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Volumn 179, Issue 21, 1997, Pages 6843-6850

The tyrocidine biosynthesis operon of Bacillus brevis: Complete nucleotide sequence and biochemical characterization of functional internal adenylation domains

Author keywords

[No Author keywords available]

Indexed keywords

PEPTIDE SYNTHASE; TYROCIDINE;

EID: 0030669091     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/jb.179.21.6843-6850.1997     Document Type: Article
Times cited : (253)

References (55)
  • 1
    • 0018800089 scopus 로고
    • A rapid alkaline extraction procedure for screening recombinant plasmid DNA
    • Birnboim, H. C., and J. Doly. 1979. A rapid alkaline extraction procedure for screening recombinant plasmid DNA. Nucleic Acids Res. 7:1513-1523.
    • (1979) Nucleic Acids Res. , vol.7 , pp. 1513-1523
    • Birnboim, H.C.1    Doly, J.2
  • 2
    • 0030584662 scopus 로고    scopus 로고
    • Crystal structure of firefly luciferase throws light on a superfamily of adenylate-forming enzymes
    • Conti, E., N. P. Franks, and P. Brick, 1996. Crystal structure of firefly luciferase throws light on a superfamily of adenylate-forming enzymes. Structure 4:287-298.
    • (1996) Structure , vol.4 , pp. 287-298
    • Conti, E.1    Franks, N.P.2    Brick, P.3
  • 3
    • 0030756031 scopus 로고    scopus 로고
    • Structural basis for the activation of phenylalanine in the non-ribosomal biosynthesis of gramicidin S
    • Conti, E., T. Stachelhaus, M. A. Marahiel, and P. Brick. 1997. Structural basis for the activation of phenylalanine in the non-ribosomal biosynthesis of gramicidin S. EMBO J. 16:4174-4183.
    • (1997) EMBO J. , vol.16 , pp. 4174-4183
    • Conti, E.1    Stachelhaus, T.2    Marahiel, M.A.3    Brick, P.4
  • 5
    • 0028807689 scopus 로고
    • Multienzymatic nonribosomal peptide biosynthesis: Identification of the functional domains catalysing peptide elongation and epimerisation
    • De Crécy-Lagard, V., P. Marlière, and W. Saurin. 1995. Multienzymatic nonribosomal peptide biosynthesis: identification of the functional domains catalysing peptide elongation and epimerisation. C. R. Acad. Sci. III 318: 927-936.
    • (1995) C. R. Acad. Sci. III , vol.318 , pp. 927-936
    • De Crécy-Lagard, V.1    Marlière, P.2    Saurin, W.3
  • 6
    • 0028896569 scopus 로고
    • Expression of an active adenylate-forming domain of peptide synthetases corresponding to acyl-CoA-synthetases
    • Dieckmann, R., Y. O. Lee, H. van Liempt, H. von Döhren, and H. Kleinkauf. 1995. Expression of an active adenylate-forming domain of peptide synthetases corresponding to acyl-CoA-synthetases. FEBS Lett. 357:212-216.
    • (1995) FEBS Lett. , vol.357 , pp. 212-216
    • Dieckmann, R.1    Lee, Y.O.2    Van Liempt, H.3    Von Döhren, H.4    Kleinkauf, H.5
  • 9
    • 0014421732 scopus 로고
    • Biosynthesis of tyrocidine by a cell-free enzyme system of Bacillus brevis ATCC 8185. II. Amino acid substitution in tyrocidine
    • Fujikawa, K., Y. Sakamoto, T. Suzuki, and K. Kurahashi. 1968. Biosynthesis of tyrocidine by a cell-free enzyme system of Bacillus brevis ATCC 8185. II. Amino acid substitution in tyrocidine. Biochim. Biophys. Acta 169:520-533.
    • (1968) Biochim. Biophys. Acta , vol.169 , pp. 520-533
    • Fujikawa, K.1    Sakamoto, Y.2    Suzuki, T.3    Kurahashi, K.4
  • 10
    • 0026019195 scopus 로고
    • Interaction of AbrB, a transcriptional regulator from Bacillus subtilis, with the promoters of the transition state-activated genes tyca and spoVG
    • Fürbass, R., M. Gocht, P. Zuber, and M. A. Marahiel. 1991. Interaction of AbrB, a transcriptional regulator from Bacillus subtilis, with the promoters of the transition state-activated genes tycA and spoVG. Mol. Gen. Genet. 225: 347-354.
    • (1991) Mol. Gen. Genet. , vol.225 , pp. 347-354
    • Fürbass, R.1    Gocht, M.2    Zuber, P.3    Marahiel, M.A.4
  • 11
    • 0031035424 scopus 로고    scopus 로고
    • A locus coding for putative non-ribosomal peptide/polyketide synthase functions is mutated in a swarming-defective Proteus mirabilis strain
    • Gaisser, S., and C. Hughes. 1997. A locus coding for putative non-ribosomal peptide/polyketide synthase functions is mutated in a swarming-defective Proteus mirabilis strain. Mol. Gen. Genet. 253:415-427.
    • (1997) Mol. Gen. Genet. , vol.253 , pp. 415-427
    • Gaisser, S.1    Hughes, C.2
  • 13
    • 0028226896 scopus 로고
    • Analysis of core sequences in the D-Phe activating domain of the multifunctional peptide synthetase TycA by site-directed mutagenesis
    • Gocht, M., and M. A. Marahiel. 1994. Analysis of core sequences in the D-Phe activating domain of the multifunctional peptide synthetase TycA by site-directed mutagenesis. J. Bacteriol. 176:2654-2662.
    • (1994) J. Bacteriol. , vol.176 , pp. 2654-2662
    • Gocht, M.1    Marahiel, M.A.2
  • 14
    • 0027996536 scopus 로고
    • Bacterial expression of catalytically active fragments of the multifunctional enzyme enniatin synthetase
    • Haese, A., R. Pieper, T. von Ostrowski, and R. Zocher. 1994. Bacterial expression of catalytically active fragments of the multifunctional enzyme enniatin synthetase. J. Mol. Biol. 243:116-122.
    • (1994) J. Mol. Biol. , vol.243 , pp. 116-122
    • Haese, A.1    Pieper, R.2    Von Ostrowski, T.3    Zocher, R.4
  • 15
    • 0027466435 scopus 로고
    • Molecular characterization of the enniatin synthetase gene encoding a multifunctional enzyme catalysing N-methyldepsipeptide formation in Fusarium scirpi
    • Haese, A., M. Schubert, M. Herrmann, and R. Zocher. 1993. Molecular characterization of the enniatin synthetase gene encoding a multifunctional enzyme catalysing N-methyldepsipeptide formation in Fusarium scirpi. Mol. Microbiol. 7:905-914.
    • (1993) Mol. Microbiol. , vol.7 , pp. 905-914
    • Haese, A.1    Schubert, M.2    Herrmann, M.3    Zocher, R.4
  • 16
    • 0025833673 scopus 로고
    • The nucleotide sequence for a proline-activating domain of gramicidin S synthetase 2 gene from Bacillus brevis
    • Hori, K., Y. Yamamoto, K. Tokita, F. Saito, T. Kurotsu, M. Kanda, K. Okamura, J. Furuyama, and Y. Saito. 1991. The nucleotide sequence for a proline-activating domain of gramicidin S synthetase 2 gene from Bacillus brevis. J. Biochem. 110:111-119.
    • (1991) J. Biochem. , vol.110 , pp. 111-119
    • Hori, K.1    Yamamoto, Y.2    Tokita, K.3    Saito, F.4    Kurotsu, T.5    Kanda, M.6    Okamura, K.7    Furuyama, J.8    Saito, Y.9
  • 17
    • 0017646341 scopus 로고
    • The peptide antibiotics of Bacillus: Chemistry, biogenesis, and possible functions
    • Katz, E., and A. L. Demain. 1977. The peptide antibiotics of Bacillus: chemistry, biogenesis, and possible functions. Bacteriol. Rev. 41:449-474.
    • (1977) Bacteriol. Rev. , vol.41 , pp. 449-474
    • Katz, E.1    Demain, A.L.2
  • 18
    • 85151872634 scopus 로고
    • Kinetics of amino acid activation in gramicidin S synthesis
    • H. Kleinkauf and H. von Döhren (ed.), Walter de Gruyter, Berlin, Germany
    • Kittelberger, R., M. Altmann, and H. von Döhren. 1982. Kinetics of amino acid activation in gramicidin S synthesis, p. 209-218. In H. Kleinkauf and H. von Döhren (ed.), Peptide antibiotics, biosynthesis and functions. Walter de Gruyter, Berlin, Germany.
    • (1982) Peptide Antibiotics, Biosynthesis and Functions , pp. 209-218
    • Kittelberger, R.1    Altmann, M.2    Von Döhren, H.3
  • 19
    • 0026331192 scopus 로고
    • Cell-free biosynthesis of cyclosporin A and analogues
    • Kleinkauf, H., J. Dittmann, and A. Lawen. 1991. Cell-free biosynthesis of cyclosporin A and analogues. Biomed. Biochim. Acta 50:219-224.
    • (1991) Biomed. Biochim. Acta , vol.50 , pp. 219-224
    • Kleinkauf, H.1    Dittmann, J.2    Lawen, A.3
  • 20
    • 0025024567 scopus 로고
    • Nonribosomal biosynthesis of peptide antibiotics
    • Kleinkauf, H., and H. von Döhren. 1990. Nonribosomal biosynthesis of peptide antibiotics. Eur. J. Biochem. 192:1-15.
    • (1990) Eur. J. Biochem. , vol.192 , pp. 1-15
    • Kleinkauf, H.1    Von Döhren, H.2
  • 21
    • 0029921158 scopus 로고    scopus 로고
    • A nonribosomal system of peptide biosynthesis
    • Kleinkauf, H., and H. von Döhren. 1996. A nonribosomal system of peptide biosynthesis. Eur. J. Biochem. 236:335-351.
    • (1996) Eur. J. Biochem. , vol.236 , pp. 335-351
    • Kleinkauf, H.1    Von Döhren, H.2
  • 22
    • 0024437776 scopus 로고
    • Gramicidin S biosynthesis operon containing the structural genes grsA and grsB has an open reading frame encoding a protein homologous to fatty acid thioesterases
    • Krätzschmar, J., M. Krause, and M. A. Marahiel. 1989. Gramicidin S biosynthesis operon containing the structural genes grsA and grsB has an open reading frame encoding a protein homologous to fatty acid thioesterases. J. Bacteriol. 171:5422-5429.
    • (1989) J. Bacteriol. , vol.171 , pp. 5422-5429
    • Krätzschmar, J.1    Krause, M.2    Marahiel, M.A.3
  • 23
    • 0021856963 scopus 로고
    • Molecular cloning of an ornithine-activating fragment of the gramicidin S synthetase 2 gene from Bacillus brevis and its expression in Escherichia coli
    • Krause, M., M. A. Marahiel, H. von Döhren, and H. Kleinkauf. 1985. Molecular cloning of an ornithine-activating fragment of the gramicidin S synthetase 2 gene from Bacillus brevis and its expression in Escherichia coli. J. Bacteriol. 162:1120-1125.
    • (1985) J. Bacteriol. , vol.162 , pp. 1120-1125
    • Krause, M.1    Marahiel, M.A.2    Von Döhren, H.3    Kleinkauf, H.4
  • 25
    • 0027250118 scopus 로고
    • Substrate specificities of cyclosporin synthetase and peptolide SDZ 214-103 synthetase. Comparison of the substrate specificities of the related multifunctional polypeptides
    • Lawen, A., and R. Traber. 1993. Substrate specificities of cyclosporin synthetase and peptolide SDZ 214-103 synthetase. Comparison of the substrate specificities of the related multifunctional polypeptides. J. Biol. Chem. 268: 20452-20465.
    • (1993) J. Biol. Chem. , vol.268 , pp. 20452-20465
    • Lawen, A.1    Traber, R.2
  • 26
    • 0016417481 scopus 로고
    • Tyrocidine synthetase system
    • Lee, S. G., and F. Lipmann. 1975. Tyrocidine synthetase system. Methods Enzymol. 43:585-602.
    • (1975) Methods Enzymol. , vol.43 , pp. 585-602
    • Lee, S.G.1    Lipmann, F.2
  • 27
    • 0016539243 scopus 로고
    • The relation between sporulation and the induction of antibiotic synthesis and of amino acid uptake in Bacillus brevis
    • Lee, S. G., V. Littau, and F. Lipmann. 1975. The relation between sporulation and the induction of antibiotic synthesis and of amino acid uptake in Bacillus brevis. J. Cell Biol. 66:233-242.
    • (1975) J. Cell Biol. , vol.66 , pp. 233-242
    • Lee, S.G.1    Littau, V.2    Lipmann, F.3
  • 28
    • 0015939489 scopus 로고
    • Purification of the polyenzymes responsible for tyrocidine synthesis and their dissociation into subunits
    • Lee, S. G., R. Roskoski, Jr., K. Bauer, and F. Lipmann. 1973. Purification of the polyenzymes responsible for tyrocidine synthesis and their dissociation into subunits. Biochemistry 12:398-405.
    • (1973) Biochemistry , vol.12 , pp. 398-405
    • Lee, S.G.1    Roskoski Jr., R.2    Bauer, K.3    Lipmann, F.4
  • 29
    • 0022375455 scopus 로고
    • Cloning of the tyrocidine synthetase 1 gene from Bacillus brevis and its expression in Escherichia coli
    • Marahiel, M. A., M. Krause, and H. J. Skarpeid. 1985. Cloning of the tyrocidine synthetase 1 gene from Bacillus brevis and its expression in Escherichia coli. Mol. Gen. Genet. 201:231-236.
    • (1985) Mol. Gen. Genet. , vol.201 , pp. 231-236
    • Marahiel, M.A.1    Krause, M.2    Skarpeid, H.J.3
  • 30
    • 85036484341 scopus 로고    scopus 로고
    • Modular peptide synthetases involved in non-ribosomal peptide synthesis
    • in press
    • Marahiel, M. A., T. Stachelhaus, and H. D. Mootz. Modular peptide synthetases involved in non-ribosomal peptide synthesis. Chem. Rev., in press.
    • Chem. Rev.
    • Marahiel, M.A.1    Stachelhaus, T.2    Mootz, H.D.3
  • 31
    • 0024334515 scopus 로고
    • Gene cluster containing the genes for tyrocidine synthetases 1 and 2 from Bacillus brevis: Evidence for an operon
    • Mittenhuber, G., R. Weckermann, and M. A. Marahiel. 1989. Gene cluster containing the genes for tyrocidine synthetases 1 and 2 from Bacillus brevis: evidence for an operon. J. Bacteriol. 171:4881-4887.
    • (1989) J. Bacteriol. , vol.171 , pp. 4881-4887
    • Mittenhuber, G.1    Weckermann, R.2    Marahiel, M.A.3
  • 32
    • 0026488610 scopus 로고
    • Enniatin synthetasts from different fusaria exhibiting distinct amino acid specificities
    • Tokyo
    • Pieper, R., H. Kleinkauf, and R. Zocher. 1992. Enniatin synthetasts from different fusaria exhibiting distinct amino acid specificities. J. Antibiot. (Tokyo) 45:1273-1277.
    • (1992) J. Antibiot. , vol.45 , pp. 1273-1277
    • Pieper, R.1    Kleinkauf, H.2    Zocher, R.3
  • 33
    • 0030002729 scopus 로고    scopus 로고
    • D-Lysergyl peptide synthetase from the ergot fungus Claviceps purpurea
    • Riederer, B., M. Han, and U. Keller. 1996. D-Lysergyl peptide synthetase from the ergot fungus Claviceps purpurea. J. Biol. Chem. 271:27524-27530.
    • (1996) J. Biol. Chem. , vol.271 , pp. 27524-27530
    • Riederer, B.1    Han, M.2    Keller, U.3
  • 34
    • 0016640942 scopus 로고
    • Tyrocidine and the linear gramicidin. Do these peptide antibiotics play an antagonistic regulative role in sporulation?
    • Ristow, H., B. Schazschneider, K. Bauer, and H. Kleinkauf. 1975. Tyrocidine and the linear gramicidin. Do these peptide antibiotics play an antagonistic regulative role in sporulation? Biochim. Biophys. Acta 390:246-252.
    • (1975) Biochim. Biophys. Acta , vol.390 , pp. 246-252
    • Ristow, H.1    Schazschneider, B.2    Bauer, K.3    Kleinkauf, H.4
  • 35
    • 0014937517 scopus 로고
    • Tyrocidine biosynthesis by three complementary fractions from Bacillus brevis (ATCC 8185)
    • Roskoski, R., Jr., W. Gevers, H. Kleinkauf, and F. Lipmann. 1970. Tyrocidine biosynthesis by three complementary fractions from Bacillus brevis (ATCC 8185). Biochemistry 9:4839-4845.
    • (1970) Biochemistry , vol.9 , pp. 4839-4845
    • Roskoski Jr., R.1    Gevers, W.2    Kleinkauf, H.3    Lipmann, F.4
  • 36
    • 0013943586 scopus 로고
    • Studies on amino acid substitution in the biosynthesis of the antibiotic polypeptide tyrocidine
    • Ruttenberg, M. A., and B. Mach. 1966. Studies on amino acid substitution in the biosynthesis of the antibiotic polypeptide tyrocidine. Biochemistry 5: 2864-2869.
    • (1966) Biochemistry , vol.5 , pp. 2864-2869
    • Ruttenberg, M.A.1    Mach, B.2
  • 39
    • 0016358158 scopus 로고
    • Interaction between the antibiotic tyrocidine and DNA in vitro
    • Schazschneider, B., H. Ristow, and H. Kleinkauf. 1974. Interaction between the antibiotic tyrocidine and DNA in vitro. Nature 249:757-759.
    • (1974) Nature , vol.249 , pp. 757-759
    • Schazschneider, B.1    Ristow, H.2    Kleinkauf, H.3
  • 40
    • 0026348903 scopus 로고
    • An active serine is involved in covalent substrate amino acid binding at each reaction center of gramicidin S synthetase
    • Schlumbohm, W., T. Stein, C. Ullrich, J. Vater, M. Krause, M. A. Marahiel, V. Kruft, and B. Wittmann-Liebold. 1991. An active serine is involved in covalent substrate amino acid binding at each reaction center of gramicidin S synthetase. J. Biol. Chem. 266:23135-23141.
    • (1991) J. Biol. Chem. , vol.266 , pp. 23135-23141
    • Schlumbohm, W.1    Stein, T.2    Ullrich, C.3    Vater, J.4    Krause, M.5    Marahiel, M.A.6    Kruft, V.7    Wittmann-Liebold, B.8
  • 41
    • 0027087171 scopus 로고
    • The cyclic peptide synthetase catalyzing HC-toxin production in the filamentous fungus Cochliobolus carbonum is encoded by a 15.7-kilobase open reading frame
    • Scott-Craig, J. S., D. G. Panaccione, J. A. Pocard, and J. D. Walton. 1992. The cyclic peptide synthetase catalyzing HC-toxin production in the filamentous fungus Cochliobolus carbonum is encoded by a 15.7-kilobase open reading frame. J. Biol. Chem. 267:26044-26049.
    • (1992) J. Biol. Chem. , vol.267 , pp. 26044-26049
    • Scott-Craig, J.S.1    Panaccione, D.G.2    Pocard, J.A.3    Walton, J.D.4
  • 42
    • 0025004152 scopus 로고
    • The multifunctional peptide synthetase performing the first step of penicillin biosynthesis in Penicillium chrysogenum is a 421,073 dalton protein similar to Bacillus brevis peptide antibiotic synthetases
    • Smith, D. J., A. J. Earl, and G. Turner. 1990. The multifunctional peptide synthetase performing the first step of penicillin biosynthesis in Penicillium chrysogenum is a 421,073 dalton protein similar to Bacillus brevis peptide antibiotic synthetases. EMBO J. 9:2743-2750.
    • (1990) EMBO J. , vol.9 , pp. 2743-2750
    • Smith, D.J.1    Earl, A.J.2    Turner, G.3
  • 43
    • 0016700864 scopus 로고
    • Detection of specific sequences among DNA fragments separated by gel electrophoresis
    • Southern, E. M. 1975. Detection of specific sequences among DNA fragments separated by gel electrophoresis. J. Mol. Biol. 98:503-517.
    • (1975) J. Mol. Biol. , vol.98 , pp. 503-517
    • Southern, E.M.1
  • 44
    • 0028837014 scopus 로고
    • Modular structure of genes encoding multifunctional peptide synthetases required for non-ribosomal peptide synthesis
    • Stachelhaus, T., and M. A. Marahiel. 1995. Modular structure of genes encoding multifunctional peptide synthetases required for non-ribosomal peptide synthesis. FEMS Microbiol. Lett. 125:3-14.
    • (1995) FEMS Microbiol. Lett. , vol.125 , pp. 3-14
    • Stachelhaus, T.1    Marahiel, M.A.2
  • 45
    • 0028908601 scopus 로고
    • Modular structure of peptide synthetases revealed by dissection of the multifunctional enzyme GrsA
    • Stachelhaus, T., and M. A. Marahiel. 1995. Modular structure of peptide synthetases revealed by dissection of the multifunctional enzyme GrsA. J. Biol. Chem. 270:6163-6169.
    • (1995) J. Biol. Chem. , vol.270 , pp. 6163-6169
    • Stachelhaus, T.1    Marahiel, M.A.2
  • 47
    • 0029034197 scopus 로고
    • Rational design of peptide antibiotics by targeted replacement of bacterial and fungal domains
    • Stachelhaus, T., A. Schneider, and M. A. Marahiel. 1995. Rational design of peptide antibiotics by targeted replacement of bacterial and fungal domains. Science 269:69-72.
    • (1995) Science , vol.269 , pp. 69-72
    • Stachelhaus, T.1    Schneider, A.2    Marahiel, M.A.3
  • 48
    • 0028964503 scopus 로고
    • Gramicidin S synthetase 1 (phenylalanine racemase), a prototype of amino acid racemases containing the cofactor 4′-phosphopantetheine
    • Stein, T., B. Kluge, J. Vater, P. Franke, A. Otto, and B. Wittmann-Liebold. 1995. Gramicidin S synthetase 1 (phenylalanine racemase), a prototype of amino acid racemases containing the cofactor 4′-phosphopantetheine. Biochemistry 34:4633-4642.
    • (1995) Biochemistry , vol.34 , pp. 4633-4642
    • Stein, T.1    Kluge, B.2    Vater, J.3    Franke, P.4    Otto, A.5    Wittmann-Liebold, B.6
  • 50
    • 0020371308 scopus 로고
    • Isolation and properties of Bacillus brevis mutants unable to produce tyrocidine
    • Symons, D. C., and B. Hodgson. 1982. Isolation and properties of Bacillus brevis mutants unable to produce tyrocidine. J. Bacteriol. 151:580-590.
    • (1982) J. Bacteriol. , vol.151 , pp. 580-590
    • Symons, D.C.1    Hodgson, B.2
  • 51
    • 0027897646 scopus 로고
    • Analysis of bacitracin B using fast atom bombardment and tandem mass spectrometry
    • Tetler, L. W., S. N. Davey, and M. Morris. 1993. Analysis of bacitracin B using fast atom bombardment and tandem mass spectrometry. Biol. Mass Spectrom. 22:712-720.
    • (1993) Biol. Mass Spectrom. , vol.22 , pp. 712-720
    • Tetler, L.W.1    Davey, S.N.2    Morris, M.3
  • 52
    • 0028959563 scopus 로고
    • A putative new peptide synthase operon in Bacillus subtilis: Partial characterization
    • Reading
    • Tognoni, A., E. Franchi, C. Magistrelli, E. Colombo, P. Cosmina, and G. Grandi. 1995. A putative new peptide synthase operon in Bacillus subtilis: partial characterization. Microbiology (Reading) 141:645-648.
    • (1995) Microbiology , vol.141 , pp. 645-648
    • Tognoni, A.1    Franchi, E.2    Magistrelli, C.3    Colombo, E.4    Cosmina, P.5    Grandi, G.6
  • 53
    • 0026926521 scopus 로고
    • Four homologous domains in the primary structure of GrsB are related to domains in a superfamily of adenylate-forming enzymes
    • Turgay, K., M. Krause, and M. A. Marahiel. 1992. Four homologous domains in the primary structure of GrsB are related to domains in a superfamily of adenylate-forming enzymes. Mol. Microbiol. 6:529-546.
    • (1992) Mol. Microbiol. , vol.6 , pp. 529-546
    • Turgay, K.1    Krause, M.2    Marahiel, M.A.3
  • 54
    • 0028284699 scopus 로고
    • The peptide synthetase catalyzing cyclosporine production in Tolypocladium niveum is encoded by a giant 45.8-kilobase open reading frame
    • Weber, G., K. Schörgendorfer, E. Schneider-Scherzer, and E. Leitner. 1994. The peptide synthetase catalyzing cyclosporine production in Tolypocladium niveum is encoded by a giant 45.8-kilobase open reading frame. Curr. Genet 26:120-125.
    • (1994) Curr. Genet , vol.26 , pp. 120-125
    • Weber, G.1    Schörgendorfer, K.2    Schneider-Scherzer, E.3    Leitner, E.4
  • 55
    • 0024224534 scopus 로고
    • Complete nucleotide sequence of the tycA gene coding the tyrocidine synthetase 1 from Bacillus brevis
    • Weckermann, R., R. Fürbass, and M. A. Marahiel. 1988. Complete nucleotide sequence of the tycA gene coding the tyrocidine synthetase 1 from Bacillus brevis. Nucleic Acids Res. 16:11841.
    • (1988) Nucleic Acids Res. , vol.16 , pp. 11841
    • Weckermann, R.1    Fürbass, R.2    Marahiel, M.A.3


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