메뉴 건너뛰기




Volumn 236, Issue 1, 1996, Pages 283-293

Catabolic ornithine carbamoyltransferase of Pseudomonas aeruginosa - Importance of the N-terminal region for dodecameric structure and homotropic carbamoylphosphate cooperativity

Author keywords

Allosteric; Ornithine carbamoyltransferase

Indexed keywords

CARBAMOYL PHOSPHATE; HYBRID PROTEIN; ORNITHINE CARBAMOYLTRANSFERASE;

EID: 0029864712     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1432-1033.1996.00283.x     Document Type: Article
Times cited : (17)

References (43)
  • 1
    • 0023369209 scopus 로고
    • Primary and quaternary structure of the catabolic ornithine carbamoyltransferase from Pseudomonas aeruginosa., Extensive sequence homology with the anabolic ornithine carbamoyltransferase of Escherichia coli
    • Baur, H., Stalon, V., Falmagne, P., Lüthi, E. & Haas, D. (1987) Primary and quaternary structure of the catabolic ornithine carbamoyltransferase from Pseudomonas aeruginosa., Extensive sequence homology with the anabolic ornithine carbamoyltransferase of Escherichia coli, Eur. J. Biochem. 166, 111–117.
    • (1987) Eur. J. Biochem. , vol.166 , pp. 111-117
    • Baur, H.1    Stalon, V.2    Falmagne, P.3    Lüthi, E.4    Haas, D.5
  • 2
    • 0024584223 scopus 로고
    • Sequence analysis and expression of the arginine deiminase and carbamate kinase genes of Pseudomonas aeruginosa
    • Baur, H., Lüthi, E., Stalon, V., Mercenier, A. & Haas, D. (1989) Sequence analysis and expression of the arginine deiminase and carbamate kinase genes of Pseudomonas aeruginosa, Eur. J. Biochem. 179, 53–60.
    • (1989) Eur. J. Biochem. , vol.179 , pp. 53-60
    • Baur, H.1    Lüthi, E.2    Stalon, V.3    Mercenier, A.4    Haas, D.5
  • 3
    • 0024998366 scopus 로고
    • Converting catabolic ornithine carbamoyltransferase to an anabolic enzyme
    • Baur, H., Tricot, C., Stalon, V. & Haas, D. (1990) Converting catabolic ornithine carbamoyltransferase to an anabolic enzyme, J. Biol Chem. 265, 14728–14731.
    • (1990) J. Biol Chem. , vol.265 , pp. 14728-14731
    • Baur, H.1    Tricot, C.2    Stalon, V.3    Haas, D.4
  • 4
    • 0003769049 scopus 로고
    • X‐PLOR, a system for X‐ray crystallography and NMR
    • Brünger, A. T. (1992) X‐PLOR, a system for X‐ray crystallography and NMR, Yale University Press, New Haven CT.
    • (1992)
    • Brünger, A.T.1
  • 5
    • 0018416690 scopus 로고
    • Cloning and endonuclease restriction analysis of argF, and of the control region of the argECBH, bipolar operon in Escherichia coli
    • Crabeel, M., Charlier, D., Cunin, R. & Glansdorff, N. (1979) Cloning and endonuclease restriction analysis of argF, and of the control region of the argECBH, bipolar operon in Escherichia coli, Gene 5, 207–231.
    • (1979) Gene , vol.5 , pp. 207-231
    • Crabeel, M.1    Charlier, D.2    Cunin, R.3    Glansdorff, N.4
  • 6
    • 0023709234 scopus 로고
    • A one‐tube plasmid DNA mini‐preparation suitable for sequencing
    • Del Sal, G., Manfioletti, G. & Schneider, C. (1988) A one‐tube plasmid DNA mini‐preparation suitable for sequencing, Nucleic Acids Res. 16, 9878.
    • (1988) Nucleic Acids Res. , vol.16 , pp. 9878
    • Del Sal, G.1    Manfioletti, G.2    Schneider, C.3
  • 7
    • 0021967278 scopus 로고
    • Immunological and structural relatedness of catabolic ornithine carbamoyltranstferases and the anabolic enzmes of enterobacteriaceae
    • Falmagne, P., Portetelle, D. & Stalon, V. (1985) Immunological and structural relatedness of catabolic ornithine carbamoyltranstferases and the anabolic enzmes of enterobacteriaceae, J. Bacteriol. 161, 714–719.
    • (1985) J. Bacteriol. , vol.161 , pp. 714-719
    • Falmagne, P.1    Portetelle, D.2    Stalon, V.3
  • 8
    • 0025453157 scopus 로고
    • High efficiency electroporation of Pseudomonas aeruginosa, using frozen cell suspensions
    • Farinha, M. A. & Kropinski, A. (1990) High efficiency electroporation of Pseudomonas aeruginosa, using frozen cell suspensions, FEMS Microbiol. Lett. 70, 221–226.
    • (1990) FEMS Microbiol. Lett. , vol.70 , pp. 221-226
    • Farinha, M.A.1    Kropinski, A.2
  • 9
    • 0026487172 scopus 로고
    • RNA processing modulates expression of the arcDABC, operon in Pseudomonas aeruginosa
    • Gamper, M., Ganter, B., Polito, M. R. & Haas, D. (1992) RNA processing modulates expression of the arcDABC, operon in Pseudomonas aeruginosa, J. Mol. Biol. 226, 943–957.
    • (1992) J. Mol. Biol. , vol.226 , pp. 943-957
    • Gamper, M.1    Ganter, B.2    Polito, M.R.3    Haas, D.4
  • 10
    • 0017744884 scopus 로고
    • The genetic organization of arginine biosynthesis in Pseudomonas aeruginosa
    • Haas, D., Holloway, B. W., Schamböck, A. & Leisinger, T. (1977) The genetic organization of arginine biosynthesis in Pseudomonas aeruginosa, Mol. Gen. Genet. 154, 7–22.
    • (1977) Mol. Gen. Genet. , vol.154 , pp. 7-22
    • Haas, D.1    Holloway, B.W.2    Schamböck, A.3    Leisinger, T.4
  • 11
    • 0018673918 scopus 로고
    • Genetic and physiological characterization of Pseudomonas aeruginosa, mutants affected in the catabolic ornithine carbamoyltransferase
    • Haas, D., Evans, R., Mercenier, A., Simon, J. P. & Stalon, V. (1979) Genetic and physiological characterization of Pseudomonas aeruginosa, mutants affected in the catabolic ornithine carbamoyltransferase, J. Bacteriol. 139, 713–720.
    • (1979) J. Bacteriol. , vol.139 , pp. 713-720
    • Haas, D.1    Evans, R.2    Mercenier, A.3    Simon, J.P.4    Stalon, V.5
  • 12
    • 0024024569 scopus 로고
    • Anabolic ornithine carbamoyltransferase of Pseudomonas aeruginosa: Nucleotide sequence and transcriptional control of the argF, structural gene
    • Itoh, Y., Soldati, L., Stalon, V., Falmagne, P., Terawaki, Y., Leisinger, T. & Haas, D. (1988). Anabolic ornithine carbamoyltransferase of Pseudomonas aeruginosa: Nucleotide sequence and transcriptional control of the argF, structural gene, J. Bacteriol. 170, 2725–2734.
    • (1988) J. Bacteriol. , vol.170 , pp. 2725-2734
    • Itoh, Y.1    Soldati, L.2    Stalon, V.3    Falmagne, P.4    Terawaki, Y.5    Leisinger, T.6    Haas, D.7
  • 14
    • 0022371102 scopus 로고
    • Substrate specificity and protonation state of ornithine transcarbamylase as determined by pH studies
    • Kuo, L. C., Herzberg, W. & Lipscomb, W. N. (1985). Substrate specificity and protonation state of ornithine transcarbamylase as determined by pH studies, Biochemistry 24, 4754–4761.
    • (1985) Biochemistry , vol.24 , pp. 4754-4761
    • Kuo, L.C.1    Herzberg, W.2    Lipscomb, W.N.3
  • 15
    • 0024978522 scopus 로고
    • X‐ray diffraction analysis on single crystals of recombinant Escherichia coli, ornithine transcarbamoylase
    • Kuo, L. C. & Seaton, B. A. (1989) X‐ray diffraction analysis on single crystals of recombinant Escherichia coli, ornithine transcarbamoylase, J. Biol. Chem. 264, 16246–16248.
    • (1989) J. Biol. Chem. , vol.264 , pp. 16246-16248
    • Kuo, L.C.1    Seaton, B.A.2
  • 16
    • 0024397566 scopus 로고
    • Triggering of allostery in an enzyme by point mutation: ornithine transcarbamoylase
    • Kuo, L. C., Zambidis, I. & Caron, C. (1989) Triggering of allostery in an enzyme by point mutation: ornithine transcarbamoylase, Science 245, 522–524.
    • (1989) Science , vol.245 , pp. 522-524
    • Kuo, L.C.1    Zambidis, I.2    Caron, C.3
  • 17
    • 0017293245 scopus 로고
    • Ornithine carbamoyltransferase from Escherichia coli W
    • Legrain, C. & Stalon, V. (1976) Ornithine carbamoyltransferase from Escherichia coli W, Eur. J. Biochem. 63, 289–301.
    • (1976) Eur. J. Biochem. , vol.63 , pp. 289-301
    • Legrain, C.1    Stalon, V.2
  • 18
    • 0025881316 scopus 로고
    • Molecular size and symmetry of Pseudomonas aeruginosa, catabolic ornithine carbamoyltransferase. An X‐ray crystallography analysis
    • Marcq, S., Diaz‐Ruano, A., Charlier, P., Dideberg, O., Tricot, C., Piérard, A. & Stalon, V. (1991) Molecular size and symmetry of Pseudomonas aeruginosa, catabolic ornithine carbamoyltransferase. An X‐ray crystallography analysis, J. Mol. Biol. 220, 9–12.
    • (1991) J. Mol. Biol. , vol.220 , pp. 9-12
    • Marcq, S.1    Diaz‐Ruano, A.2    Charlier, P.3    Dideberg, O.4    Tricot, C.5    Piérard, A.6    Stalon, V.7
  • 19
    • 0025000043 scopus 로고
    • Sequence of the argF, gene encoding ornithine transcarbamoylase from Neisseria gonorrhoeae
    • Martin, P. R., Cooperider, J. W. & Mulks, M. H. (1990) Sequence of the argF, gene encoding ornithine transcarbamoylase from Neisseria gonorrhoeae, Gene 94, 139–140.
    • (1990) Gene , vol.94 , pp. 139-140
    • Martin, P.R.1    Cooperider, J.W.2    Mulks, M.H.3
  • 20
    • 0017768878 scopus 로고
    • Lamboid phages that simplify the recovery of in vitro recombinants
    • Murray, N. E., Brammar, W. J. & Murray, K. (1977) Lamboid phages that simplify the recovery of in vitro recombinants, Mol. Gen. Genet. 150, 53–61.
    • (1977) Mol. Gen. Genet. , vol.150 , pp. 53-61
    • Murray, N.E.1    Brammar, W.J.2    Murray, K.3
  • 21
    • 0028173008 scopus 로고
    • Methionine‐321 in the C‐terminal α‐helix of catabolic ornithine carbamoyltransferase from Pseudomonas aeruginosa is important for positive homotropic cooperativity
    • Nguyen, V. T., Tricot, C., Stalon, V., Dideberg, O., Villeret, V. & Haas, D. (1994) Methionine‐321 in the C‐terminal α‐helix of catabolic ornithine carbamoyltransferase from Pseudomonas aeruginosa is important for positive homotropic cooperativity. FEMS Microbiol. Lett. 124, 411–418.
    • (1994) FEMS Microbiol. Lett. , vol.124 , pp. 411-418
    • Nguyen, V.T.1    Tricot, C.2    Stalon, V.3    Dideberg, O.4    Villeret, V.5    Haas, D.6
  • 22
    • 0018894398 scopus 로고
    • Stabilization and purification of ornithine transcarbamoylase from Neisseria gonorrhoeae
    • Powers, C. N. & Pierson, D. L. (1980) Stabilization and purification of ornithine transcarbamoylase from Neisseria gonorrhoeae, J. Bacteriol. 141, 544–549.
    • (1980) J. Bacteriol. , vol.141 , pp. 544-549
    • Powers, C.N.1    Pierson, D.L.2
  • 23
    • 0019841516 scopus 로고
    • The plasmid cloning vector pBR325 contains a 482 base‐pair‐long inverted duplication
    • Prentki, P., Karch, F., Iida, S. & Meyer, J. (1981) The plasmid cloning vector pBR325 contains a 482 base‐pair‐long inverted duplication, Gene 14, 289–299.
    • (1981) Gene , vol.14 , pp. 289-299
    • Prentki, P.1    Karch, F.2    Iida, S.3    Meyer, J.4
  • 24
    • 0014622121 scopus 로고
    • Modified methods for the determination of carbamylaspartate
    • 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
  • 25
    • 0023112502 scopus 로고
    • Mode of replicon fusion mediated by the duplicated insertion sequence IS21 in Escherichia coli
    • Reimmann, C. & Haas, D. (1987) Mode of replicon fusion mediated by the duplicated insertion sequence IS21 in Escherichia coli, Genetics 115, 619–625.
    • (1987) Genetics , vol.115 , pp. 619-625
    • Reimmann, C.1    Haas, D.2
  • 26
    • 0021839517 scopus 로고
    • Transposon insertion mutagenesis of Pseudomonas aeruginosa, with a Tn5 derivative: application to physical mapping of the arc gene cluster
    • Rella, M., Mercenier, A. & Haas, D. (1985) Transposon insertion mutagenesis of Pseudomonas aeruginosa, with a Tn5 derivative: application to physical mapping of the arc gene cluster, Gene 33, 293–303.
    • (1985) Gene , vol.33 , pp. 293-303
    • Rella, M.1    Mercenier, A.2    Haas, D.3
  • 27
    • 0004136246 scopus 로고
    • Molecular cloning, a laboratory manual
    • Sambrook, J., Fritsch, E. F. & Maniatis, T. (1989) Molecular cloning, a laboratory manual (2nd edn) Cold Spring Harbor Laboratory Press, Cold Spring Harbor NY.
    • (1989)
    • Sambrook, J.1    Fritsch, E.F.2    Maniatis, T.3
  • 28
    • 0014208217 scopus 로고
    • The occurrence of a catabolic and an anabolic ornithine carbamoyltransferase in Pseudomonas
    • Stalon, V., Ramos, F., Piérard, A. & Wiame, J. M. (1967) The occurrence of a catabolic and an anabolic ornithine carbamoyltransferase in Pseudomonas, Biochim. Biophys. Acta 139, 91–97.
    • (1967) Biochim. Biophys. Acta , vol.139 , pp. 91-97
    • Stalon, V.1    Ramos, F.2    Piérard, A.3    Wiame, J.M.4
  • 29
    • 0015515028 scopus 로고
    • Regulation of the catabolic ornithine carbamoyltransferase of Pseudomonas fluorescens: a comparison with the anabolic transferase and a mutationally modified catabolic transferase
    • 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 a mutationally modified catabolic transferase, Eur. J. Biochem. 29, 25–35.
    • (1972) Eur. J. Biochem. , vol.29 , pp. 25-35
    • Stalon, V.1    Ramos, F.2    Piérard, A.3    Wiame, J.M.4
  • 30
    • 0017623937 scopus 로고
    • Anabolic ornithine carbamoyltransferase of Pseudomonas
    • Stalon, V., Legrain, C. & Wiame, J. M. (1977) Anabolic ornithine carbamoyltransferase of Pseudomonas, Eur. J. Biochem. 74, 319–327.
    • (1977) Eur. J. Biochem. , vol.74 , pp. 319-327
    • Stalon, V.1    Legrain, C.2    Wiame, J.M.3
  • 31
    • 0015294303 scopus 로고
    • A mutant sex factor of Pseudomonas aeruginosa
    • Stanisich, V. & Holloway, B. (1972) A mutant sex factor of Pseudomonas aeruginosa, Genet. Res. 19, 91–108.
    • (1972) Genet. Res. , vol.19 , pp. 91-108
    • Stanisich, V.1    Holloway, B.2
  • 32
    • 0026591727 scopus 로고
    • Conversion of the noncooperative Bacillus subtilis asparate transcarbamoylase into a cooperative enzyme by a single amino acid substitution
    • Stebbins, J. W. & Kantrowitz, E. R. (1992) Conversion of the noncooperative Bacillus subtilis asparate transcarbamoylase into a cooperative enzyme by a single amino acid substitution, Biochemistry 31, 2328–2332.
    • (1992) Biochemistry , vol.31 , pp. 2328-2332
    • Stebbins, J.W.1    Kantrowitz, E.R.2
  • 33
  • 34
    • 0027197457 scopus 로고
    • Steady‐state kinetics and analysis of pH dependence on wild‐type and a modified allosteric Pseudomonas aeruginosa ornithine carbamoyltransferase containing the replacement of glutamate 105 by alanine
    • Tricot, C., Nguyen, V. T. & Stalon, V. (1993) Steady‐state kinetics and analysis of pH dependence on wild‐type and a modified allosteric Pseudomonas aeruginosa ornithine carbamoyltransferase containing the replacement of glutamate 105 by alanine, Eur. J. Biochem. 215, 833–839.
    • (1993) Eur. J. Biochem. , vol.215 , pp. 833-839
    • Tricot, C.1    Nguyen, V.T.2    Stalon, V.3
  • 35
    • 0028202520 scopus 로고
    • Catabolic ornithine carbamoyltransferase of Pseudomonas aeruginosa. Changes of allosteric properties resulting from modifications at the C‐terminus
    • Tricot, C., Schmid, S., Baur, H., Villeret, V., Dideberg, O., Haas, D. & Stalon, V. (1994) Catabolic ornithine carbamoyltransferase of Pseudomonas aeruginosa. Changes of allosteric properties resulting from modifications at the C‐terminus, Eur. J. Biochem. 221, 555–561.
    • (1994) Eur. J. Biochem. , vol.221 , pp. 555-561
    • Tricot, C.1    Schmid, S.2    Baur, H.3    Villeret, V.4    Dideberg, O.5    Haas, D.6    Stalon, V.7
  • 36
    • 0021664042 scopus 로고
    • Pseudomonas aeruginosa, mutants affected in anaerobic growth on arginine: evidence for a four‐gene cluster encoding the arginine deiminase pathway
    • Vander Wauven, C., Piérard, A., Klay‐Raymann, M. & Haas, D. (1984) Pseudomonas aeruginosa, mutants affected in anaerobic growth on arginine: evidence for a four‐gene cluster encoding the arginine deiminase pathway, J. Bacteriol. 160, 928–934.
    • (1984) J. Bacteriol. , vol.160 , pp. 928-934
    • Vander Wauven, C.1    Piérard, A.2    Klay‐Raymann, M.3    Haas, D.4
  • 37
    • 0021759590 scopus 로고
    • Evolutionary divergence of genes for ornithine and aspartate carbamoyltransferases: complete sequence and mode of regulation of the Escherichia coli argF gene; comparison of argF with argI and pyrB
    • Van Vliet, F., Cunin, R., Jacobs, A., Piette, J., Gigot, D., Lauwereys, A., Piérard, A. & Glansdorff, N. (1984) Evolutionary divergence of genes for ornithine and aspartate carbamoyltransferases: complete sequence and mode of regulation of the Escherichia coli argF gene; comparison of argF with argI and pyrB, Nucleic Acids Res. 12, 6277–6289.
    • (1984) Nucleic Acids Res. , vol.12 , pp. 6277-6289
    • Van Vliet, F.1    Cunin, R.2    Jacobs, A.3    Piette, J.4    Gigot, D.5    Lauwereys, A.6    Piérard, A.7    Glansdorff, N.8
  • 38
    • 0025809486 scopus 로고
    • New pUC‐derived cloning vectors with different selectable markers and DNA replication origins
    • Vieira, J. & Messing, J. (1991). New pUC‐derived cloning vectors with different selectable markers and DNA replication origins, Gene 100, 189–194.
    • (1991) Gene , vol.100 , pp. 189-194
    • Vieira, J.1    Messing, J.2
  • 39
    • 85120510688 scopus 로고
    • Villeret, V. (1994) Ph.D. thesis, Université de Liège.
    • (1994)
    • Villeret, V.1
  • 40
    • 0028881913 scopus 로고
    • Crystal structure of Pseudomonas aeruginosa catabolic ornithine carbamoyltransferase at 3.0 Å resolution. A different oligomeric organization in the transcarbamoylase family
    • Villeret, V., Tricot, C., Stalon, V. & Dideberg, O. (1995) Crystal structure of Pseudomonas aeruginosa catabolic ornithine carbamoyltransferase at 3.0 Å resolution. A different oligomeric organization in the transcarbamoylase family, Proc. Natl Acad. Sci. USA 92, 10762–10766.
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 10762-10766
    • Villeret, V.1    Tricot, C.2    Stalon, V.3    Dideberg, O.4
  • 41
    • 0025104532 scopus 로고
    • Molecular evolution and genetic engineering of protein domains involving aspartate transcarbamoylase
    • Wild, J. R. & Wales, M. E. (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
  • 42
    • 0021943518 scopus 로고
    • Improved M13 phage cloning vectors and host strains: nucleotide sequences of the M13mp18 and pUC19 vectors
    • Yanisch‐Perron, C., Vieira, J. & Messing, J. (1985) Improved M13 phage cloning vectors and host strains: nucleotide sequences of the M13mp18 and pUC19 vectors, Gene 33, 103–119.
    • (1985) Gene , vol.33 , pp. 103-119
    • Yanisch‐Perron, C.1    Vieira, J.2    Messing, J.3
  • 43
    • 0019507999 scopus 로고
    • Characterization of P1argF derivatives from Escherichia coli K12 transduction
    • York, M. K. & Stodolsky, M. (1981) Characterization of P1 argF derivatives from Escherichia coli K12 transduction, Mol. Gen. Genet. 181, 230–240.
    • (1981) Mol. Gen. Genet. , vol.181 , pp. 230-240
    • York, M.K.1    Stodolsky, M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.