메뉴 건너뛰기




Volumn 178, Issue 22, 1996, Pages 6496-6507

Biosynthesis of diaminopimelate, the precursor of lysine and a component of peptidoglycan, is an essential function of Mycobacterium smegmatis

Author keywords

[No Author keywords available]

Indexed keywords

DIAMINOPIMELIC ACID; LYSINE; PEPTIDOGLYCAN;

EID: 10344230938     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/jb.178.22.6496-6507.1996     Document Type: Article
Times cited : (156)

References (71)
  • 1
    • 0027449968 scopus 로고
    • Cloning of the lysA gene from Mycobacterium tuberculosis
    • Andersen, Å. B., and E. B. Hansen. 1993. Cloning of the lysA gene from Mycobacterium tuberculosis. Gene 124:105-109.
    • (1993) Gene , vol.124 , pp. 105-109
    • Andersen, Å.B.1    Hansen, E.B.2
  • 3
    • 0029895614 scopus 로고    scopus 로고
    • Targeted replacement of the mycocerosic acid synthase gene in Mycobacterium bovis BCG produces a mutant that lacks mycosides
    • Azad, A. K., T. D. Sirakova, L. M. Rogers, and P. E. Kolattukudy. 1996. Targeted replacement of the mycocerosic acid synthase gene in Mycobacterium bovis BCG produces a mutant that lacks mycosides. Proc. Natl. Acad. Sci. USA 93:4787-4792.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 4787-4792
    • Azad, A.K.1    Sirakova, T.D.2    Rogers, L.M.3    Kolattukudy, P.E.4
  • 7
    • 0001060326 scopus 로고
    • Lipids and carbohydrates of Mycobacterium tuberculosis
    • B. R. Bloom (ed.). ASM Press, Washington, D.C.
    • Besra, G. S., and D. Chatterjee. 1994. Lipids and carbohydrates of Mycobacterium tuberculosis, p. 285-306. In B. R. Bloom (ed.), Tuberculosis: pathogenesis, protection, and control. ASM Press, Washington, D.C.
    • (1994) Tuberculosis: Pathogenesis, Protection, and Control , pp. 285-306
    • Besra, G.S.1    Chatterjee, D.2
  • 9
    • 0022002462 scopus 로고
    • Cloning and structure of the gene for the subunits of aspartokinase II from Bacillus subtilis
    • Bondaryk, R. P., and H. Paulus. 1985. Cloning and structure of the gene for the subunits of aspartokinase II from Bacillus subtilis. J. Biol. Chem. 260:585-591.
    • (1985) J. Biol. Chem. , vol.260 , pp. 585-591
    • Bondaryk, R.P.1    Paulus, H.2
  • 10
    • 0021928787 scopus 로고
    • Expression of the gene for Bacillus subtilis aspartokinase II in Escherichia coli
    • Bondaryk, R. P., and H. Paulus. 1985. Expression of the gene for Bacillus subtilis aspartokinase II in Escherichia coli. J. Biol. Chem. 260:592-597.
    • (1985) J. Biol. Chem. , vol.260 , pp. 592-597
    • Bondaryk, R.P.1    Paulus, H.2
  • 11
    • 0014674485 scopus 로고
    • A complementation analysis of the restriction and modification of DNA in Escherichia coli
    • Boyer, H., and D. Roulland-Dussoin. 1969. A complementation analysis of the restriction and modification of DNA in Escherichia coli. J. Mol. Biol. 41:459-472.
    • (1969) J. Mol. Biol. , vol.41 , pp. 459-472
    • Boyer, H.1    Roulland-Dussoin, D.2
  • 12
    • 0000449110 scopus 로고
    • Ultrastructure of Mycobacterium tuberculosis
    • B. R. Bloom (ed.). ASM Press, Washington, D.C.
    • Brennan, P. J., and P. Draper. 1994. Ultrastructure of Mycobacterium tuberculosis, p. 271-284. In B. R. Bloom (ed.), Tuberculosis: pathogenesis, protection, and control. ASM Press, Washington, D.C.
    • (1994) Tuberculosis: Pathogenesis, Protection, and Control , pp. 271-284
    • Brennan, P.J.1    Draper, P.2
  • 15
    • 0019936273 scopus 로고
    • Activities and regulation of the enzymes of lysine biosynthesis in a lysine-excreting strain of Bacillus megaterium
    • Chatterjee, S. P., and P. J. White. 1982. Activities and regulation of the enzymes of lysine biosynthesis in a lysine-excreting strain of Bacillus megaterium. J. Gen. Microbiol. 128:1073-1081.
    • (1982) J. Gen. Microbiol. , vol.128 , pp. 1073-1081
    • Chatterjee, S.P.1    White, P.J.2
  • 16
    • 0026350742 scopus 로고
    • A novel transposon trap for mycobacteria: Isolation and characterization of IS1096
    • Cirillo, J. D., R. G. Barletta, B. R. Bloom, and W. R. Jacobs, Jr. 1991. A novel transposon trap for mycobacteria: isolation and characterization of IS1096. J. Bacteriol. 173:7772-7780.
    • (1991) J. Bacteriol. , vol.173 , pp. 7772-7780
    • Cirillo, J.D.1    Barletta, R.G.2    Bloom, B.R.3    Jacobs Jr., W.R.4
  • 17
    • 2642691113 scopus 로고
    • Efficient electrotransformation of Mycobacterium smegmatis
    • Bio-Rad Laboratories, Richmond, Calif.
    • Cirillo, J. D., T. R. Weisbrod, and W. R. Jacobs, Jr. 1993. Efficient electrotransformation of Mycobacterium smegmatis. Bio-Rad echnical bulletin no. 1360. Bio-Rad Laboratories, Richmond, Calif.
    • (1993) Bio-Rad Echnical Bulletin No. 1360 , vol.1360
    • Cirillo, J.D.1    Weisbrod, T.R.2    Jacobs Jr., W.R.3
  • 18
    • 0028180404 scopus 로고
    • Isolation and characterization of the aspartate semialdehyde dehydrogenase and asparlokinase genes from mycobacteria
    • Cirillo, J. D., T. R. Weisbrod, L. Pascopella, and W. R. Jacobs, Jr. 1994. Isolation and characterization of the aspartate semialdehyde dehydrogenase and asparlokinase genes from mycobacteria. Mol. Microbiol. 11:629-639.
    • (1994) Mol. Microbiol. , vol.11 , pp. 629-639
    • Cirillo, J.D.1    Weisbrod, T.R.2    Pascopella, L.3    Jacobs Jr., W.R.4
  • 19
    • 0024145176 scopus 로고
    • Regulation of enzymes of lysine biosynthesis in Corynebacterium glutamicum
    • Cremer, J., C. Treptow, L. Eggeling, and H. Sahm. 1988. Regulation of enzymes of lysine biosynthesis in Corynebacterium glutamicum. J. Gen. Microbiol. 134:3221-3229.
    • (1988) J. Gen. Microbiol. , vol.134 , pp. 3221-3229
    • Cremer, J.1    Treptow, C.2    Eggeling, L.3    Sahm, H.4
  • 20
    • 0028291730 scopus 로고
    • Global tuberculosis incidence and mortality during 1990-2000
    • Dolin, P. J., M. C. Raviglione, and A. Kochi. 1994. Global tuberculosis incidence and mortality during 1990-2000. Bull. W. H. O. 72:213-220.
    • (1994) Bull. W. H. O. , vol.72 , pp. 213-220
    • Dolin, P.J.1    Raviglione, M.C.2    Kochi, A.3
  • 21
    • 0023195874 scopus 로고
    • Peptidoglycan and arabinogalactan of Mycobacterium leprae
    • Draper, P., O. Kandler, and A. Darbre. 1987. Peptidoglycan and arabinogalactan of Mycobacterium leprae. J. Gen. Microbiol. 133:1187-1194.
    • (1987) J. Gen. Microbiol. , vol.133 , pp. 1187-1194
    • Draper, P.1    Kandler, O.2    Darbre, A.3
  • 23
    • 0027201142 scopus 로고
    • Gene structure and expression of the Corynebacterium flavum N13 ask-asd operon
    • Follettie, M. T., O. P. Peoples, C. Agoropoulo, and A. J. Sinskey. 1993. Gene structure and expression of the Corynebacterium flavum N13 ask-asd operon. J. Bacteriol. 175:4096-4103.
    • (1993) J. Bacteriol. , vol.175 , pp. 4096-4103
    • Follettie, M.T.1    Peoples, O.P.2    Agoropoulo, C.3    Sinskey, A.J.4
  • 24
    • 0014429842 scopus 로고
    • The relationship of dipicolinate and lysine biosynthesis in Bacillus megaterium
    • Fukuda, A., and C. Gilvarg. 1968. The relationship of dipicolinate and lysine biosynthesis in Bacillus megaterium. J. Biol. Chem. 243:3871-3876.
    • (1968) J. Biol. Chem. , vol.243 , pp. 3871-3876
    • Fukuda, A.1    Gilvarg, C.2
  • 25
    • 0025110368 scopus 로고
    • Cloning and characterization of the asd gene of Salmonella typhimurium: Use in stable maintenance of recombinant plasmids in Salmonella vaccine strains
    • Galán, J. E., K. Nakayama, and R. Curtiss III. 1990. Cloning and characterization of the asd gene of Salmonella typhimurium: use in stable maintenance of recombinant plasmids in Salmonella vaccine strains. Gene 94:29-35.
    • (1990) Gene , vol.94 , pp. 29-35
    • Galán, J.E.1    Nakayama, K.2    Curtiss III, R.3
  • 26
    • 0025755803 scopus 로고
    • Cloning and characterization of the Pseudomonas aeruginosa lasR gene, a transcriptional activator of elastase expression
    • Gambello, M. J., and B. H. Iglewski. 1991. Cloning and characterization of the Pseudomonas aeruginosa lasR gene, a transcriptional activator of elastase expression. J. Bacteriol. 173:3000-3009.
    • (1991) J. Bacteriol. , vol.173 , pp. 3000-3009
    • Gambello, M.J.1    Iglewski, B.H.2
  • 27
    • 0014385732 scopus 로고
    • Use of bacteriolytic enzymes in determination of wall structure and their role in cell metabolism
    • Ghuysen, J. M. 1968. Use of bacteriolytic enzymes in determination of wall structure and their role in cell metabolism. Bacteriol. Rev. 32:425-464.
    • (1968) Bacteriol. Rev. , vol.32 , pp. 425-464
    • Ghuysen, J.M.1
  • 28
    • 0028200851 scopus 로고
    • Tuberculosis and acquired immunodeficiency syndrome: A historical perspective on recent developments
    • Haas, D. W., and R. M. Des Prez. 1994. Tuberculosis and acquired immunodeficiency syndrome: a historical perspective on recent developments. Am. J. Med. 96:439-450.
    • (1994) Am. J. Med. , vol.96 , pp. 439-450
    • Haas, D.W.1    Des Prez, R.M.2
  • 29
    • 0022016158 scopus 로고
    • Directed formation of deletions and duplications using Mud(Ap, lac)
    • Hughes, K. T., and J. R. Roth. 1985. Directed formation of deletions and duplications using Mud(Ap, lac). Genetics 109:263-282.
    • (1985) Genetics , vol.109 , pp. 263-282
    • Hughes, K.T.1    Roth, J.R.2
  • 30
    • 0019877072 scopus 로고
    • Rapid and efficient cosmid cloning
    • Ish-Horowicz, D., and J. F. Burke. 1981. Rapid and efficient cosmid cloning. Nucleic Acids Res. 9:2989-2998.
    • (1981) Nucleic Acids Res. , vol.9 , pp. 2989-2998
    • Ish-Horowicz, D.1    Burke, J.F.2
  • 33
    • 0025697281 scopus 로고
    • Aspartokinase genes lysCα and lysCβ overlap and are adjacent to the aspartate β-semialdehyde dehydrogenase gene asd in Corynebacterium glutamicum
    • Kalinowski, J., B. Bachmann, G. Theirbach, and A. Pühler. 1990. Aspartokinase genes lysCα and lysCβ overlap and are adjacent to the aspartate β-semialdehyde dehydrogenase gene asd in Corynebacterium glutamicum. Mol. Gen. Genet. 224:317-324.
    • (1990) Mol. Gen. Genet. , vol.224 , pp. 317-324
    • Kalinowski, J.1    Bachmann, B.2    Theirbach, G.3    Pühler, A.4
  • 34
    • 0025802142 scopus 로고
    • Genetic and biochemical analysis of the aspartokinase from Corynebacterium glutamicum
    • Kalinowski, J., J. Cremer, B. Bachmann, L. Eggeling, H. Sahm, and A. Pühler. 1991. Genetic and biochemical analysis of the aspartokinase from Corynebacterium glutamicum. Mol. Microbiol. 5:1197-1204.
    • (1991) Mol. Microbiol. , vol.5 , pp. 1197-1204
    • Kalinowski, J.1    Cremer, J.2    Bachmann, B.3    Eggeling, L.4    Sahm, H.5    Pühler, A.6
  • 35
    • 0027997210 scopus 로고
    • Cloning and sequence analysis of the rpsL and rpsG genes of Mycobacterium smegmatis and characterization of mutations causing resistance to streptomycin
    • Kenney, T. J., and G. Churchward. 1994. Cloning and sequence analysis of the rpsL and rpsG genes of Mycobacterium smegmatis and characterization of mutations causing resistance to streptomycin. J. Bacteriol. 176:6153-6156.
    • (1994) J. Bacteriol. , vol.176 , pp. 6153-6156
    • Kenney, T.J.1    Churchward, G.2
  • 36
    • 0001506351 scopus 로고
    • Streptomycin resistance: A genetically recessive mutation
    • Lederberg, J. 1951. Streptomycin resistance: a genetically recessive mutation. J. Bacteriol. 61:549-550.
    • (1951) J. Bacteriol. , vol.61 , pp. 549-550
    • Lederberg, J.1
  • 37
    • 0015180517 scopus 로고
    • The mycobacterial cell wall
    • Lederer, E. 1971. The mycobacterial cell wall. Pure Appl. Chem. 25:135-165.
    • (1971) Pure Appl. Chem. , vol.25 , pp. 135-165
    • Lederer, E.1
  • 38
    • 0026323938 scopus 로고
    • Site-specific integration of mycobacteriophage L5: Integration-proficient vectors for Mycobacterium smegmatis, BCG, and M. tuberculosis
    • Lee, M. H., L. Pascopella, W. R. Jacobs, Jr., and G. F. Hatfull. 1991. Site-specific integration of mycobacteriophage L5: integration-proficient vectors for Mycobacterium smegmatis, BCG, and M. tuberculosis. Proc. Natl. Acad. Sci. USA 88:3111-3115.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 3111-3115
    • Lee, M.H.1    Pascopella, L.2    Jacobs Jr., W.R.3    Hatfull, G.F.4
  • 40
    • 0025001556 scopus 로고
    • Nucleotide sequence and organization of the upstream region of the Corynebacterium glutamicum lysA gene
    • Marcel, T., J. A. C. Archer, D. Mengin-Lecreuix, and A. J. Sinksey. 1990. Nucleotide sequence and organization of the upstream region of the Corynebacterium glutamicum lysA gene. Mol. Microbiol. 4:1819-1830.
    • (1990) Mol. Microbiol. , vol.4 , pp. 1819-1830
    • Marcel, T.1    Archer, J.A.C.2    Mengin-Lecreuix, D.3    Sinksey, A.J.4
  • 42
    • 0025129860 scopus 로고
    • Evidence for the nature of the link between the arabinogalactan and peptidoglycan of mycobacterial cell walls
    • McNeil, M., M. Daffe, and P. J. Brennan. 1990. Evidence for the nature of the link between the arabinogalactan and peptidoglycan of mycobacterial cell walls. J. Biol. Chem. 265:18200-18206.
    • (1990) J. Biol. Chem. , vol.265 , pp. 18200-18206
    • McNeil, M.1    Daffe, M.2    Brennan, P.J.3
  • 43
    • 0025773345 scopus 로고
    • Structure, function, and biogenesis of the cell envelope of mycobacteria
    • McNeil, M. R., and P. J. Brennan. 1994. Structure, function, and biogenesis of the cell envelope of mycobacteria. Res. Microbiol. 142:451-463.
    • (1994) Res. Microbiol. , vol.142 , pp. 451-463
    • McNeil, M.R.1    Brennan, P.J.2
  • 44
    • 0342849031 scopus 로고
    • Interrelationship between lysine and α,ε-diaminopimlic acid and their derivatives and analogs in mutants of Escherichia coli
    • Meadow, P., D. S. Hoare, and E. Work. 1957. Interrelationship between lysine and α,ε-diaminopimlic acid and their derivatives and analogs in mutants of Escherichia coli. Biochem. J. 66:270-282.
    • (1957) Biochem. J. , vol.66 , pp. 270-282
    • Meadow, P.1    Hoare, D.S.2    Work, E.3
  • 46
    • 85035173368 scopus 로고    scopus 로고
    • Personal communication
    • Mizuguchi, Y. Personal communication.
    • Mizuguchi, Y.1
  • 47
    • 0028800051 scopus 로고
    • Transcriptional regulation of repressor synthesis in mycobacteriophage L5
    • Nesbit, C. E., M. E. Levin, M. K. Donnelly-Wu, and G. F. Hatfull. 1995. Transcriptional regulation of repressor synthesis in mycobacteriophage L5. Mol. Microbiol. 17:1045-1056.
    • (1995) Mol. Microbiol. , vol.17 , pp. 1045-1056
    • Nesbit, C.E.1    Levin, M.E.2    Donnelly-Wu, M.K.3    Hatfull, G.F.4
  • 48
    • 0025767090 scopus 로고
    • Permeability of the mycobacterial cell wall
    • Nikaido, H., and V. Jarlier. 1994. Permeability of the mycobacterial cell wall. Res. Microbiol. 142:437-442.
    • (1994) Res. Microbiol. , vol.142 , pp. 437-442
    • Nikaido, H.1    Jarlier, V.2
  • 49
    • 0027521264 scopus 로고
    • A gene encoding arginyl-tRNA synthetase is located in the upstream region of the lysA gene in Brevobacterium lactofermentum: Regulation of argS-lysA cluster expression by arginine
    • Oguiza, J. A., M. Malumbres, G. Eriani, A. Pisabarro, L. M. Mateos, F. Martin, and J. F. Martin. 1993. A gene encoding arginyl-tRNA synthetase is located in the upstream region of the lysA gene in Brevobacterium lactofermentum: regulation of argS-lysA cluster expression by arginine. J. Bacteriol. 175:7356-7362.
    • (1993) J. Bacteriol. , vol.175 , pp. 7356-7362
    • Oguiza, J.A.1    Malumbres, M.2    Eriani, G.3    Pisabarro, A.4    Mateos, L.M.5    Martin, F.6    Martin, J.F.7
  • 50
    • 0014213654 scopus 로고
    • Regulation by methionine of the synthesis of a third aspartokinase and of a second homoserine dehydrogenase in Escherichia coli K-12
    • Patte, J.-C., G. Le Bras, and G. N. Cohen. 1967. Regulation by methionine of the synthesis of a third aspartokinase and of a second homoserine dehydrogenase in Escherichia coli K-12. Biochim. Biophys. Acta 136:245-257.
    • (1967) Biochim. Biophys. Acta , vol.136 , pp. 245-257
    • Patte, J.-C.1    Le Bras, G.2    Cohen, G.N.3
  • 51
    • 0028889845 scopus 로고
    • Global epidemiology of tuberculosis
    • Raviglione, M. C., J. D. E. Snider, and A. Kochi. 1995. Global epidemiology of tuberculosis. JAMA 273:220-226.
    • (1995) JAMA , vol.273 , pp. 220-226
    • Raviglione, M.C.1    Snider, J.D.E.2    Kochi, A.3
  • 52
    • 0029078403 scopus 로고
    • The urease locus of Mycobacterium tuberculosis and its utilization for the demonstration of allelic exchange in Mycobacterium bovis bacillus Calmette-Guérin
    • Reyrat, J.-M., F.-X. Berthet, and B. Gicqnel. 1995. The urease locus of Mycobacterium tuberculosis and its utilization for the demonstration of allelic exchange in Mycobacterium bovis bacillus Calmette-Guérin. Proc. Natl. Acad. Sci. USA 92:8768-8772.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 8768-8772
    • Reyrat, J.-M.1    Berthet, F.-X.2    Gicqnel, B.3
  • 53
    • 10344251192 scopus 로고
    • Role of α,ε-diaminopimelic acid in the cellular integrity of Escherichia coli
    • Rhuland, L. E. 1956. Role of α,ε-diaminopimelic acid in the cellular integrity of Escherichia coli. J. Bacteriol. 73:778-783.
    • (1956) J. Bacteriol. , vol.73 , pp. 778-783
    • Rhuland, L.E.1
  • 54
    • 0024535556 scopus 로고
    • Exchange of chromosomal and plasmid alleles in Escherichia coli by selection for loss of a dominant antibiotic sensitivity marker
    • Russell, C. B., and F. W. Dahlquist. 1989. Exchange of chromosomal and plasmid alleles in Escherichia coli by selection for loss of a dominant antibiotic sensitivity marker. J. Bacteriol. 171:2614-2618.
    • (1989) J. Bacteriol. , vol.171 , pp. 2614-2618
    • Russell, C.B.1    Dahlquist, F.W.2
  • 55
    • 0028979580 scopus 로고
    • +: A dominant selectable marker for gene replacement in mycobacteria
    • +: a dominant selectable marker for gene replacement in mycobacteria. Mol. Microbiol. 16:991-1000.
    • (1995) Mol. Microbiol. , vol.16 , pp. 991-1000
    • Sander, P.1    Meier, A.2    Böttger, E.C.3
  • 56
    • 0015462556 scopus 로고
    • Peptidoglycan types of bacterial cell walls and their taxonomic implications
    • Schleifer, K. H., and O. Kandler. 1972. Peptidoglycan types of bacterial cell walls and their taxonomic implications. Bacteriol. Rev. 36:407-477.
    • (1972) Bacteriol. Rev. , vol.36 , pp. 407-477
    • Schleifer, K.H.1    Kandler, O.2
  • 57
    • 0021056590 scopus 로고
    • Genetic methods for analysis and manipulation of inversion mutations in bacteria
    • Schmid, M. B., and J. R. Roth. 1983. Genetic methods for analysis and manipulation of inversion mutations in bacteria. Genetics 105:517-537.
    • (1983) Genetics , vol.105 , pp. 517-537
    • Schmid, M.B.1    Roth, J.R.2
  • 58
    • 0027531686 scopus 로고
    • Corynebacterium glutamicum arginyl-tRNA synthetase
    • Sharp, P. M., and K. J. Mitchell. 1993. Corynebacterium glutamicum arginyl-tRNA synthetase. Mol. Microbiol. 8:200.
    • (1993) Mol. Microbiol. , vol.8 , pp. 200
    • Sharp, P.M.1    Mitchell, K.J.2
  • 59
    • 0028810414 scopus 로고
    • Attenuated Shigella as a DNA delivery vehicle for DNA-mediated immunization
    • Sizemore, D. R., A. A. Branstrom, and J. C. Sadoff. 1995. Attenuated Shigella as a DNA delivery vehicle for DNA-mediated immunization. Science 270: 299-302.
    • (1995) Science , vol.270 , pp. 299-302
    • Sizemore, D.R.1    Branstrom, A.A.2    Sadoff, J.C.3
  • 60
    • 0027420061 scopus 로고
    • New suicide vector for gene replacement in yersiniac and other gram-negative bacteria
    • Skrzypek, E., P. L. Haddix, G. V. Plano, and S. C. Straley. 1993. New suicide vector for gene replacement in yersiniac and other gram-negative bacteria. Plasmids 29:160-163.
    • (1993) Plasmids , vol.29 , pp. 160-163
    • Skrzypek, E.1    Haddix, P.L.2    Plano, G.V.3    Straley, S.C.4
  • 61
    • 0025081151 scopus 로고
    • Isolation and characterization of efficient plasmid transformation mutants of Mycobacterium smegmatis
    • Snapper, S. B., R. E. Melton, S. Mustafa, T. Kieser, and W. R. Jacobs, Jr. 1990. Isolation and characterization of efficient plasmid transformation mutants of Mycobacterium smegmatis. Mol. Microbiol. 4:1911-1919.
    • (1990) Mol. Microbiol. , vol.4 , pp. 1911-1919
    • Snapper, S.B.1    Melton, R.E.2    Mustafa, S.3    Kieser, T.4    Jacobs Jr., W.R.5
  • 63
    • 0024566894 scopus 로고
    • Metabolism of aspartate in Mycobacterium smegmatis
    • Sritharan, V. O., P. R. Wheeler, and C. Ratledge. 1989. Metabolism of aspartate in Mycobacterium smegmatis. Eur. J. Biochem. 180:587-593.
    • (1989) Eur. J. Biochem. , vol.180 , pp. 587-593
    • Sritharan, V.O.1    Wheeler, P.R.2    Ratledge, C.3
  • 64
    • 0028243351 scopus 로고
    • MycDB: An integrated mycobacterial database
    • Staffen, B., and S. T. Cole. 1994. MycDB: an integrated mycobacterial database. Mol. Microbiol. 5:517-534.
    • (1994) Mol. Microbiol. , vol.5 , pp. 517-534
    • Staffen, B.1    Cole, S.T.2
  • 66
    • 0021054334 scopus 로고
    • Regulatory pattern of the Escherichia coli lysA gene: Expression of chromosomal lysA-lacZ fusions
    • Stragier, P., F. Borne, F. Richaud, C. Richaud, and J.-C. Patte. 1983. Regulatory pattern of the Escherichia coli lysA gene: expression of chromosomal lysA-lacZ fusions. J. Bacteriol. 156:1198-1203.
    • (1983) J. Bacteriol. , vol.156 , pp. 1198-1203
    • Stragier, P.1    Borne, F.2    Richaud, F.3    Richaud, C.4    Patte, J.-C.5
  • 67
    • 0020954580 scopus 로고
    • Regulation of diaminopimelate decarboxylase synthesis in Escherichia coli. I. Identification of a lysR gene encoding an activator of the lysA gene
    • Stragier, P., F. Richaud, F. Borne, and J.-C. Patte. 1983. Regulation of diaminopimelate decarboxylase synthesis in Escherichia coli. I. Identification of a lysR gene encoding an activator of the lysA gene. J. Mol. Biol. 168:307-320.
    • (1983) J. Mol. Biol. , vol.168 , pp. 307-320
    • Stragier, P.1    Richaud, F.2    Borne, F.3    Patte, J.-C.4
  • 68
    • 0015989915 scopus 로고
    • Mapping the structural genes of the three aspartokinases and of the two homoserine dehydrogenases of Escherichia coli K-12
    • Thèze, J., D. Margarita, G. N. Cohen, F. Borne, and J. C. Patte. 1974. Mapping the structural genes of the three aspartokinases and of the two homoserine dehydrogenases of Escherichia coli K-12. J. Bacteriol. 117:133-143.
    • (1974) J. Bacteriol. , vol.117 , pp. 133-143
    • Thèze, J.1    Margarita, D.2    Cohen, G.N.3    Borne, F.4    Patte, J.C.5
  • 69
    • 0017794395 scopus 로고
    • Amino acid biosynthesis and its regulation
    • Umbarger, H. E. 1978. Amino acid biosynthesis and its regulation. Annu. Rev. Biochem. 47:533-606.
    • (1978) Annu. Rev. Biochem. , vol.47 , pp. 533-606
    • Umbarger, H.E.1
  • 70
    • 0016209670 scopus 로고
    • Occurrence of D-alanyl-(D)-meso-diaminopimelic acid and meso-diaminopimelyl-meso-diaminopimelic acid interpeptide linkages in the peptidoglycan of mycobacteria
    • Wietzerbin, J., B. C. Das, J.-F. Petit, E. Lederer, M. Leyh-Bouille, and J.-M. Ghuysen. 1974. Occurrence of D-alanyl-(D)-meso-diaminopimelic acid and meso-diaminopimelyl-meso-diaminopimelic acid interpeptide linkages in the peptidoglycan of mycobacteria. Biochemistry 13:3471-3476.
    • (1974) Biochemistry , vol.13 , pp. 3471-3476
    • Wietzerbin, J.1    Das, B.C.2    Petit, J.-F.3    Lederer, E.4    Leyh-Bouille, M.5    Ghuysen, J.-M.6
  • 71
    • 0025014844 scopus 로고
    • Comparison of the three aspartokinase isozymes in Bacillus subtilis Marburg and 168
    • Zhang, J.-J., F.-M. Hu, N.-Y. Chen, and H. Paulus. 1990. Comparison of the three aspartokinase isozymes in Bacillus subtilis Marburg and 168. J. Bacteriol. 172:701-708.
    • (1990) J. Bacteriol. , vol.172 , pp. 701-708
    • Zhang, J.-J.1    Hu, F.-M.2    Chen, N.-Y.3    Paulus, H.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.