메뉴 건너뛰기




Volumn 142, Issue 7, 1996, Pages 1873-1879

A reappraisal of the diversity and class distribution of aspartate transcarbamoylases in Gram-negative bacteria

Author keywords

Aspartate transcarbamoylase; Molecular evolution; Phylogeny

Indexed keywords

ASPARTATE CARBAMOYLTRANSFERASE;

EID: 0029884319     PISSN: 13500872     EISSN: None     Source Type: Journal    
DOI: 10.1099/13500872-142-7-1873     Document Type: Article
Times cited : (6)

References (25)
  • 1
    • 0014851604 scopus 로고
    • Protein analysis by electrophoretic molecular sieving in a gel of graded porosity
    • Arcus, A. C. (1970). Protein analysis by electrophoretic molecular sieving in a gel of graded porosity. Anal Biochem 37, 53-63.
    • (1970) Anal Biochem , vol.37 , pp. 53-63
    • Arcus, A.C.1
  • 2
    • 0027373260 scopus 로고
    • Subunit structure of class A aspartate transcarbamoylase from Pseudomonas fluorescens
    • Bergh, S. T. & Evans, D. E. (1993). Subunit structure of class A aspartate transcarbamoylase from Pseudomonas fluorescens. Proc Natl Acad Sci USA 90, 9819-9822.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 9819-9822
    • Bergh, S.T.1    Evans, D.E.2
  • 3
    • 0014602890 scopus 로고
    • Molecular size and feedback-regulation characteristics of bacterial aspartate transcarbamylases
    • Bethell, M. R. & 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
  • 4
    • 0016752552 scopus 로고
    • Purification and properties of Bacillus subtilis aspartate transcarbamylase
    • Brabson, 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
    • Brabson, J.S.1    Switzer, R.L.2
  • 5
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of proteins utilizing the principle of protein-dye binding
    • Bradford, M. M. (1976). A rapid and sensitive method for the quantitation of microgram quantities of proteins utilizing the principle of protein-dye binding. Anal Biochem 72, 248-254.
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 6
    • 0022580816 scopus 로고
    • Evolution of aromatic biosynthesis and functional phylogenetic positioning of Azomonas, Azotobacfer and rRNA group I pseudomonads
    • Byng, G. S., Berry, A. & Jensen, R. A. (1986). Evolution of aromatic biosynthesis and functional phylogenetic positioning of Azomonas, Azotobacfer and rRNA group I pseudomonads. Arch Microbiol 144, 222-227.
    • (1986) Arch Microbiol , vol.144 , pp. 222-227
    • Byng, G.S.1    Berry, A.2    Jensen, R.A.3
  • 7
    • 0015953773 scopus 로고
    • Aspartate transcarbamoylase from Streptococcus faecalis. Purification, properties and nature of an allosteric activator site
    • Chang, T.-Y. (1974). Aspartate transcarbamoylase from Streptococcus faecalis. Purification, properties and nature of an allosteric activator site. Biochemistry 13, 629-638.
    • (1974) Biochemistry , vol.13 , pp. 629-638
    • Chang, T.-Y.1
  • 8
    • 0027564279 scopus 로고
    • The evolutionary history of the first three enzymes in pyrimidine biosynthesis
    • Davidson, J. N., Chen, C. C., Jamison, R. S., Musmanno, L. A. & Kern, C. B. (1993). The evolutionary history of the first three enzymes in pyrimidine biosynthesis. BioEssays 15, 157-164.
    • (1993) BioEssays , vol.15 , pp. 157-164
    • Davidson, J.N.1    Chen, C.C.2    Jamison, R.S.3    Musmanno, L.A.4    Kern, C.B.5
  • 9
    • 0018823403 scopus 로고
    • Intra- and intergenic similarities of ribosomal ribonucleic acid cistrons of free-living nitrogen-fixing bacteria
    • DeSmedt, J., Bauwens, M., Tygat, R. & Deley, J. (1980). Intra- and intergenic similarities of ribosomal ribonucleic acid cistrons of free-living nitrogen-fixing bacteria. Int J Syst Bacteriol 30, 106-112.
    • (1980) Int J Syst Bacteriol , vol.30 , pp. 106-112
    • DeSmedt, J.1    Bauwens, M.2    Tygat, R.3    Deley, J.4
  • 10
    • 0019869568 scopus 로고
    • Regulatory variance of aspartate transcarbamoylase among strains of Yersinia enterocolitica and Yersinia enterocolitica-like organisms
    • Foltermann, K. F., Wild, J. R., Zink, D. L. & O'Donovan, G. A. (1981). Regulatory variance of aspartate transcarbamoylase among strains of Yersinia enterocolitica and Yersinia enterocolitica-like organisms. Curr Microbiol 6, 43-47.
    • (1981) Curr Microbiol , vol.6 , pp. 43-47
    • Foltermann, K.F.1    Wild, J.R.2    Zink, D.L.3    O'Donovan, G.A.4
  • 11
    • 0014216815 scopus 로고
    • The purification of aspartate transcarbamylase of Escherichia coli and separation of its protein subunits
    • Gerhart, J. C. & Holoubek, H. (1967). The purification of aspartate transcarbamylase of Escherichia coli and separation of its protein subunits. J Biol Chem 242, 2886-2892.
    • (1967) J Biol Chem , vol.242 , pp. 2886-2892
    • Gerhart, J.C.1    Holoubek, H.2
  • 12
    • 0018536455 scopus 로고
    • Wheat germ aspartate transcarbamylase. Purification and cold lability
    • Grayson, J. E., Yon, R. J. & Butterworth, P. J. (1979). Wheat germ aspartate transcarbamylase. Purification and cold lability. Biochem J 183, 239-245.
    • (1979) Biochem J , vol.183 , pp. 239-245
    • Grayson, J.E.1    Yon, R.J.2    Butterworth, P.J.3
  • 13
    • 0025058563 scopus 로고
    • Escherichia coli aspartate transcarbamoylase: The molecular basis for a concerted allosteric transition
    • Kantrowitz, E. R. & Lipscomb, W. N. (1990). Escherichia coli aspartate transcarbamoylase: 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
  • 14
    • 0346054921 scopus 로고
    • Structure of the unligated aspartate carbamoyl transferase of Escherichia coli at 2-6 Å resolution
    • Ke, H.-M., Honzatco, R. B. & Lipscomb, W. N. (1984). Structure of the unligated aspartate carbamoyl transferase of Escherichia coli at 2-6 Å resolution. Proc Natl Acad Sci USA 81, 4037-4040.
    • (1984) Proc Natl Acad Sci USA , vol.81 , pp. 4037-4040
    • Ke, H.-M.1    Honzatco, R.B.2    Lipscomb, W.N.3
  • 15
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. (1970). Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 16
    • 0000794471 scopus 로고
    • VP
    • Edited by P. H. A. Sneath, N. S. Mair, M. E. Sharpe & J. G. Holt. Baltimore: Williams & Wilkins
    • VP. In Bergey's Manual of Systematic Bacteriology, Vol. 2, pp. 1035-1043. Edited by P. H. A. Sneath, N. S. Mair, M. E. Sharpe & J. G. Holt. Baltimore: Williams & Wilkins.
    • (1986) Bergey's Manual of Systematic Bacteriology , vol.2 , pp. 1035-1043
    • Murray, R.G.E.1
  • 18
    • 0342416705 scopus 로고
    • Regeneration of active enzyme by formation of hybrids from inactive derivatives: Implications for active sites shared between polypeptide chains of aspartate transcarbamylase
    • Robey, E. A. & Schachman, H. K. (1985). Regeneration of active enzyme by formation of hybrids from inactive derivatives: implications for active sites shared between polypeptide chains of aspartate transcarbamylase. Proc Natl Acad Sci USA 82, 361-365.
    • (1985) Proc Natl Acad Sci USA , vol.82 , pp. 361-365
    • Robey, E.A.1    Schachman, H.K.2
  • 19
    • 0028969125 scopus 로고
    • Aspartate transcarbamoylase genes from Pseudomonas putida: Requirement for an inactive dihydro-orotase for assembly into the dodecameric holoenzyme
    • Schurr, M. J., Vickrey, J. F., Kumar, A. P., Campbell, A. L., Cunin, R., Benjamin, R. C., Shanley, M. S. & O'Donovan, G. A. (1995). Aspartate transcarbamoylase genes from Pseudomonas putida: requirement for an inactive dihydro-orotase 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
  • 20
    • 0027332714 scopus 로고
    • Purification of aspartate transcarbamoylase from Pseudomonas syringas
    • Shepherdson, M. & McPhail, D. (1993). Purification of aspartate transcarbamoylase from Pseudomonas syringas. FEMS Microbiol Lett 114, 201-206.
    • (1993) FEMS Microbiol Lett , vol.114 , pp. 201-206
    • Shepherdson, M.1    McPhail, D.2
  • 21
    • 0024339081 scopus 로고
    • Organisation of the URA2 gene: Identification of a defective dihydroorotase-like domain in the multifunctional carbamoyl phosphate synthetase-aspartate transcarbamoylase complex
    • Souciet, J. L., Nagy, M., Le Gouar, M., Lacroute, F. & Potier, S. (1989). Organisation of the URA2 gene: identification of a defective dihydroorotase-like domain in the multifunctional carbamoyl phosphate synthetase-aspartate transcarbamoylase complex. 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
  • 22
    • 0011313230 scopus 로고
    • De novo pyrimidine nucleotide synthesis
    • Edited by A. L. Sonenshein, J. A. Hoch & R. Losick. Washington, DC: American Society for Microbiology
    • Switzer, R. L. & Quinn, C. L. (1993). De novo pyrimidine nucleotide synthesis. In bacillus subtilis and Other Gram-positive Bacteria, pp. 343-358. Edited by A. L. Sonenshein, J. A. Hoch & R. Losick. Washington, DC: American Society for Microbiology.
    • (1993) Bacillus Subtilis and Other Gram-positive Bacteria , pp. 343-358
    • Switzer, R.L.1    Quinn, C.L.2
  • 23
    • 0019301279 scopus 로고
    • Regulatory divergence of aspartate transcarbamoylases within the Enterobacteriaceae
    • Wild, J. R., Foltermann, K. J. & O'Donovan, G. A. (1980). Regulatory divergence of aspartate transcarbamoylases within the Enterobacteriaceae. Arch Biochem Biophys 201, 506-517.
    • (1980) Arch Biochem Biophys , vol.201 , pp. 506-517
    • Wild, J.R.1    Foltermann, K.J.2    O'Donovan, G.A.3
  • 25
    • 0023184331 scopus 로고
    • Bacterial evolution
    • Woese, C. R. (1987). Bacterial evolution. Microbiol Rev 51, 221-271.
    • (1987) Microbiol Rev , vol.51 , pp. 221-271
    • Woese, C.R.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.