메뉴 건너뛰기




Volumn 182, Issue 13, 2000, Pages 3626-3631

Characterization of a Bordetella pertussis diaminopimelate (DAP) biosynthesis locus identifies dapC, a novel gene coding for an N-succinyl- L,L-DAP aminotransferase

Author keywords

[No Author keywords available]

Indexed keywords

AMINOTRANSFERASE; DIAMINOPIMELIC ACID; PYRIDOXAL 5 PHOSPHATE;

EID: 0034044066     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.182.13.3626-3631.2000     Document Type: Article
Times cited : (25)

References (39)
  • 1
    • 0017277818 scopus 로고
    • Assay of proteins in the presence of interfering materials
    • Bensadoun, A., and U. Weinstein. 1976. Assay of proteins in the presence of interfering materials. Anal. Biochem. 70:241-250.
    • (1976) Anal. Biochem. , vol.70 , pp. 241-250
    • Bensadoun, A.1    Weinstein, U.2
  • 2
    • 0031670734 scopus 로고    scopus 로고
    • Linkage map of Escherichia coli E-12, edition 10: The traditional map
    • Berlyn, M. K. B. 1998. Linkage map of Escherichia coli E-12, edition 10: the traditional map. Microbiol. Mol. Biol. Rev. 62:814-984.
    • (1998) Microbiol. Mol. Biol. Rev. , vol.62 , pp. 814-984
    • Berlyn, M.K.B.1
  • 4
    • 0026758369 scopus 로고
    • Cloning, characterization, and expression of the dapE gene of Escherichia coli
    • Bouvier, J., C. Richaud, W. Higgins, C. Bogler, and P. Stragier. 1992. Cloning, characterization, and expression of the dapE gene of Escherichia coli. J. Bacteriol. 174:5265-5271.
    • (1992) J. Bacteriol. , vol.174 , pp. 5265-5271
    • Bouvier, J.1    Richaud, C.2    Higgins, W.3    Bogler, C.4    Stragier, P.5
  • 5
    • 0015029675 scopus 로고
    • Genetic analysis of diaminopimelic acid-and lysine-requiring mutants of Escherihia coli
    • Bukhari, A. I., and A. L. Taylor. 1971. Genetic analysis of diaminopimelic acid-and lysine-requiring mutants of Escherihia coli. J. Bacteriol. 105:844-854.
    • (1971) J. Bacteriol. , vol.105 , pp. 844-854
    • Bukhari, A.I.1    Taylor, A.L.2
  • 6
    • 0027448979 scopus 로고
    • A phase variant of Bordetella pertussis with a mutation in a new locus involved in the regulation of pertussis toxin and adenylate cyclase toxin expression
    • Carbonelti, N. H., N. Khelef, N. Guiso, and R. Gross. 1993. A phase variant of Bordetella pertussis with a mutation in a new locus involved in the regulation of pertussis toxin and adenylate cyclase toxin expression. J. Bacteriol. 175:6679-6688.
    • (1993) J. Bacteriol. , vol.175 , pp. 6679-6688
    • Carbonelti, N.H.1    Khelef, N.2    Guiso, N.3    Gross, R.4
  • 7
    • 0024399681 scopus 로고
    • Biological activities and chemical composition of purified tracheal cytotoxin of Bordetella pertussis
    • Cookson, B. T., C. Hwei-Ling, L. A. Herwaldt, and W. E. Goldman. 1989. Biological activities and chemical composition of purified tracheal cytotoxin of Bordetella pertussis. Infect. Immun. 57:2223-2229.
    • (1989) Infect. Immun. , vol.57 , pp. 2223-2229
    • Cookson, B.T.1    Hwei-Ling, C.2    Herwaldt, L.A.3    Goldman, W.E.4
  • 8
    • 0029782572 scopus 로고    scopus 로고
    • Synthesis and evaluation of novel substrates and inhibitors of N-succinyl-L,L-diaminopimelate aminotransferase (DAP-AT) from Escherichia coli
    • Cox, R. J., W. A. Sherwin, L. K. P. Lam, and J. C. Vederas. 1996. Synthesis and evaluation of novel substrates and inhibitors of N-succinyl-L,L-diaminopimelate aminotransferase (DAP-AT) from Escherichia coli. J. Am. Chem. Soc. 118:7449-7460.
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 7449-7460
    • Cox, R.J.1    Sherwin, W.A.2    Lam, L.K.P.3    Vederas, J.C.4
  • 9
    • 0024513781 scopus 로고
    • Recombinant avirulent Salmonella vaccine strains with stable maintenance and high level expression of cloned genes in vivo
    • Curtiss, R., III, K. Nakayama, and S. M. Kelley. 1989. Recombinant avirulent Salmonella vaccine strains with stable maintenance and high level expression of cloned genes in vivo. Immunol. Investig. 18:583-596.
    • (1989) Immunol. Investig. , vol.18 , pp. 583-596
    • Curtiss R. III1    Nakayama, K.2    Kelley, S.M.3
  • 10
    • 0021760092 scopus 로고
    • A comprehensive set of sequence analysis programs for the VAX
    • Devereux, J., P. Haeberli, and O. Smithies. 1984. A comprehensive set of sequence analysis programs for the VAX. Nucleic Acids Res. 12:387-395.
    • (1984) Nucleic Acids Res. , vol.12 , pp. 387-395
    • Devereux, J.1    Haeberli, P.2    Smithies, O.3
  • 11
    • 0029653518 scopus 로고
    • Whole-genome random sequencing and assembly of Haemophilus influenzae Rd
    • Fleischmann, R. D., M. D. Adams, O. White, et al. 1995. Whole-genome random sequencing and assembly of Haemophilus influenzae Rd. Science 269:496-512.
    • (1995) Science , vol.269 , pp. 496-512
    • Fleischmann, R.D.1    Adams, M.D.2    White, O.3
  • 12
    • 0029744175 scopus 로고    scopus 로고
    • A new gene locus of Bordetella pertussis defines a novel family of prokaryotic transcriptional accessory proteins
    • Fuchs, T. M., H. Deppisch, V. Scarlato, and R. Gross. 1996. A new gene locus of Bordetella pertussis defines a novel family of prokaryotic transcriptional accessory proteins. J. Bacteriol. 178:4445-4452.
    • (1996) J. Bacteriol. , vol.178 , pp. 4445-4452
    • Fuchs, T.M.1    Deppisch, H.2    Scarlato, V.3    Gross, R.4
  • 13
    • 0013945686 scopus 로고
    • The amino acid utilization by phase I Bordetella pertussis in a chemically defined medium
    • Goldner, M., C. M. Jakus, H. K. Rhodes, and R. J. Wilson. 1966. The amino acid utilization by phase I Bordetella pertussis in a chemically defined medium. J. Gen. Microbiol. 44:439-444.
    • (1966) J. Gen. Microbiol. , vol.44 , pp. 439-444
    • Goldner, M.1    Jakus, C.M.2    Rhodes, H.K.3    Wilson, R.J.4
  • 14
    • 0025295967 scopus 로고
    • Differential plasmid rescue from transgenic mouse DNAs into Escherichia coli methylation-restriction mutants
    • Grant, S. G., J. Jessee, F. R. Bloom, and D. Hanaban. 1990. Differential plasmid rescue from transgenic mouse DNAs into Escherichia coli methylation-restriction mutants. Proc. Natl. Acad. Sci. USA 87:4645-4649.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 4645-4649
    • Grant, S.G.1    Jessee, J.2    Bloom, F.R.3    Hanaban, D.4
  • 15
    • 0020972316 scopus 로고
    • o-Phthaldialdehyde precolumn derivatization and reversed-phase high-performance liquid chromatography of polypeptide hydrolysates and physiological fluids
    • Jones, B. N., and J. P. Gilligan. 1983. o-Phthaldialdehyde precolumn derivatization and reversed-phase high-performance liquid chromatography of polypeptide hydrolysates and physiological fluids. J. Chromatogr. 266:471-482.
    • (1983) J. Chromatogr. , vol.266 , pp. 471-482
    • Jones, B.N.1    Gilligan, J.P.2
  • 16
    • 0029655167 scopus 로고
    • Sequence analysis of the genome of the unicellular cyanohacterium Synechocystis sp. Strain PCC 6803. I. Sequence features in the 1 MB region from map position 64% to 92% of the genome
    • Kaneko, T., A. Tanaka, S. Sato, H. Kotani, T. Sazuka, N. Miyajima, M. Sugiura, and S. Tabata. 1995. Sequence analysis of the genome of the unicellular cyanohacterium Synechocystis sp. strain PCC 6803. I. Sequence features in the 1 MB region from map position 64% to 92% of the genome. DNA Res. 2:153-166.
    • (1995) DNA Res. , vol.2 , pp. 153-166
    • Kaneko, T.1    Tanaka, A.2    Sato, S.3    Kotani, H.4    Sazuka, T.5    Miyajima, N.6    Sugiura, M.7    Tabata, S.8
  • 17
    • 0030863414 scopus 로고    scopus 로고
    • Characterization of Helicobacter pylori dapE and construction of a conditionally lethal dapE mutant
    • Karita, M., M. L. Etterbeek, M. H. Forsyth, M. K. R. Tummuru, and M. J. Blaser. 1997. Characterization of Helicobacter pylori dapE and construction of a conditionally lethal dapE mutant. Infect. Immun. 65:4158-4164.
    • (1997) Infect. Immun. , vol.65 , pp. 4158-4164
    • Karita, M.1    Etterbeek, M.L.2    Forsyth, M.H.3    Tummuru, M.K.R.4    Blaser, M.J.5
  • 18
    • 0000705899 scopus 로고
    • N-succinyl-L-α,ε-diaminopimelic acid deacylase
    • Kindler, S. H., and C. Gilvarg. 1960. N-succinyl-L-α,ε-diaminopimelic acid deacylase. J. Biol. Chem. 235:3532-3535.
    • (1960) J. Biol. Chem. , vol.235 , pp. 3532-3535
    • Kindler, S.H.1    Gilvarg, C.2
  • 19
    • 0028302175 scopus 로고
    • Characterization of a 3-dihydroquinase gene from Actinobacter pleuropneumoniae with homology to the eukaryotic cenes qa-2 and QUTE
    • Lalonde, G., P. D. O'Hanley, B. A. Stocker, and K. Denich. 1994. Characterization of a 3-dihydroquinase gene from Actinobacter pleuropneumoniae with homology to the eukaryotic cenes qa-2 and QUTE. Mol. Microbiol. 11:273-280.
    • (1994) Mol. Microbiol. , vol.11 , pp. 273-280
    • Lalonde, G.1    O'Hanley, P.D.2    Stocker, B.A.3    Denich, K.4
  • 20
    • 0033537677 scopus 로고    scopus 로고
    • The dual biosynthetic capability of N-acetylornithine aminotransferase in arginine and Lysine biosynthesis
    • Ledwidge, R., and J. S. Blanchard. 1999. The dual biosynthetic capability of N-acetylornithine aminotransferase in arginine and Lysine biosynthesis. Biochemistry 38:3019-3024.
    • (1999) Biochemistry , vol.38 , pp. 3019-3024
    • Ledwidge, R.1    Blanchard, J.S.2
  • 21
    • 0029018206 scopus 로고
    • Tracheal cytotoxin structural requirements for respiratory epithelial damage in pertussis
    • Luker, K. E., A. N. Tyler, G. R. Marshall, and W. E. Goldman. 1995. Tracheal cytotoxin structural requirements for respiratory epithelial damage in pertussis. Mol. Microbiol. 16:733-743.
    • (1995) Mol. Microbiol. , vol.16 , pp. 733-743
    • Luker, K.E.1    Tyler, A.N.2    Marshall, G.R.3    Goldman, W.E.4
  • 22
    • 0001501761 scopus 로고    scopus 로고
    • Biosynthesis of threonine and lysine
    • F. C. Neidhardt, R. Curtiss III, J. L. Ingraham, E. C. C. Lin, K. B. Low, B. Magasanik, W. S. Reznikoff, M. Riley, M. Schaechter, and H. E. Umbarger (ed.), ASM Press, Washington, D.C.
    • Patte, J.-C. 1996. Biosynthesis of threonine and lysine, p. 528-541. In F. C. Neidhardt, R. Curtiss III, J. L. Ingraham, E. C. C. Lin, K. B. Low, B. Magasanik, W. S. Reznikoff, M. Riley, M. Schaechter, and H. E. Umbarger (ed.), Esfherichia coli and Salmonella, 2nd ed., vol. 1. ASM Press, Washington, D.C.
    • (1996) Esfherichia Coli and Salmonella, 2nd Ed. , vol.1 , pp. 528-541
    • Patte, J.-C.1
  • 23
    • 14444280134 scopus 로고    scopus 로고
    • Cloning of the dapB gene, encoding dihydrodipicolinate reductase, from Mycobacterium tuberculosis
    • Pavelka, M. S., Jr., T. R. Weisbrod, and W. R. Jacobs, Jr. 1997. Cloning of the dapB gene, encoding dihydrodipicolinate reductase, from Mycobacterium tuberculosis. J. Bacteriol. 179:2777-2782.
    • (1997) J. Bacteriol. , vol.179 , pp. 2777-2782
    • Pavelka M.S., Jr.1    Weisbrod, T.R.2    Jacobs W.R., Jr.3
  • 24
    • 0000728798 scopus 로고
    • N-succinyl-L-diaminopimelic-glutamic transaminase
    • Pelerkofsky, B., and C. Gilvarg. 1961. N-succinyl-L-diaminopimelic-glutamic transaminase. J. Biol. Chem. 236:1432-1438.
    • (1961) J. Biol. Chem. , vol.236 , pp. 1432-1438
    • Pelerkofsky, B.1    Gilvarg, C.2
  • 25
    • 0021689428 scopus 로고
    • Regulation of expression and nucleotide sequence of the Escherichia coli dapD gene
    • Richaud, C., F. V. Richaud, C. Martin, C. Haziza, and J.-C. Patte. 1984. Regulation of expression and nucleotide sequence of the Escherichia coli dapD gene. J. Biol. Chem. 259:14824-14828.
    • (1984) J. Biol. Chem. , vol.259 , pp. 14824-14828
    • Richaud, C.1    Richaud, F.V.2    Martin, C.3    Haziza, C.4    Patte, J.-C.5
  • 28
    • 0029958658 scopus 로고    scopus 로고
    • Three-dimensional structure of meso-diaminopimelic acid dehydrogenase from Corynebacterium glutamicum
    • Scapin, G., S. G. Reddy, and J. S. Blanchard. 1996. Three-dimensional structure of meso-diaminopimelic acid dehydrogenase from Corynebacterium glutamicum. Biochemistry 35:13540-13551.
    • (1996) Biochemistry , vol.35 , pp. 13540-13551
    • Scapin, G.1    Reddy, S.G.2    Blanchard, J.S.3
  • 29
    • 0032502243 scopus 로고    scopus 로고
    • Substrate and inhibitor binding sites in Corynebacterium glutamicum diaminopimelate dehydrogenase
    • Scapin, G., M. Cirilli, S. G. Reddy, Y. Gao, J. C. Vederas, and J. S. Blanchard. 1998. Substrate and inhibitor binding sites in Corynebacterium glutamicum diaminopimelate dehydrogenase. Biochemistry 37:3278-3285.
    • (1998) Biochemistry , vol.37 , pp. 3278-3285
    • Scapin, G.1    Cirilli, M.2    Reddy, S.G.3    Gao, Y.4    Vederas, J.C.5    Blanchard, J.S.6
  • 31
    • 0021027842 scopus 로고
    • A broad host range mobilization system for in vivo genetic engineering: Transposon mutagenesis in gram negative bacteria
    • Simon, R., U. Priefer, and A. Pühler. 1983. A broad host range mobilization system for in vivo genetic engineering: transposon mutagenesis in gram negative bacteria. Biotechnology 1:784-791.
    • (1983) Biotechnology , vol.1 , pp. 784-791
    • Simon, R.1    Priefer, U.2    Pühler, A.3
  • 32
    • 0029824741 scopus 로고    scopus 로고
    • Sequence analysis of the Bacillus subtilis chromosome region between the serA and kdg loci cloned in a yeast artificial chromosome
    • Sorokin, A., V. Azevedo, E. Zumstein, N. Galleron, S. D. Ehrlich, and P. Serror. 1996. Sequence analysis of the Bacillus subtilis chromosome region between the serA and kdg loci cloned in a yeast artificial chromosome. Microbiology 142:2005-2016.
    • (1996) Microbiology , vol.142 , pp. 2005-2016
    • Sorokin, A.1    Azevedo, V.2    Zumstein, E.3    Galleron, N.4    Ehrlich, S.D.5    Serror, P.6
  • 33
    • 0014862345 scopus 로고
    • A simple chemically defined medium for the production of phase I Bordetella pertussis
    • Stainer, D. W., and M. J. Scholte. 1970. A simple chemically defined medium for the production of phase I Bordetella pertussis. J. Gen. Microbiol. 63:7501-7510.
    • (1970) J. Gen. Microbiol. , vol.63 , pp. 7501-7510
    • Stainer, D.W.1    Scholte, M.J.2
  • 34
    • 0025893376 scopus 로고
    • Subcellular localization and immunological detection of proteins encoded by the vir locus of Bordetella pertussis
    • Stibitz, S., and M. S. Yang. 1991. Subcellular localization and immunological detection of proteins encoded by the vir locus of Bordetella pertussis. J. Bacteriol. 174:4288-4296.
    • (1991) J. Bacteriol. , vol.174 , pp. 4288-4296
    • Stibitz, S.1    Yang, M.S.2
  • 36
    • 0030835739 scopus 로고    scopus 로고
    • The complete genome sequence of the gastric pathogen Helicohacter pylori
    • Tomb, J. F., O. White, A. R. Kerlavage, et al. 1997. The complete genome sequence of the gastric pathogen Helicohacter pylori. Nature 388:539-547.
    • (1997) Nature , vol.388 , pp. 539-547
    • Tomb, J.F.1    White, O.2    Kerlavage, A.R.3
  • 37
    • 0031750104 scopus 로고    scopus 로고
    • Different modes of diaminopimelate synthesis and their role in cell wall integrity: A study with Corynebacterium glutamicum
    • Wehrmann, A., B. Phillip, H. Sahm, and L. Eggeling. 1998. Different modes of diaminopimelate synthesis and their role in cell wall integrity: a study with Corynebacterium glutamicum. J. Bacteriol. 180:3159-3165.
    • (1998) J. Bacteriol. , vol.180 , pp. 3159-3165
    • Wehrmann, A.1    Phillip, B.2    Sahm, H.3    Eggeling, L.4
  • 38
    • 0014705659 scopus 로고
    • Bacterial distribution of the use of succinyl and acetyl blocking groups in diaminopimelic acid biosynthesis
    • Weinberger, S., and C. Gilvarg. 1970. Bacterial distribution of the use of succinyl and acetyl blocking groups in diaminopimelic acid biosynthesis. J. Bacteriol. 101:323-324.
    • (1970) J. Bacteriol. , vol.101 , pp. 323-324
    • Weinberger, S.1    Gilvarg, C.2
  • 39
    • 0342891007 scopus 로고
    • A new naturally occurring amino acid
    • Work, E. 1950. A new naturally occurring amino acid. Nature 165:74-75.
    • (1950) Nature , vol.165 , pp. 74-75
    • Work, E.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.