메뉴 건너뛰기




Volumn 28, Issue 6, 1998, Pages 1323-1334

The group a streptococcal dipeptide permease (Dpp) is involved in the uptake of essential amino acids and affects the expression of cysteine protease

Author keywords

[No Author keywords available]

Indexed keywords

ABC TRANSPORTER; CYSTEINE PROTEINASE; DIPEPTIDE; PERMEASE; VIRULENCE FACTOR;

EID: 0031776883     PISSN: 0950382X     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1365-2958.1998.00898.x     Document Type: Article
Times cited : (71)

References (49)
  • 1
    • 0028072561 scopus 로고
    • The dipeptide permease of Escherichia coli closely resembles other bacterial transport systems and shows growth-phase-dependent expression
    • Abouhamad, W.N., and Manson, M.D. (1994) The dipeptide permease of Escherichia coli closely resembles other bacterial transport systems and shows growth-phase-dependent expression. Mol Microbiol 14: 1077-1092.
    • (1994) Mol Microbiol , vol.14 , pp. 1077-1092
    • Abouhamad, W.N.1    Manson, M.D.2
  • 2
    • 0025732327 scopus 로고
    • Peptide transport and chemotaxis in Escherichia coli and Salmonella typhimurium: Characterization of the dipeptide permease (Dpp) and the dipeptide-binding protein
    • Abouhamad, W.N., Manson, M., Gibson, M.M., and Higgins, C.F. (1991) Peptide transport and chemotaxis in Escherichia coli and Salmonella typhimurium: characterization of the dipeptide permease (Dpp) and the dipeptide-binding protein. Mol Microbiol 5: 1035-1047.
    • (1991) Mol Microbiol , vol.5 , pp. 1035-1047
    • Abouhamad, W.N.1    Manson, M.2    Gibson, M.M.3    Higgins, C.F.4
  • 3
    • 0025327409 scopus 로고
    • The ami locus of the Gram-positive bacterium Streptococcus pneumoniae is similar to binding protein-dependent transport operons of Gram-negative bacteria
    • Alloing, G., Trombe, M.C., and Claverys, J.P. (1990) The ami locus of the Gram-positive bacterium Streptococcus pneumoniae is similar to binding protein-dependent transport operons of Gram-negative bacteria. Mol Microbiol 4: 633-644.
    • (1990) Mol Microbiol , vol.4 , pp. 633-644
    • Alloing, G.1    Trombe, M.C.2    Claverys, J.P.3
  • 4
    • 0028128820 scopus 로고
    • Three highly homologous membrane-bound lipoproteins participate in oligopeptide transport by the Ami system of the Grampositive Streptococcus pneumoniae
    • Alloing, G., de Philip, P., and Claverys, J.P. (1994) Three highly homologous membrane-bound lipoproteins participate in oligopeptide transport by the Ami system of the Grampositive Streptococcus pneumoniae. J Mol Biol 241: 44-58.
    • (1994) J Mol Biol , vol.241 , pp. 44-58
    • Alloing, G.1    De Philip, P.2    Claverys, J.P.3
  • 6
    • 0028941597 scopus 로고
    • Streptococcal cysteine proteinase releases biologically active fragments of streptococcal surface proteins
    • Berge, A., and Björck, L. (1995) Streptococcal cysteine proteinase releases biologically active fragments of streptococcal surface proteins. J Biol Chem 270: 9862-9867.
    • (1995) J Biol Chem , vol.270 , pp. 9862-9867
    • Berge, A.1    Björck, L.2
  • 7
    • 10244261522 scopus 로고    scopus 로고
    • Activation of a 66-kilodalton human endothelial cell matrix metalloprotease by Streptococcus pyogenes extracellular cysteine protease
    • Burns, E.H., Marciel, A.M., and Musser, J.M. (1996) Activation of a 66-kilodalton human endothelial cell matrix metalloprotease by Streptococcus pyogenes extracellular cysteine protease. Infect Immun 64: 4744-4750.
    • (1996) Infect Immun , vol.64 , pp. 4744-4750
    • Burns, E.H.1    Marciel, A.M.2    Musser, J.M.3
  • 8
    • 0025751633 scopus 로고
    • Genetic manipulation of pathogenic streptococci
    • Caparon, M.G., and Scott, J.R. (1991) Genetic manipulation of pathogenic streptococci. Methods Enzymol 204: 556-586.
    • (1991) Methods Enzymol , vol.204 , pp. 556-586
    • Caparon, M.G.1    Scott, J.R.2
  • 9
    • 0000102947 scopus 로고
    • Effect of amino acids on steady-state growth of a group A hemolytic streptococcus
    • Davies, H.C., Karush, F., and Rudd, J.H. (1965) Effect of amino acids on steady-state growth of a group A hemolytic streptococcus. J Bacteriol 89: 421-427.
    • (1965) J Bacteriol , vol.89 , pp. 421-427
    • Davies, H.C.1    Karush, F.2    Rudd, J.H.3
  • 10
    • 0027446537 scopus 로고
    • Transport of 5-aminolevulinic acid by the dipeptide permease in Salmonella typhimurium
    • Elliot, T. (1993) Transport of 5-aminolevulinic acid by the dipeptide permease in Salmonella typhimurium. J Bacteriol 175: 325-331.
    • (1993) J Bacteriol , vol.175 , pp. 325-331
    • Elliot, T.1
  • 11
    • 0029977011 scopus 로고    scopus 로고
    • Role of CodY in regulation of the Bacillus subtilis hut operon
    • Fisher, S.H., Rohrer, K., and Ferson, A.E. (1996) Role of CodY in regulation of the Bacillus subtilis hut operon. J Bacteriol 178: 3779-3784.
    • (1996) J Bacteriol , vol.178 , pp. 3779-3784
    • Fisher, S.H.1    Rohrer, K.2    Ferson, A.E.3
  • 12
    • 0029092632 scopus 로고
    • Specificity of peptide transport systems in Lactococcus lactis: Evidence for a third system which transports hydrophobic di- and tripeptides
    • Foucaud, C., Kunji, E.R.S., Hagting, A., Richard, J., Konings, W.N., Desmazeaud, M., et al. (1995) Specificity of peptide transport systems in Lactococcus lactis: evidence for a third system which transports hydrophobic di- and tripeptides. J Bacteriol 177: 4652-4657.
    • (1995) J Bacteriol , vol.177 , pp. 4652-4657
    • Foucaud, C.1    Kunji, E.R.S.2    Hagting, A.3    Richard, J.4    Konings, W.N.5    Desmazeaud, M.6
  • 13
    • 0021193852 scopus 로고
    • Genetic characterization and molecular cloning of the tripeptide permease (tpp) genes of Salmonella typhimurium
    • Gibson, M.M., Price, M., and Higgins, C.F. (1984) Genetic characterization and molecular cloning of the tripeptide permease (tpp) genes of Salmonella typhimurium. J Bacteriol 160: 122-130.
    • (1984) J Bacteriol , vol.160 , pp. 122-130
    • Gibson, M.M.1    Price, M.2    Higgins, C.F.3
  • 14
    • 0028179387 scopus 로고
    • The di- and tripeptide transport protein of Lactococcus lactis: A new type of bacterial transporter
    • Hagting, E., Kunji, E.R.S., Leenhouts, K.J., Poolman, B., and Konings, W.N. (1994) The di- and tripeptide transport protein of Lactococcus lactis: a new type of bacterial transporter. J Biol Chem 269: 11391-11399.
    • (1994) J Biol Chem , vol.269 , pp. 11391-11399
    • Hagting, E.1    Kunji, E.R.S.2    Leenhouts, K.J.3    Poolman, B.4    Konings, W.N.5
  • 15
    • 0029164287 scopus 로고
    • The ABC of channel regulation
    • Higgins, C.F. (1995) The ABC of channel regulation. Cell 82: 693-696.
    • (1995) Cell , vol.82 , pp. 693-696
    • Higgins, C.F.1
  • 16
    • 0023644827 scopus 로고
    • Molecular characterization of the oligopeptide permease of Salmonella typhimurium
    • Hiles, I.A., Gallagher, M.P., Jamieson, D.J., and Higgins, C.F. (1987) Molecular characterization of the oligopeptide permease of Salmonella typhimurium. J Mol Biol 195: 125-142.
    • (1987) J Mol Biol , vol.195 , pp. 125-142
    • Hiles, I.A.1    Gallagher, M.P.2    Jamieson, D.J.3    Higgins, C.F.4
  • 17
    • 0030063057 scopus 로고    scopus 로고
    • A binding-lipoprotein-dependent oligopeptide transport system in Streptococcus gordonii essential for uptake of hexa- and heptapeptides
    • Jenkinson, H.F., Baker, R.A., and Tannock, G.W. (1996) A binding-lipoprotein-dependent oligopeptide transport system in Streptococcus gordonii essential for uptake of hexa- and heptapeptides. J Bacteriol 178: 68-77.
    • (1996) J Bacteriol , vol.178 , pp. 68-77
    • Jenkinson, H.F.1    Baker, R.A.2    Tannock, G.W.3
  • 19
    • 0027893017 scopus 로고
    • A conserved Streptococcus pyogenes extracellular cysteine protease cleaves human fibronectin and degrades vitronectin
    • Kapur, V., Topouzis, S., Majesky, M.W., Li, L.L., Hamrick, M.R., Hamill, R.J., et al. (1993) A conserved Streptococcus pyogenes extracellular cysteine protease cleaves human fibronectin and degrades vitronectin. Microb Pathogen 15: 327-346.
    • (1993) Microb Pathogen , vol.15 , pp. 327-346
    • Kapur, V.1    Topouzis, S.2    Majesky, M.W.3    Li, L.L.4    Hamrick, M.R.5    Hamill, R.J.6
  • 20
    • 0025349185 scopus 로고
    • Identification of the polyamine-induced protein as a periplasmic oligopeptide binding protein
    • Kashiwagi, K., Yamaguchi, Y., Sakai, Y., Kobayashi, H., and Igarashi, K. (1990) Identification of the polyamine-induced protein as a periplasmic oligopeptide binding protein. J Biol Chem 265: 8387-8391.
    • (1990) J Biol Chem , vol.265 , pp. 8387-8391
    • Kashiwagi, K.1    Yamaguchi, Y.2    Sakai, Y.3    Kobayashi, H.4    Igarashi, K.5
  • 21
    • 0029572448 scopus 로고
    • Biological properties of a Streptococcus pyogenes mutant generated by Tn916 insertion in mga
    • Kihlberg, B.M., Cooney, J., Caparon, M.G., Olsen, A., and Björck, L. (1995) Biological properties of a Streptococcus pyogenes mutant generated by Tn916 insertion in mga. Microb Pathogen 19: 299-315.
    • (1995) Microb Pathogen , vol.19 , pp. 299-315
    • Kihlberg, B.M.1    Cooney, J.2    Caparon, M.G.3    Olsen, A.4    Björck, L.5
  • 22
    • 0031053298 scopus 로고    scopus 로고
    • Identification of the lrp gene in Bradyrhizobium japonicum and its role in regulation on delta-aminolevulinic acid uptake
    • King, N.D., and O'Brian, M.R. (1997) Identification of the lrp gene in Bradyrhizobium japonicum and its role in regulation on delta-aminolevulinic acid uptake. J Bacteriol 179: 1828-1831.
    • (1997) J Bacteriol , vol.179 , pp. 1828-1831
    • King, N.D.1    O'Brian, M.R.2
  • 23
    • 0027971083 scopus 로고
    • Identification of a second oligopeptide transport system in Bacillus subtilis and determination of its role in sporulation
    • Koide, A., and Hoch, J.A. (1994) Identification of a second oligopeptide transport system in Bacillus subtilis and determination of its role in sporulation. Mol Microbiol 13: 417-426.
    • (1994) Mol Microbiol , vol.13 , pp. 417-426
    • Koide, A.1    Hoch, J.A.2
  • 24
    • 0028985665 scopus 로고
    • Transport of á-casein-derived peptides by the oligopeptide transport system is a crucial step in the proteolytic pathway of Lactococcus lactis
    • Kunji, E.R.S., Hagting, A., de Vries, C.J., Juillard, V., Haandrikman, A.J., Poolman, B., et al. (1995) Transport of á-casein-derived peptides by the oligopeptide transport system is a crucial step in the proteolytic pathway of Lactococcus lactis. J Biol Chem 270: 1569-1574.
    • (1995) J Biol Chem , vol.270 , pp. 1569-1574
    • Kunji, E.R.S.1    Hagting, A.2    De Vries, C.J.3    Juillard, V.4    Haandrikman, A.J.5    Poolman, B.6
  • 25
    • 0030044159 scopus 로고    scopus 로고
    • Enterococcus faecalis pheromone binding protein, PrgZ, recruits a chromosomal oligopeptide permease system (Opp) to import sex pheromone pCF10 for induction of conjugation
    • Leonard, B.A.B., Podbielski, A., Hedberg, P.J., and Dunny, G.M. (1996) Enterococcus faecalis pheromone binding protein, PrgZ, recruits a chromosomal oligopeptide permease system (Opp) to import sex pheromone pCF10 for induction of conjugation. Proc Natl Acad Sci USA 93: 260-264.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 260-264
    • Leonard, B.A.B.1    Podbielski, A.2    Hedberg, P.J.3    Dunny, G.M.4
  • 26
    • 0030960001 scopus 로고    scopus 로고
    • Inactivation of Streptococcus pyogenes extracellular cysteine protease significantly decreases mouse lethality of serotype M3 and M49 strains
    • Lukomski, S., Sreevatsan, S., Amberg, C., Reichardt, W., Woischnik, M., Podbielski, A., et al. (1997) Inactivation of Streptococcus pyogenes extracellular cysteine protease significantly decreases mouse lethality of serotype M3 and M49 strains. J Clin Invest 99: 2574-2580.
    • (1997) J Clin Invest , vol.99 , pp. 2574-2580
    • Lukomski, S.1    Sreevatsan, S.2    Amberg, C.3    Reichardt, W.4    Woischnik, M.5    Podbielski, A.6
  • 27
    • 0030753825 scopus 로고    scopus 로고
    • Role of mga in growth phase regulation of virulence genes of the group A streptococcus
    • Mclver, K., and Scott, J.R. (1997) Role of mga in growth phase regulation of virulence genes of the group A streptococcus. J Bacteriol 179: 5178-5187.
    • (1997) J Bacteriol , vol.179 , pp. 5178-5187
    • Mclver, K.1    Scott, J.R.2
  • 28
    • 0028857768 scopus 로고
    • Specific binding of the activator Mga to promoter sequences of the emm and scpA genes in the group A streptococcus
    • McIver, K.S., Heath, A.S., Grenn, B.D., and Scott, J.R. (1995) Specific binding of the activator Mga to promoter sequences of the emm and scpA genes in the group A streptococcus. J Bacteriol 177: 6619-6624.
    • (1995) J Bacteriol , vol.177 , pp. 6619-6624
    • McIver, K.S.1    Heath, A.S.2    Grenn, B.D.3    Scott, J.R.4
  • 29
    • 0022474926 scopus 로고
    • Peptide chemotaxis in E. coli involves the Tap signal transducer and the dipeptide permease
    • Manson, M.D., Blank, V., Brade, G., and Higgins, C.F. (1986) Peptide chemotaxis in E. coli involves the Tap signal transducer and the dipeptide permease. Nature 321: 253-256.
    • (1986) Nature , vol.321 , pp. 253-256
    • Manson, M.D.1    Blank, V.2    Brade, G.3    Higgins, C.F.4
  • 30
    • 0025005040 scopus 로고
    • Comparison of epidemic and endemic group G streptococci by restriction enzyme analysis
    • Martin, N.J., Kaplan, E.L, Gerber, M.A., Menegus, M.A., Randolph, M., Bell, K., et al. (1990) Comparison of epidemic and endemic group G streptococci by restriction enzyme analysis. J Clin Microbiol 28: 1881-1886.
    • (1990) J Clin Microbiol , vol.28 , pp. 1881-1886
    • Martin, N.J.1    Kaplan, E.L.2    Gerber, M.A.3    Menegus, M.A.4    Randolph, M.5    Bell, K.6
  • 32
    • 0030909215 scopus 로고    scopus 로고
    • Cloning and functional expression in Escherichia coli of the gene encoding the di- and tripeptide transport protein of Lactobacillus helveticus
    • Nakajima, H., Hagting, A., Kunji, E.R.S., Poolman, B., and Konings, W.N. (1997) Cloning and functional expression in Escherichia coli of the gene encoding the di- and tripeptide transport protein of Lactobacillus helveticus. Appl Environ Microbiol 63: 2213-2217.
    • (1997) Appl Environ Microbiol , vol.63 , pp. 2213-2217
    • Nakajima, H.1    Hagting, A.2    Kunji, E.R.S.3    Poolman, B.4    Konings, W.N.5
  • 33
    • 0026084296 scopus 로고
    • Identification and characterization of dppA, an Escherichia coli gene encoding a periplasmic dipeptide transport protein
    • Olson, E.R., Dunyak, D.S., Jurss, L.M., and Poorman, R.A. (1991) Identification and characterization of dppA, an Escherichia coli gene encoding a periplasmic dipeptide transport protein. J Bacteriol 173: 234-244.
    • (1991) J Bacteriol , vol.173 , pp. 234-244
    • Olson, E.R.1    Dunyak, D.S.2    Jurss, L.M.3    Poorman, R.A.4
  • 34
    • 0028861517 scopus 로고
    • The group A streptococcal virR49 gene controls expression of four structural vir regulon genes
    • Podbielski, A., Flosdorff, A., and Weber-Heynemann, J. (1995) The group A streptococcal virR49 gene controls expression of four structural vir regulon genes. Infect Immun 63: 9-20.
    • (1995) Infect Immun , vol.63 , pp. 9-20
    • Podbielski, A.1    Flosdorff, A.2    Weber-Heynemann, J.3
  • 35
    • 0030476579 scopus 로고    scopus 로고
    • What is the size of the group A streptococcal vir regulon? The Mga regulator affects expression of secreted and surface virulence factors
    • Podbielski, A., Woischnik, M., Pohl, B., and Schmidt, K.H. (1996a) What is the size of the group A streptococcal vir regulon? The Mga regulator affects expression of secreted and surface virulence factors. Med Microbiol Immunol 185: 171-181.
    • (1996) Med Microbiol Immunol , vol.185 , pp. 171-181
    • Podbielski, A.1    Woischnik, M.2    Pohl, B.3    Schmidt, K.H.4
  • 36
    • 0029798285 scopus 로고    scopus 로고
    • Molecular characterization of group A streptococcal (GAS) oligopeptide permease (Opp) and its effect on cysteine protease production
    • Podbielski, A., Pohl, B., Woischnik, M., Körner, C., Schmidt, K.H., Rozdzinski, E., and Leonard, B.A.B. (1996b) Molecular characterization of group A streptococcal (GAS) oligopeptide permease (Opp) and its effect on cysteine protease production. Mol Microbiol 21: 1087-1099.
    • (1996) Mol Microbiol , vol.21 , pp. 1087-1099
    • Podbielski, A.1    Pohl, B.2    Woischnik, M.3    Körner, C.4    Schmidt, K.H.5    Rozdzinski, E.6    Leonard, B.A.B.7
  • 37
    • 0030600488 scopus 로고    scopus 로고
    • Novel series of plasmid vectors for gene inactivation and expression analysis in group A streptococci (GAS)
    • Podbielski, A., Spellerberg, B., Woischnik, M., Pohl, B., and Lütticken, R. (1996c) Novel series of plasmid vectors for gene inactivation and expression analysis in group A streptococci (GAS). Gene 177: 137-147.
    • (1996) Gene , vol.177 , pp. 137-147
    • Podbielski, A.1    Spellerberg, B.2    Woischnik, M.3    Pohl, B.4    Lütticken, R.5
  • 39
    • 0028979280 scopus 로고
    • An extended - 10 promoter alone directs transcription of the Dpnll operon of Streptococcus pneumoniae
    • Sabelnikov, A.G., Greenberg, B., and Lacks, S.A. (1995) An extended - 10 promoter alone directs transcription of the Dpnll operon of Streptococcus pneumoniae. J Mol Biol 250: 144-155.
    • (1995) J Mol Biol , vol.250 , pp. 144-155
    • Sabelnikov, A.G.1    Greenberg, B.2    Lacks, S.A.3
  • 40
    • 0029837946 scopus 로고    scopus 로고
    • CodY is required for nutritional repression of Bacillus subtilis genetic competence
    • Serror, P., and Sonenshein, A.L. (1996a) CodY is required for nutritional repression of Bacillus subtilis genetic competence. J Bacteriol 178: 5910-5915.
    • (1996) J Bacteriol , vol.178 , pp. 5910-5915
    • Serror, P.1    Sonenshein, A.L.2
  • 41
    • 0029999864 scopus 로고    scopus 로고
    • Interaction of CodY, a novel Bacillus subtilis DNA-binding protein, with the dpp promoter region
    • Serror, P., and Sonenshein, A.L. (1996b) Interaction of CodY, a novel Bacillus subtilis DNA-binding protein, with the dpp promoter region. Mol Microbiol 20: 843-852.
    • (1996) Mol Microbiol , vol.20 , pp. 843-852
    • Serror, P.1    Sonenshein, A.L.2
  • 42
    • 0030042784 scopus 로고    scopus 로고
    • Streptococcal cysteine protease augments lung injury induced by products of group A streptococci
    • Shanley, T.P., Schrier, D., Kapur, V., Kehoe, M., Musser, J.M., and Ward, P.A. (1996) Streptococcal cysteine protease augments lung injury induced by products of group A streptococci. Infect Immun 64: 870-877.
    • (1996) Infect Immun , vol.64 , pp. 870-877
    • Shanley, T.P.1    Schrier, D.2    Kapur, V.3    Kehoe, M.4    Musser, J.M.5    Ward, P.A.6
  • 43
    • 0022407696 scopus 로고
    • Complete nucleotide sequence of macrolide-lincosamide-streptogramin B-resistance transposon Tn917 in Streptococcus faecalis
    • Shaw, J.H., and Clewell, D.B. (1985) Complete nucleotide sequence of macrolide-lincosamide-streptogramin B-resistance transposon Tn917 in Streptococcus faecalis. J Bacteriol 164: 782-796.
    • (1985) J Bacteriol , vol.164 , pp. 782-796
    • Shaw, J.H.1    Clewell, D.B.2
  • 44
    • 0027198224 scopus 로고
    • Mutations that relieve nutritional repression of the Bacillus subtilis dipeptide permease operon
    • Slack, F.J., Mueller, J.P., and Sonenshein, A.L. (1993) Mutations that relieve nutritional repression of the Bacillus subtilis dipeptide permease operon. J Bacteriol 175: 4605-4614.
    • (1993) J Bacteriol , vol.175 , pp. 4605-4614
    • Slack, F.J.1    Mueller, J.P.2    Sonenshein, A.L.3
  • 45
    • 0028968835 scopus 로고    scopus 로고
    • A gene required for nutritional repression of the Bacillus subtilis dipeptide permease operon
    • Slack, F.J., Serror, P., Joyce, E., and Sonnenshein, A.L. (1998) A gene required for nutritional repression of the Bacillus subtilis dipeptide permease operon. Mol Microbiol 15: 689-702.
    • (1998) Mol Microbiol , vol.15 , pp. 689-702
    • Slack, F.J.1    Serror, P.2    Joyce, E.3    Sonnenshein, A.L.4
  • 46
    • 0026675265 scopus 로고
    • Novel streptococcal-integration shuttle vectors for gene cloning and inactivation
    • Tao, L., LeBlanc, D.J., and Ferretti, J.J. (1992) Novel streptococcal-integration shuttle vectors for gene cloning and inactivation. Gene 120: 105-110.
    • (1992) Gene , vol.120 , pp. 105-110
    • Tao, L.1    LeBlanc, D.J.2    Ferretti, J.J.3
  • 47
    • 0027375439 scopus 로고
    • Genetic and biochemical characterization of the oligopeptide transport system of Lactococcus lactis
    • Tynkkynen, S., Buist, G., Kunji, E., Kok, J., Poolman, B., Venema, G., et al. (1993) Genetic and biochemical characterization of the oligopeptide transport system of Lactococcus lactis. J Bacteriol 175: 7523-7532.
    • (1993) J Bacteriol , vol.175 , pp. 7523-7532
    • Tynkkynen, S.1    Buist, G.2    Kunji, E.3    Kok, J.4    Poolman, B.5    Venema, G.6
  • 48
    • 0018901441 scopus 로고
    • Growth characteristics of group A streptococci in a new chemically defined medium
    • van de Rijn, I., and Kessler, R.E. (1980) Growth characteristics of group A streptococci in a new chemically defined medium. Infect Immun 27: 444-448.
    • (1980) Infect Immun , vol.27 , pp. 444-448
    • Van De Rijn, I.1    Kessler, R.E.2
  • 49
    • 0027532660 scopus 로고
    • The periplasmic dipeptide permease system transports 5-aminolevulinic acid in Escherichia coli
    • Verkamp, E., Backman, V.M., Björnsson, J.M., Söil, D., and Eggertsson, G. (1993) The periplasmic dipeptide permease system transports 5-aminolevulinic acid in Escherichia coli. J Bacteriol 175: 1452-1456.
    • (1993) J Bacteriol , vol.175 , pp. 1452-1456
    • Verkamp, E.1    Backman, V.M.2    Björnsson, J.M.3    Söil, D.4    Eggertsson, G.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.