N. (1998). 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) Microbiology , vol.144 , pp. 1435-1441
    • Xu, Y.1    Zhang, Y.2    Liang, Z.3    Van De Casteele, M.4    Legrain, C.5    Glansdorff, N.6
  • 9
    • 0028144138 scopus 로고
    • Aspartate transcarbamylase from Escherichia coli: Activity and regulation
    • 9. Lipscomb, W.N. (1994). Aspartate transcarbamylase from Escherichia coli: activity and regulation. Adv. Enzymol. 68, 67-152.
    • (1994) Adv. Enzymol. , vol.68 , pp. 67-152
    • Lipscomb, W.N.1
  • 10
    • 0020587010 scopus 로고
    • Amino acid sequence of the catalytic subunit of aspartate transcarbamoylase from Escherichia coli
    • 10. Konigsberg, W.H. & Henderson, L. (1983). Amino acid sequence of the catalytic subunit of aspartate transcarbamoylase from Escherichia coli. Proc. Natl Acad. Sci. USA 80, 2467-2471.
    • (1983) Proc. Natl Acad. Sci. USA , vol.80 , pp. 2467-2471
    • Konigsberg, W.H.1    Henderson, L.2
  • 11
    • 0020540661 scopus 로고
    • Nucleotide sequence of the structural gene (pyrB) that encodes the catalytic polypeptide of aspartate transcarbamoylase of Escherichia coli
    • 11. Hoover, T.A., Roof, W.D., Foltermann, K.F., O'Donovan, G.A., Benconi, D.A. & Wild, J.R. (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    Benconi, D.A.5    Wild, J.R.6
  • 12
    • 0342416706 scopus 로고
    • Location of amino acid alterations in mutants of aspartate transcarbamoylase: Structural aspects of interallelic complementation
    • 12. Schachman, H.K., Pauza, C., Navre, M., Karels, M.J., Wu, L. & Yang, Y.R. (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.2    Navre, M.3    Karels, M.J.4    Wu, L.5    Yang, Y.R.6
  • 13
    • 0014426681 scopus 로고
    • New structural model of E. coli aspartate transcarbamylase and the amino-acid sequence of the regulatory polypeptide chain
    • 13. Weber, K. (1968). New structural model of E. coli aspartate transcarbamylase and the amino-acid sequence of the regulatory polypeptide chain. Nature 218, 1116-1119.
    • (1968) Nature , vol.218 , pp. 1116-1119
    • Weber, K.1
  • 14
    • 0014426672 scopus 로고
    • Crystallographic determination of symmetry of aspartate transcarbamylase
    • 14. Wiley, D.C. & Lipscomb, W.N. (1968). Crystallographic determination of symmetry of aspartate transcarbamylase. Nature (London) 218, 1119-1121.
    • (1968) Nature (London) , vol.218 , pp. 1119-1121
    • Wiley, D.C.1    Lipscomb, W.N.2
  • 15
    • 0023660840 scopus 로고
    • Structural asymmetry in the CTP-liganded form of aspartate carbamoyltransferase from Escherichia coli
    • 15. Kim, K.H., Pan, Z., Honzatko, R.B., Ke, H.-M. & Lipscomb, W.N. (1987). Structural asymmetry in the CTP-liganded form of aspartate carbamoyltransferase from Escherichia coli. J. Mol. Biol. 196, 853-875.
    • (1987) J. Mol. Biol. , vol.196 , pp. 853-875
    • Kim, K.H.1    Pan, Z.2    Honzatko, R.B.3    Ke, H.-M.4    Lipscomb, W.N.5
  • 16
    • 0023160005 scopus 로고
    • 2.5 Å structure of aspartate carbamoyltransferase complexed with bisubstrale analog N-(phosphonoacetyl)-L-aspartate
    • 16. Krause, K.L., Voltz, K.W. & Lipscomb, W.N. (1987). 2.5 Å structure of aspartate carbamoyltransferase complexed with bisubstrale analog N-(phosphonoacetyl)-L-aspartate. J. Mol. Biol. 193, 527-553.
    • (1987) J. Mol. Biol. , vol.193 , pp. 527-553
    • Krause, K.L.1    Voltz, K.W.2    Lipscomb, W.N.3
  • 17
    • 0001738507 scopus 로고
    • Control of pyrimidine biosynthesis in Escherichia coli by a feed-back mechanism
    • 17. Yates, R.A. & Pardee, A.B. (1956). Control of pyrimidine biosynthesis in Escherichia coli by a feed-back mechanism. J. Biol. Chem. 221, 757-770.
    • (1956) J. Biol. Chem. , vol.221 , pp. 757-770
    • Yates, R.A.1    Pardee, A.B.2
  • 18
    • 0005552966 scopus 로고
    • In the presence of CTP, UTP becomes an allosteric inhibitor of aspartate transcarbamoylase
    • 18. Wild, J.R., Loughrey-Chen, S.J. & Corder, T.S. (1989). In the presence of CTP, UTP becomes an allosteric inhibitor of aspartate transcarbamoylase. Proc. Natl Acad. Sci. USA 86, 46-50.
    • (1989) Proc. Natl Acad. Sci. USA , vol.86 , pp. 46-50
    • Wild, J.R.1    Loughrey-Chen, S.J.2    Corder, T.S.3
  • 19
    • 0001425337 scopus 로고
    • The enzymology of control by feedback inhibition
    • 19. Gerhart, J.C. & Pardee, A.B. (1962). The enzymology of control by feedback inhibition. J. Biol. Chem. 237, 891-896.
    • (1962) J. Biol. Chem. , vol.237 , pp. 891-896
    • Gerhart, J.C.1    Pardee, A.B.2
  • 20
    • 0014320526 scopus 로고
    • Carbamyl phosphate: An allosteric substrate for aspartate transcarbamylase of Escherichia coli
    • 20. Bethell, M.R., Smith, K.E., White, J.S. & Jones, M.E. (1968). Carbamyl phosphate: an allosteric substrate for aspartate transcarbamylase of Escherichia coli. Proc. Natl Acad. Sci., USA 60, 1442-1449.
    • (1968) Proc. Natl Acad. Sci., USA , vol.60 , pp. 1442-1449
    • Bethell, M.R.1    Smith, K.E.2    White, J.S.3    Jones, M.E.4
  • 21
    • 0020367718 scopus 로고
    • Interaction of phosphate ligands with Escherichia coli aspartate carbamoyltransferase in the cristalline state
    • 21. Honzatko, R.B. & Lipscomb, W.N. (1982). Interaction of phosphate ligands with Escherichia coli aspartate carbamoyltransferase in the cristalline state. J. Mol. Biol. 160, 265-286.
    • (1982) J. Mol. Biol. , vol.160 , pp. 265-286
    • Honzatko, R.B.1    Lipscomb, W.N.2
  • 22
    • 0029991767 scopus 로고    scopus 로고
    • Hyperthermophilic procaryotes
    • 22. Stetter, K.O. (1996). Hyperthermophilic procaryotes. FEMS Microbiol. Reviews 18, 149-158.
    • (1996) FEMS Microbiol. Reviews , vol.18 , pp. 149-158
    • Stetter, K.O.1
  • 27
    • 0030873134 scopus 로고    scopus 로고
    • Aspartate transcarbamylase from the deep-sea hyperthermophilic archaeon Pyrococcus abyssi: Genetic organisation, structure, and expression in Escherichia coli
    • 27. Purcarea, C., Hervé, G., Ladjimi, M.M. & Cunin, R. (1997). Aspartate transcarbamylase from the deep-sea hyperthermophilic archaeon Pyrococcus abyssi: genetic organisation, structure, and expression in Escherichia coli. J. Bacteriol. 179, 4143-4157.
    • (1997) J. Bacteriol. , vol.179 , pp. 4143-4157
    • Purcarea, C.1    Hervé, G.2    Ladjimi, M.M.3    Cunin, R.4
  • 28
    • 0028146899 scopus 로고
    • The catalytic and regulatory properties of aspartate transcarbamoylase from Pyrococcus abyssi, a new deep-sea hyperthermopilic archaebacterium
    • 28. Purcarea, C., Erauso, G., Prieur, D. & Hervé, G. (1994). The catalytic and regulatory properties of aspartate transcarbamoylase from Pyrococcus abyssi, a new deep-sea hyperthermopilic archaebacterium. Microbiology 140, 1967-75.
    • (1994) Microbiology , vol.140 , pp. 1967-1975
    • Purcarea, C.1    Erauso, G.2    Prieur, D.3    Hervé, G.4
  • 30
    • 0020417643 scopus 로고
    • Genetic selection for reciprocal translocation at chosen chromosomal sites in Saccharomyces cerevisiae
    • 30. Potier, S., Winsor, B. & Lacroute, F. (1982). Genetic selection for reciprocal translocation at chosen chromosomal sites in Saccharomyces cerevisiae. Mol Cell. Biol. 2, 1025-1032.
    • (1982) Mol Cell. Biol. , vol.2 , pp. 1025-1032
    • Potier, S.1    Winsor, B.2    Lacroute, F.3
  • 32
    • 0001572474 scopus 로고
    • Topography of cotransducible arginine mutations in E. coli K12
    • 32. Glansdorff, N. (1965). Topography of cotransducible arginine mutations in E. coli K12. Genetics 51, 167-179.
    • (1965) Genetics , vol.51 , pp. 167-179
    • Glansdorff, N.1
  • 33
    • 0017202874 scopus 로고
    • Regulation of arginine biosynthesis in S. cerevisiae: Isolation of a cis-dominant, constitutive mutant of ornithine carbamoyltransferase synthesis
    • 33. Messenguy, F. (1976). Regulation of arginine biosynthesis in S. cerevisiae: isolation of a cis-dominant, constitutive mutant of ornithine carbamoyltransferase synthesis. J. Bacteriol. 128, 49-55.
    • (1976) J. Bacteriol. , vol.128 , pp. 49-55
    • Messenguy, F.1
  • 35
    • 0014622121 scopus 로고
    • Modified methods for the determination of carbamylaspartate
    • 35. Prescott, L.M. & Jones, M.E. (1969). Modified methods for the determination of carbamylaspartate. Anal Biochem. 32, 408-419.
    • (1969) Anal Biochem. , vol.32 , pp. 408-419
    • Prescott, L.M.1    Jones, M.E.2
  • 36
    • 0015506189 scopus 로고
    • Biosynthesis of Escherichia coli aspartate transcarbamylase
    • 36. Perbal, B. & Hervé, G. (1972). Biosynthesis of Escherichia coli aspartate transcarbamylase. J. Mol. Biol. 70, 511-529.
    • (1972) J. Mol. Biol. , vol.70 , pp. 511-529
    • Perbal, B.1    Hervé, G.2
  • 39
    • 0025016827 scopus 로고
    • Crystal structures of phosphonoacetamide ligated T and phosphoacetamide and malonate ligated R states of ATCase at 2.8-Å resolution and neutral pH
    • 39. Gouaux, J.E. & Lipscomb, W.N. (1990). Crystal structures of phosphonoacetamide ligated T and phosphoacetamide and malonate ligated R states of ATCase at 2.8-Å resolution and neutral pH. Biochemistry 29, 389-402.
    • (1990) Biochemistry , vol.29 , pp. 389-402
    • Gouaux, J.E.1    Lipscomb, W.N.2
  • 41
    • 0023160005 scopus 로고
    • The 2.5 Å structure of aspartate carbamoyltransferase complexed with the bisubstrate analogue N-(phosphonoacetyl)-L-aspartate
    • 41. Krause, K.L., Volz, K.W. & Lipscomb, W.N. (1987). The 2.5 Å structure of aspartate carbamoyltransferase complexed with the bisubstrate analogue N-(phosphonoacetyl)-L-aspartate. J. Mol. Biol. 193, 527-553.
    • (1987) J. Mol. Biol. , vol.193 , pp. 527-553
    • Krause, K.L.1    Volz, K.W.2    Lipscomb, W.N.3
  • 42
    • 0024021799 scopus 로고
    • Three dimentional structure of carbamoylphosphate and succinate bound to aspartate carbamoyltransferase
    • 42. Gouaux, J.E. & Lipscomb, W.N. (1988). Three dimentional structure of carbamoylphosphate 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
  • 43
    • 0025002987 scopus 로고
    • Structural consequences of effector binding to the T-state of aspartate carbamoyltarnsferase: Crystal structures of the unligated and ATP-and CTP-complexed enzymes at 2.6-A resolution
    • 43. Stevens, R.C., Gouaux, J.E. & Lipscomb, W.N. (1990). Structural consequences of effector binding to the T-state of aspartate carbamoyltarnsferase: 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
  • 44
    • 0027399487 scopus 로고
    • Crystal structure of CTP ligated T state aspartate transcarbamoylase at 2.5 Å resolution: Implication for ATCase
    • 44. Kosman, R.P., Gouaux, J.E. & Lipscomb, W.N. (1993). Crystal structure of CTP ligated T state aspartate transcarbamoylase at 2.5 Å resolution: implication for ATCase. Proteins 15, 147-177.
    • (1993) Proteins , vol.15 , pp. 147-177
    • Kosman, R.P.1    Gouaux, J.E.2    Lipscomb, W.N.3
  • 45
    • 0024231301 scopus 로고
    • Complex of N-phosphonacetyl-L-aspartate with aspartate carbamoyltransferasc X ray refinementn analysis of conformational changes and catalytic and allosteric mechanisms
    • 45. Ke, H.-M., Lipscomb, W.N., Cho, Y. & Honzatko, R.B. (1988). Complex of N-phosphonacetyl-L-aspartate with aspartate carbamoyltransferasc X ray refinementn analysis of conformational changes and catalytic and allosteric mechanisms. J. Mol. Biol. 204, 725-747.
    • (1988) J. Mol. Biol. , vol.204 , pp. 725-747
    • Ke, H.-M.1    Lipscomb, W.N.2    Cho, Y.3    Honzatko, R.B.4
  • 46
    • 0030844095 scopus 로고    scopus 로고
    • Cloning and identification of the Sulfolobus solfataricus lrp gene encoding an archaeal homologue of the eubacterial leucine-responsive global transcriptional regulator Lrp
    • 46. Charlier, D., Roovers, M., Thia-Toong, T.-L., Durbecq, V. & Glansdorff, N. (1997). Cloning and identification of the Sulfolobus solfataricus lrp gene encoding an archaeal homologue of the eubacterial leucine-responsive global transcriptional regulator Lrp. Gene 201, 63-68.
    • (1997) Gene , vol.201 , pp. 63-68
    • Charlier, D.1    Roovers, M.2    Thia-Toong, T.-L.3    Durbecq, V.4    Glansdorff, N.5
  • 47
    • 0017104605 scopus 로고
    • Unique aspect of the regulation of the aspartate transcarbamylase of Serratia marcescens
    • 47. Wild, J.R., Belser, W.L. & O'Donovan, G.A. (1976) Unique aspect of the regulation of the aspartate transcarbamylase of Serratia marcescens. J. Bacteriol. 128, 766-775.
    • (1976) J. Bacteriol. , vol.128 , pp. 766-775
    • Wild, J.R.1    Belser, W.L.2    O'Donovan, G.A.3
  • 48
    • 0017894911 scopus 로고
    • The effect of pH on the cooperative behavior of aspartate transcarbamylase from Escherichia coli
    • 48. Pastra-Landis, S.C., Evans, D.R. & Lipscomb, W.N. (1978). The effect of pH on the cooperative behavior of aspartate transcarbamylase from Escherichia coli. J. Biol. Chem. 253, 4624-4630.
    • (1978) J. Biol. Chem. , vol.253 , pp. 4624-4630
    • Pastra-Landis, S.C.1    Evans, D.R.2    Lipscomb, W.N.3
  • 49
    • 0014669702 scopus 로고
    • Aspartate transcarbamylase: Kinetic studies of the catalytic subunit
    • 49. Porter, R.W., Modebe, M.O. & Stark, G.R. (1969). Aspartate transcarbamylase: kinetic studies of the catalytic subunit. J. Biol. Chem. 244, 1846-1859.
    • (1969) J. Biol. Chem. , vol.244 , pp. 1846-1859
    • Porter, R.W.1    Modebe, M.O.2    Stark, G.R.3
  • 50
    • 0014707511 scopus 로고
    • Hybridization of native and chemically modified enzymes. III. The catalytic subunits of aspartate transcarbamylase
    • 50. Meighan, E.A., Pigiet, V.P. & Schachman, H.K. (1970). Hybridization of native and chemically modified enzymes. III. The catalytic subunits of aspartate transcarbamylase. Proc. Natl Acad. Sci. USA 65, 234-241.
    • (1970) Proc. Natl Acad. Sci. USA , vol.65 , pp. 234-241
    • Meighan, E.A.1    Pigiet, V.P.2    Schachman, H.K.3
  • 51
    • 0015505467 scopus 로고
    • Biosynthesis of an aspartate transcarbamylase lacking cooperative interactions. Disconnection of homotropic and heterotropic interaction under influence of 2-thiouracil
    • 51. Kerbiriou, D. & Hervé, G. (1972). Biosynthesis of an aspartate transcarbamylase lacking cooperative interactions. Disconnection of homotropic and heterotropic interaction under 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.