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Volumn , Issue , 2017, Pages 151-180

Physiology of actinobacteria

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EID: 85042459034     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1007/978-3-319-60339-1_7     Document Type: Chapter
Times cited : (1)

References (161)
  • 1
    • 0023673918 scopus 로고
    • Gene organization and structure of the Streptomyces lividans gal operon
    • Adams CW, Fornwald JA, Schmidt FJ et al (1988) Gene organization and structure of the Streptomyces lividans gal operon. J bacterial 170:203-212
    • (1988) J Bacterial , vol.170 , pp. 203-212
    • Adams, C.W.1    Fornwald, J.A.2    Schmidt, F.J.3
  • 2
    • 0031001449 scopus 로고    scopus 로고
    • Incomplete denitrification (NO and N2O) from nitrate by Streptomyces violaceoruber and S. Nitrosporeus revealed by acetylene inhibition and 15N gas chromatography quadrupole mass spectrometry analyses
    • 15N gas chromatography quadrupole mass spectrometry analyses. Naturwissenschaften 84:145-147
    • (1997) Naturwissenschaften , vol.84 , pp. 145-147
    • Albrecht, A.1    Ottow, J.2    Benckiser, G.3
  • 3
    • 0017194229 scopus 로고
    • Regulation of amino acid transport in growing cells of Streptomyces hydro-genans. II: Correlation between transport capacity and growth rate in chemostat culture
    • Alim S, Ring K (1976) Regulation of amino acid transport in growing cells of Streptomyces hydro-genans. II: correlation between transport capacity and growth rate in chemostat culture. Arch Microbiol 111:105-110
    • (1976) Arch Microbiol , vol.111 , pp. 105-110
    • Alim, S.1    Ring, K.2
  • 4
    • 0031025873 scopus 로고    scopus 로고
    • Identification of ATP-dependent phospho-fructokinase as a regulatory step in the glycolytic pathway of the actinomycete Streptomyces coelicolor A3 (2)
    • Alves AM, Euverink GJ, Bibb MJ, Dijkhuizen L (1997) Identification of ATP-dependent phospho-fructokinase as a regulatory step in the glycolytic pathway of the actinomycete Streptomyces coelicolor A3 (2). Appl Environ Microbiol 63:956-961
    • (1997) Appl Environ Microbiol , vol.63 , pp. 956-961
    • Alves, A.M.1    Euverink, G.J.2    Bibb, M.J.3    Dijkhuizen, L.4
  • 5
    • 35448940010 scopus 로고    scopus 로고
    • Phosphate control of phoA, phoC andphoD gene expression in Streptomyces coelicolor reveals significant differences in binding of PhoP to their promoter regions
    • Apel AK, Sola-Landa A, Rodríguez-García A, Martín JF (2007) Phosphate control of phoA, phoC andphoD gene expression in Streptomyces coelicolor reveals significant differences in binding of PhoP to their promoter regions. Microbiology 153:3527-3537
    • (2007) Microbiology , vol.153 , pp. 3527-3537
    • Apel, A.K.1    Sola-Landa, A.2    Rodríguez-García, A.3    Martín, J.F.4
  • 6
    • 0024758208 scopus 로고
    • Proteolytic enzymes from recombinant Streptomyces lividans TK24
    • Aretz W, Koller KP, Riess G (1989) Proteolytic enzymes from recombinant Streptomyces lividans TK24. FEMS Microbiol Lett 65:31-36
    • (1989) FEMS Microbiol Lett , vol.65 , pp. 31-36
    • Aretz, W.1    Koller, K.P.2    Riess, G.3
  • 7
    • 0027934796 scopus 로고
    • Effects of disruption of xylanase-encoding genes on the xylanolytic system of Streptomyces lividans
    • Arhin FF, Shareck F, Kluepfel D, Morosoli R (1994) Effects of disruption of xylanase-encoding genes on the xylanolytic system of Streptomyces lividans. J Bacteriol 176:4924-4930
    • (1994) J Bacteriol , vol.176 , pp. 4924-4930
    • Arhin, F.F.1    Shareck, F.2    Kluepfel, D.3    Morosoli, R.4
  • 8
    • 0031824606 scopus 로고    scopus 로고
    • Role of GlnK signal transduction protein in the regulation of nitrogen assimilation in Escherichia coli
    • Atkinson MR, Ninfa AJ (1998) Role of GlnK signal transduction protein in the regulation of nitrogen assimilation in Escherichia coli. Mol Microbiol 29:431-447
    • (1998) Mol Microbiol , vol.29 , pp. 431-447
    • Atkinson, M.R.1    Ninfa, A.J.2
  • 9
    • 0025686163 scopus 로고
    • Regulation of a thermostable a-amylase of Streptomyces thermoviola-ceus CUB74: Maltotriose is the smallest inducer
    • Bahri SM, Ward M (1990) Regulation of a thermostable a-amylase of Streptomyces thermoviola-ceus CUB74: maltotriose is the smallest inducer. Biochimie 72:8983-8895
    • (1990) Biochimie , vol.72 , pp. 8895-8983
    • Bahri, S.M.1    Ward, M.2
  • 10
    • 0024459199 scopus 로고
    • Regulation of nitrogen catabolic enzymes in Streptomyces clavuligerus
    • Bascaran V, Hardisson C, Brana AF (1989) Regulation of nitrogen catabolic enzymes in Streptomyces clavuligerus. J Gen Microbiol 135:2465-2474
    • (1989) J Gen Microbiol , vol.135 , pp. 2465-2474
    • Bascaran, V.1    Hardisson, C.2    Brana, A.F.3
  • 11
    • 0025258913 scopus 로고
    • Regulation of extracellular protease production in Streptomyces clavuligerus
    • Bascaran V, Hardisson C, Brana AF (1990) Regulation of extracellular protease production in Streptomyces clavuligerus. Appl Microbiol Biotechnol 34:208-213
    • (1990) Appl Microbiol Biotechnol , vol.34 , pp. 208-213
    • Bascaran, V.1    Hardisson, C.2    Brana, A.F.3
  • 12
    • 0014460778 scopus 로고
    • Regulation of biosynthesis of secondary metabolites
    • Behal V, Cudlin J, Vanek Z (1969) Regulation of biosynthesis of secondary metabolites. Folia Microbiol III 14:117-120
    • (1969) Folia Microbiol , vol.3 , Issue.14 , pp. 117-120
    • Behal, V.1    Cudlin, J.2    Vanek, Z.3
  • 13
    • 0025079161 scopus 로고
    • Overexpression of a Streptomyces viridochromogenes gene (GlnII) encoding a glutamine synthetase similar to those of eucaryotes confers resistance against the antibiotic phosphinothricyl-alanyl-alanine
    • Behrmann I, Hillemann D, Pühler A, Strauch E, Wohlleben W (1990) Overexpression of a Streptomyces viridochromogenes gene (glnII) encoding a glutamine synthetase similar to those of eucaryotes confers resistance against the antibiotic phosphinothricyl-alanyl-alanine. J Bacteriol 172:5326-5334
    • (1990) J Bacteriol , vol.172 , pp. 5326-5334
    • Behrmann, I.1    Hillemann, D.2    Pühler, A.3    Strauch, E.4    Wohlleben, W.5
  • 14
    • 0001501470 scopus 로고
    • CO metabolism in a thermophilic actinomycete, Streptomyces strains G26
    • Bell JM, Falconer C, Colby J, Williams E (1987) CO metabolism in a thermophilic actinomycete, Streptomyces strains G26. J Gen Microbiol 133:3445-3456
    • (1987) J Gen Microbiol , vol.133 , pp. 3445-3456
    • Bell, J.M.1    Falconer, C.2    Colby, J.3    Williams, E.4
  • 15
    • 14544294545 scopus 로고    scopus 로고
    • Bioactive microbial metabolites
    • Berdy J (2005) Bioactive microbial metabolites. J Antibiot 58:1-26
    • (2005) J Antibiot , vol.58 , pp. 1-26
    • Berdy, J.1
  • 16
    • 1342346617 scopus 로고    scopus 로고
    • In silico and transcriptional analysis of carbohydrate uptake systems of Streptomyces coelicolor A3(2)
    • Bertram R, Schlicht M, Mahr K, Nothaft H, Saier MH Jr, Titgemeyer F (2004) In silico and transcriptional analysis of carbohydrate uptake systems of Streptomyces coelicolor A3(2). J Bacteriol 186:1362-1373
    • (2004) J Bacteriol , vol.186 , pp. 1362-1373
    • Bertram, R.1    Schlicht, M.2    Mahr, K.3    Nothaft, H.4    Saier, M.H.5    Titgemeyer, F.6
  • 17
    • 15744383448 scopus 로고    scopus 로고
    • Regulation of secondary metabolism in Streptomycetes
    • Bibb MJ (2005) Regulation of secondary metabolism in Streptomycetes. Curr Op Microbiol 8:208-215
    • (2005) Curr Op Microbiol , vol.8 , pp. 208-215
    • Bibb, M.J.1
  • 18
    • 17744405737 scopus 로고
    • The agarase gene (DagA) of Streptomyces coelicolor A3(2): Affinity purification and characterization of the cloned gene product
    • Bibb MJ, Jones GH, Joseph R et al (1987) The agarase gene (dagA) of Streptomyces coelicolor A3(2): affinity purification and characterization of the cloned gene product. J Gen Microbiol 133:2089-2096
    • (1987) J Gen Microbiol , vol.133 , pp. 2089-2096
    • Bibb, M.J.1    Jones, G.H.2    Joseph, R.3
  • 19
    • 0023494723 scopus 로고
    • Cloning of Streptomyces griseus and Streptomyces lividans genes for glycerol dissimilation
    • Biro S, Chater KF (1987) Cloning of Streptomyces griseus and Streptomyces lividans genes for glycerol dissimilation. Gene 56:79-86
    • (1987) Gene , vol.56 , pp. 79-86
    • Biro, S.1    Chater, K.F.2
  • 20
    • 20444397992 scopus 로고    scopus 로고
    • Genome-scale analysis of Streptomyces coelicolor A3(2) metabolism
    • Borodina I, Krabben P, Nielsen J (2005) Genome-scale analysis of Streptomyces coelicolor A3(2) metabolism. Genome Res 15:820-829
    • (2005) Genome Res , vol.15 , pp. 820-829
    • Borodina, I.1    Krabben, P.2    Nielsen, J.3
  • 22
    • 0027205563 scopus 로고    scopus 로고
    • Proponyl-CoA carboxylase from Streptomyces coelicolor A3(2): Purification of the enzyme, cloning of the ppc gene and overexpression of the protein in a streptomycete
    • Bramwell H, Hunter IS, Coggins JR, Nimmo HG (1996) Proponyl-CoA carboxylase from Streptomyces coelicolor A3(2): purification of the enzyme, cloning of the ppc gene and overexpression of the protein in a streptomycete. Bioechem J 293:131-136
    • (1996) Bioechem J , vol.293 , pp. 131-136
    • Bramwell, H.1    Hunter, I.S.2    Coggins, J.R.3    Nimmo, H.G.4
  • 23
    • 0020283897 scopus 로고
    • Characterization of intracellular polysaccharides of Streptomyces
    • Brana AF, Manzanal MB, Hardisson C (1982) Characterization of intracellular polysaccharides of Streptomyces. Can J Microbiol 28:1320-1323
    • (1982) Can J Microbiol , vol.28 , pp. 1320-1323
    • Brana, A.F.1    Manzanal, M.B.2    Hardisson, C.3
  • 24
    • 0034047123 scopus 로고    scopus 로고
    • Biosynthesis of the polyene antifungal antibiotic nystatin in Streptomyces noursei ATCC 11455: Analysis of the gene cluster and deduction of the biosynthetic pathway
    • Brautase T, Sekurova ON, Sletta H et al (2000) Biosynthesis of the polyene antifungal antibiotic nystatin in Streptomyces noursei ATCC 11455: analysis of the gene cluster and deduction of the biosynthetic pathway. Chem Biol 7:395-403
    • (2000) Chem Biol , vol.7 , pp. 395-403
    • Brautase, T.1    Sekurova, O.N.2    Sletta, H.3
  • 25
    • 0030977043 scopus 로고    scopus 로고
    • The Streptomyces galP1 promoter was a novel RNA polymerase recognition sequence and is transcribed by a new RNA polymerase in vitro
    • Brawner ME, Matter SG, Babcock MJ, Westpheling J (1997) The Streptomyces galP1 promoter was a novel RNA polymerase recognition sequence and is transcribed by a new RNA polymerase in vitro. J Bacteriol 179:3222-3231
    • (1997) J Bacteriol , vol.179 , pp. 3222-3231
    • Brawner, M.E.1    Matter, S.G.2    Babcock, M.J.3    Westpheling, J.4
  • 26
    • 0037046271 scopus 로고    scopus 로고
    • Carbon catabolite repression in bacteria: Choice of the carbon source and autoregulatory limitation of sugar utilization
    • Brückner R, Titgemeyer F (2002) Carbon catabolite repression in bacteria: choice of the carbon source and autoregulatory limitation of sugar utilization. FEMS Microbiol Lett 209:141-148
    • (2002) FEMS Microbiol Lett , vol.209 , pp. 141-148
    • Brückner, R.1    Titgemeyer, F.2
  • 28
    • 0036148337 scopus 로고    scopus 로고
    • The candicidin gene cluster from Streptomyces griseus IMRU 3570
    • Campelo AB, Gil JA (2002) The candicidin gene cluster from Streptomyces griseus IMRU 3570. Microbiology 148:51-59
    • (2002) Microbiology , vol.148 , pp. 51-59
    • Campelo, A.B.1    Gil, J.A.2
  • 29
    • 9244222162 scopus 로고    scopus 로고
    • Analysis and manipulation of amphotericin biosynthetic genes by means of modified phage KC515 transduction techniques
    • Carmody M, Byrne B, Murphy B et al (2004) Analysis and manipulation of amphotericin biosynthetic genes by means of modified phage KC515 transduction techniques. Gene 343:107-115
    • (2004) Gene , vol.343 , pp. 107-115
    • Carmody, M.1    Byrne, B.2    Murphy, B.3
  • 30
    • 84960325313 scopus 로고    scopus 로고
    • Molecular evidence for the coordination of nitrogen and carbon metabolisms, revealed by a study on the transcriptional regulation of the agl3EFG operon that encodes a putative carbohydrate transporter in Streptomyces coelicolor
    • Cen X-F, Wang J-Z, Zhao G-P et al (2016) Molecular evidence for the coordination of nitrogen and carbon metabolisms, revealed by a study on the transcriptional regulation of the agl3EFG operon that encodes a putative carbohydrate transporter in Streptomyces coelicolor. Biochem Biophys Res Commun 471:510-514
    • (2016) Biochem Biophys Res Commun , vol.471 , pp. 510-514
    • Cen, X.-F.1    Wang, J.-Z.2    Zhao, G.-P.3
  • 31
    • 0025279664 scopus 로고
    • Extracellular metalloprotease gene of Streptomyces cacoi: Structure, nucleotide sequence and characterization of the cloned gene product
    • Chang PC, Kuo TC, Tsugita A, Lee YHM (1990) Extracellular metalloprotease gene of Streptomyces cacoi: structure, nucleotide sequence and characterization of the cloned gene product. Gene 88:87-95
    • (1990) Gene , vol.88 , pp. 87-95
    • Chang, P.C.1    Kuo, T.C.2    Tsugita, A.3    Lee, Y.4
  • 32
    • 0027384770 scopus 로고
    • Genetics of differentiation in Streptomyces
    • Chater KF (1993) Genetics of differentiation in Streptomyces. Annu Rev Microbiol 47:685-711
    • (1993) Annu Rev Microbiol , vol.47 , pp. 685-711
    • Chater, K.F.1
  • 34
    • 0019445507 scopus 로고
    • Nutrient utilization in actinomycetes. Induction of a-glucosidases in Streptomyces venezuelae
    • Chatterjee S, Vining LC (1981) Nutrient utilization in actinomycetes. Induction of a-glucosidases in Streptomyces venezuelae. Can J Microbiol 27:639-645
    • (1981) Can J Microbiol , vol.27 , pp. 639-645
    • Chatterjee, S.1    Vining, L.C.2
  • 35
    • 0024512581 scopus 로고
    • Crystallization ad preliminary analysis of glucose isomerase from Streptomyces albus
    • Dauter Z, Dauter M, Hemker J et al (1989) Crystallization ad preliminary analysis of glucose isomerase from Streptomyces albus. FEBS Lett 247:1-8
    • (1989) FEBS Lett , vol.247 , pp. 1-8
    • Dauter, Z.1    Dauter, M.2    Hemker, J.3
  • 36
    • 0024165414 scopus 로고
    • Biosynthesis of e-rhodomycinone from glucose by Streptomyces C5 and comparison with intermediary metabolism of other polyketide-producing streptomyce-tes
    • Dekleva ML, Strohl WR (1988) Biosynthesis of e-rhodomycinone from glucose by Streptomyces C5 and comparison with intermediary metabolism of other polyketide-producing streptomyce-tes. Can J Microbiol 34:1235-1240
    • (1988) Can J Microbiol , vol.34 , pp. 1235-1240
    • Dekleva, M.L.1    Strohl, W.R.2
  • 37
    • 23844490045 scopus 로고    scopus 로고
    • The high-affinity phosphate-binding protein PstS is accumulated under high fructose concentrations and mutation of the corresponding gene affects differentiation in Streptomyces lividans
    • Díaz M, Esteban A, Fernández-Abalos JM et al (2005) The high-affinity phosphate-binding protein PstS is accumulated under high fructose concentrations and mutation of the corresponding gene affects differentiation in Streptomyces lividans. Microbiology 151:2583-2592
    • (2005) Microbiology , vol.151 , pp. 2583-2592
    • Díaz, M.1    Esteban, A.2    Fernández-Abalos, J.M.3
  • 38
    • 0017356447 scopus 로고
    • Effect of primary metabolism on secondary metabolism
    • Drew SW, Demain AL (1977) Effect of primary metabolism on secondary metabolism. Annu Rev Microbiol 31:343-356
    • (1977) Annu Rev Microbiol , vol.31 , pp. 343-356
    • Drew, S.W.1    Demain, A.L.2
  • 40
    • 0014352652 scopus 로고
    • Trehalose phosphate synthesis in Streptomyces hygroscopicus: Purification of guanosine diphosphate D-glucose:D-glucose-6-phosphate 1-glucosyl-trasnferase
    • Elbein AD (1968) Trehalose phosphate synthesis in Streptomyces hygroscopicus: purification of guanosine diphosphate D-glucose:D-glucose-6-phosphate 1-glucosyl-trasnferase. J Bacteriol 96:1623-1631
    • (1968) J Bacteriol , vol.96 , pp. 1623-1631
    • Elbein, A.D.1
  • 42
    • 0014777998 scopus 로고
    • Partial purification and properties of L-phenylalanine ammonia-lyase from Streptomyces verticillatus
    • Emes AV, Vining LC (1970) Partial purification and properties of L-phenylalanine ammonia-lyase from Streptomyces verticillatus. Can J Biochem 48:613-622
    • (1970) Can J Biochem , vol.48 , pp. 613-622
    • Emes, A.V.1    Vining, L.C.2
  • 43
    • 0026483810 scopus 로고
    • Purification and characterization of a dual function 3-dehydroquinate dehydratase from Amycolatopsis methanolica
    • Euverink GJW, Hessels GI, Vrijbloed JW et al (1992) Purification and characterization of a dual function 3-dehydroquinate dehydratase from Amycolatopsis methanolica. J Gen Microbiol 138:2449-2457
    • (1992) J Gen Microbiol , vol.138 , pp. 2449-2457
    • Euverink, G.1    Hessels, G.I.2    Vrijbloed, J.W.3
  • 44
    • 0032855884 scopus 로고    scopus 로고
    • Nitrogen metabolism in Streptomyces coelicolor A3(2): Modification of glutamine synthetase I by an adenylyltransferase
    • Fink D, Falke D, Wohlleben W, Engels A (1999) Nitrogen metabolism in Streptomyces coelicolor A3(2): modification of glutamine synthetase I by an adenylyltransferase. Microbiology 145:2313-2322
    • (1999) Microbiology , vol.145 , pp. 2313-2322
    • Fink, D.1    Falke, D.2    Wohlleben, W.3    Engels, A.4
  • 45
    • 18744383916 scopus 로고    scopus 로고
    • Two transcriptional regulators GlnR and GlnRII are involved in regulation of nitrogen metabolism in Streptomyces coelicor A3(2)
    • Fink D, Weibschuch N, Reuther J, wohlleben W, Engels A (2002) Two transcriptional regulators GlnR and GlnRII are involved in regulation of nitrogen metabolism in Streptomyces coelicor A3(2). Mol Microbiol 46:331-347
    • (2002) Mol Microbiol , vol.46 , pp. 331-347
    • Fink, D.1    Weibschuch, N.2    Reuther, J.3    Wohlleben, W.4    Engels, A.5
  • 46
    • 0031848762 scopus 로고    scopus 로고
    • Cloning, expression and characterization of a type II 3-dehydroquinate dehydratase gene from Streptomyces hygroscopicus
    • Florova G, Denoya CD, Morgensten MR et al (1998) Cloning, expression and characterization of a type II 3-dehydroquinate dehydratase gene from Streptomyces hygroscopicus. Arch Biochem Biophys 350:298-306
    • (1998) Arch Biochem Biophys , vol.350 , pp. 298-306
    • Florova, G.1    Denoya, C.D.2    Morgensten, M.R.3
  • 47
    • 0017361672 scopus 로고
    • Catabolism of L-Lysine by Pseudomonas aeruginosa
    • Fothergill JC, Guest JR (1977) Catabolism of L-Lysine by Pseudomonas aeruginosa. J Gen Microbiol 99:139-155
    • (1977) J Gen Microbiol , vol.99 , pp. 139-155
    • Fothergill, J.C.1    Guest, J.R.2
  • 48
    • 0020791013 scopus 로고
    • Studies on the transport of anions and zwitterions of acidic amino acids in Streptomyces hydrogenans
    • Fritsch J, Gross W (1983) Studies on the transport of anions and zwitterions of acidic amino acids in Streptomyces hydrogenans. Z Naturforsch 38c:617-620
    • (1983) Z Naturforsch , vol.38c , pp. 617-620
    • Fritsch, J.1    Gross, W.2
  • 49
    • 0025643355 scopus 로고
    • Streptomyces thermoautotrophicus sp. Nov. A thermophilic CO- and H2-oxidizing obligate chemolithotroph
    • Gadkari D, Schricker K, Acker G et al (1990) Streptomyces thermoautotrophicus sp. Nov. A thermophilic CO- and H2-oxidizing obligate chemolithotroph. Appl Environ Microbiol 56:3727-3734
    • (1990) Appl Environ Microbiol , vol.56 , pp. 3727-3734
    • Gadkari, D.1    Schricker, K.2    Acker, G.3
  • 50
    • 0025742991 scopus 로고
    • The Mycobacterium tuberculosis shikimate pathway genes: Evolutionary relationship between biosynthetic and catabolic 3-dehydroquinases
    • Garbe T, Servos S, Hawkins A et al (1991) The Mycobacterium tuberculosis shikimate pathway genes: evolutionary relationship between biosynthetic and catabolic 3-dehydroquinases. Mol Gen Genet 228:385-392
    • (1991) Mol Gen Genet , vol.228 , pp. 385-392
    • Garbe, T.1    Servos, S.2    Hawkins, A.3
  • 52
    • 0021840485 scopus 로고
    • Characterization and regulation of p-aminobenzoic acid synthase from Streptomyces griseus
    • Gil JA, Naharro G, Villanueva JR, Martin JF (1985) Characterization and regulation of p-aminobenzoic acid synthase from Streptomyces griseus. J Gen Microbiol 131: 1279-1287
    • (1985) J Gen Microbiol , vol.131 , pp. 1279-1287
    • Gil, J.A.1    Naharro, G.2    Villanueva, J.R.3    Martin, J.F.4
  • 53
    • 0024506247 scopus 로고
    • Regulation of the production of hemi-cellulytic and cellulolytic enzymes by a Streptomyces sp. Growing on lignocellulose
    • Godden B, Legon T, Helvenstein P, Penninckx M (1989) Regulation of the production of hemi-cellulytic and cellulolytic enzymes by a Streptomyces sp. growing on lignocellulose. J Gen Microbiol 135:285-292
    • (1989) J Gen Microbiol , vol.135 , pp. 285-292
    • Godden, B.1    Legon, T.2    Helvenstein, P.3    Penninckx, M.4
  • 55
    • 0006183928 scopus 로고
    • Mutants of Streptomyces hygroscopicus deregulated in amylase and a-glucosidase formation
    • Grafe U, Bormann EJ, Roth M, Neigenfind M (1986) Mutants of Streptomyces hygroscopicus deregulated in amylase and a-glucosidase formation. Biotechnol Lett 8:615-620
    • (1986) Biotechnol Lett , vol.8 , pp. 615-620
    • Grafe, U.1    Bormann, E.J.2    Roth, M.3    Neigenfind, M.4
  • 56
    • 0015927061 scopus 로고
    • Multiple transport systems for basic amino acid transport in Streptomyces hydrogenans
    • Gross W, Burkhardt K-L (1973) Multiple transport systems for basic amino acid transport in Streptomyces hydrogenans. Biochim Biophys Acta 298:437-445
    • (1973) Biochim Biophys Acta , vol.298 , pp. 437-445
    • Gross, W.1    Burkhardt, K.-L.2
  • 57
    • 12944278548 scopus 로고
    • Effect of chloramphenicol on active amino acid transport
    • Gross W, Ring K (1971) Effect of chloramphenicol on active amino acid transport. FEBS Lett 4:319-322
    • (1971) FEBS Lett , vol.4 , pp. 319-322
    • Gross, W.1    Ring, K.2
  • 58
    • 84871002014 scopus 로고    scopus 로고
    • Identification of glucose kinase-dependent and—inde-pendent pathways for carbon control of primary metabolism, development and antibiotic production in Streptomyces coelicolor by quantitative proteomics
    • Gubbens J, Janus M, Florea BI et al (2012) Identification of glucose kinase-dependent and—inde-pendent pathways for carbon control of primary metabolism, development and antibiotic production in Streptomyces coelicolor by quantitative proteomics. Mol Microbiol 86:1490-1507
    • (2012) Mol Microbiol , vol.86 , pp. 1490-1507
    • Gubbens, J.1    Janus, M.2    Florea, B.I.3
  • 59
    • 2442671961 scopus 로고    scopus 로고
    • Identification of the Entner-Doudoroff pathway in an antibiotic producing actinomycete species
    • Gunnarsson N, Mortensen UH, Sosio M, Nielsen J (2004) Identification of the Entner-Doudoroff pathway in an antibiotic producing actinomycete species. Mol Microbiol 52:895-902
    • (2004) Mol Microbiol , vol.52 , pp. 895-902
    • Gunnarsson, N.1    Mortensen, U.H.2    Sosio, M.3    Nielsen, J.4
  • 60
    • 85007952976 scopus 로고
    • Amino acid metabolism in microorganisms. IV: L-methionine decarboxylase produced by a Streptomyces strain
    • Hagino H, Nakayama K (1968) Amino acid metabolism in microorganisms. IV: L-methionine decarboxylase produced by a Streptomyces strain. Agric Biol Chem 32:727-733
    • (1968) Agric Biol Chem , vol.32 , pp. 727-733
    • Hagino, H.1    Nakayama, K.2
  • 61
    • 0030754153 scopus 로고    scopus 로고
    • A novel alternate anaplerotic pathway to the glyoxylate cycle in streptomycetes
    • Han L, Reynolds KA (1997) A novel alternate anaplerotic pathway to the glyoxylate cycle in streptomycetes. J Bacteriol 179:5157-5164
    • (1997) J Bacteriol , vol.179 , pp. 5157-5164
    • Han, L.1    Reynolds, K.A.2
  • 62
    • 27944481182 scopus 로고    scopus 로고
    • All four Mycobacterium tuberculosis glnA genes encode glutamine synthetase activities but only GlnA1 is abundantly expressed and essential for bacterial homeostasis
    • Harth G, Maslesa-Galic S, Tullius MV, Horwitz MA (2005) All four Mycobacterium tuberculosis glnA genes encode glutamine synthetase activities but only GlnA1 is abundantly expressed and essential for bacterial homeostasis. Mol Microbiol 58:1157-1172
    • (2005) Mol Microbiol , vol.58 , pp. 1157-1172
    • Harth, G.1    Maslesa-Galic, S.2    Tullius, M.V.3    Horwitz, M.A.4
  • 63
    • 38349086492 scopus 로고    scopus 로고
    • The global role of ppGpp synthesis in morphological differentiation and antibiotic production in Streptomyces coelicolor A3(2)
    • Hesketh A, Chen WJ, Ryding J, Chang S, Bibb MJ (2007) The global role of ppGpp synthesis in morphological differentiation and antibiotic production in Streptomyces coelicolor A3(2). Genome Biol 8:R161
    • (2007) Genome Biol , vol.8 , pp. R161
    • Hesketh, A.1    Chen, W.J.2    Ryding, J.3    Chang, S.4    Bibb, M.J.5
  • 64
    • 0015858456 scopus 로고
    • Trehalose metabolism in germinating spores of Streptomyces hygroscopicus
    • Hey-Ferguson A, Mitchell M, Elbein AD (1973) Trehalose metabolism in germinating spores of Streptomyces hygroscopicus. J Bacteriol 116:1084-1085
    • (1973) J Bacteriol , vol.116 , pp. 1084-1085
    • Hey-Ferguson, A.1    Mitchell, M.2    Elbein, A.D.3
  • 65
    • 0027171913 scopus 로고
    • Genetic and biochemical characterization of the two glutamine synthetases GSI and GSII of the phosphinothricyl-alanyl-alanine producer, Streptomyces viridochromogenes Tü494
    • Hillemann D, Dammann T, Hillemann A, Wohlleben W (1993) Genetic and biochemical characterization of the two glutamine synthetases GSI and GSII of the phosphinothricyl-alanyl-alanine producer, Streptomyces viridochromogenes Tü494. J Gen Microbiol 139:1773-1783
    • (1993) J Gen Microbiol , vol.139 , pp. 1773-1783
    • Hillemann, D.1    Dammann, T.2    Hillemann, A.3    Wohlleben, W.4
  • 66
    • 0033925731 scopus 로고    scopus 로고
    • Primary metabolism and its control in streptomycetes: A most unusual group of bacteria
    • Hodgson DA (2000) primary metabolism and its control in streptomycetes: a most unusual group of bacteria. Adv Microb Physiol 42:47-238
    • (2000) Adv Microb Physiol , vol.42 , pp. 47-238
    • Hodgson, D.A.1
  • 67
    • 0029949473 scopus 로고    scopus 로고
    • Disruption of a glycogen-branching enzyme gene, glgB, specifically affects the sporulation-associated phase of glycogen accumulation in Streptomyces aureofaciens
    • Homerova D, Benada O, Kofronova O et al (1996) Disruption of a glycogen-branching enzyme gene, glgB, specifically affects the sporulation-associated phase of glycogen accumulation in Streptomyces aureofaciens. Microbiology 142:1201-1208
    • (1996) Microbiology , vol.142 , pp. 1201-1208
    • Homerova, D.1    Benada, O.2    Kofronova, O.3
  • 68
    • 0026668498 scopus 로고
    • Molecular genetic analysis of proline and tryptophan biosynthesis in Streptomyces coelicolor A3(2): Interaction between primary and secondary metabolism: A review
    • Hood DW, Heidstra R, Swoboda UK, Hodgson DA (1992) Molecular genetic analysis of proline and tryptophan biosynthesis in Streptomyces coelicolor A3(2): interaction between primary and secondary metabolism: a review. Gene 115:5-12
    • (1992) Gene , vol.115 , pp. 5-12
    • Hood, D.W.1    Heidstra, R.2    Swoboda, U.K.3    Hodgson, D.A.4
  • 69
    • 0037734084 scopus 로고    scopus 로고
    • The importance of amino acids as carbon sourcesfor Micromonospora echinospora (ATCC 15837)
    • Hoskisson PA, Sharples GP, Hobbs G (2003) The importance of amino acids as carbon sourcesfor Micromonospora echinospora (ATCC 15837). Lett Appl Microbiol 36:268-271
    • (2003) Lett Appl Microbiol , vol.36 , pp. 268-271
    • Hoskisson, P.A.1    Sharples, G.P.2    Hobbs, G.3
  • 70
    • 0033011688 scopus 로고    scopus 로고
    • The expression of the trpD, trpC and trpBA genes in Streptomyces coelicolor A3(2) is regulated by growth rate and growth phase but not by feedback repression
    • Hu DS, Hood DW, Heidstra R, Hodgson DA (1999) The expression of the trpD, trpC and trpBA genes in Streptomyces coelicolor A3(2) is regulated by growth rate and growth phase but not by feedback repression. Mol Microbiol 32:869-880
    • (1999) Mol Microbiol , vol.32 , pp. 869-880
    • Hu, D.S.1    Hood, D.W.2    Heidstra, R.3    Hodgson, D.A.4
  • 71
    • 59849105577 scopus 로고    scopus 로고
    • Reconstitution of Escherichia coli glutamine synthetase adenylyltrans-ferase from N-terminal and C-terminal fragments of the enzyme
    • Jiang P, Ninfa AJ (2009) Reconstitution of Escherichia coli glutamine synthetase adenylyltrans-ferase from N-terminal and C-terminal fragments of the enzyme. Biochemistry 48:415-423
    • (2009) Biochemistry , vol.48 , pp. 415-423
    • Jiang, P.1    Ninfa, A.J.2
  • 73
    • 0348038990 scopus 로고
    • Regulation of tryptophan metabolism and its relationship to actinomycin D synthesis
    • Ortiz-Ortiz L, Bojalil LF, Yakoleff V, Academic Press, New York
    • Katz E, Brown D, Hitchcock MJM et al (1984) Regulation of tryptophan metabolism and its relationship to actinomycin D synthesis. In: Ortiz-Ortiz L, Bojalil LF, Yakoleff V (eds) Biological, biochemical and biomedical aspects of actinomycetes. Academic Press, New York, pp 325-342
    • (1984) Biological, Biochemical and Biomedical Aspects of Actinomycetes , pp. 325-342
    • Katz, E.1    Brown, D.2    Hitchcock, M.3
  • 74
    • 0018909597 scopus 로고
    • L-lysine e-aminotransferase involved in cephamycin C synthesis in Streptomyces lactamdurans
    • Kern BA, Hendlin D, Inamine E (1980) L-lysine e-aminotransferase involved in cephamycin C synthesis in Streptomyces lactamdurans. Antimicrob Agents Chemother 17:679-685
    • (1980) Antimicrob Agents Chemother , vol.17 , pp. 679-685
    • Kern, B.A.1    Hendlin, D.2    Inamine, E.3
  • 75
    • 0019414018 scopus 로고
    • Cystathionine y-lyase activity in the cephamycin C producer Streptomyces lactamdurans
    • Kern BA, Inamine E (1981) Cystathionine y-lyase activity in the cephamycin C producer Streptomyces lactamdurans. J Antibiot 34:583-589
    • (1981) J Antibiot , vol.34 , pp. 583-589
    • Kern, B.A.1    Inamine, E.2
  • 76
    • 0037315167 scopus 로고    scopus 로고
    • Differentiation and anaerobiosis in standing liquid cultures of Streptomyces coelicolor
    • van Keulen G, Jonkers HM, Claessen D, Dijkhuizen L, Wösten HAB (2003) Differentiation and anaerobiosis in standing liquid cultures of Streptomyces coelicolor. J Bacteriol 185:1455-1458
    • (2003) J Bacteriol , vol.185 , pp. 1455-1458
    • Van Keulen, G.1    Jonkers, H.M.2    Claessen, D.3    Dijkhuizen, L.4    Wösten, H.5
  • 78
    • 0022516455 scopus 로고
    • The expression of the Escherichia coli lacZ gene in Streptomyces
    • King AA, Chater KF (1986) The expression of the Escherichia coli lacZ gene in Streptomyces. J Gen Microbiol 132:1739-1752
    • (1986) J Gen Microbiol , vol.132 , pp. 1739-1752
    • King, A.A.1    Chater, K.F.2
  • 79
    • 0015538478 scopus 로고
    • The isolation and characterization of auxotrophs of the aspartic acid family from Streptomyces lipmanii
    • Kirkpatrick JR, Godfrey OW (1973) The isolation and characterization of auxotrophs of the aspartic acid family from Streptomyces lipmanii. Folia Microbiol 18:90-101
    • (1973) Folia Microbiol , vol.18 , pp. 90-101
    • Kirkpatrick, J.R.1    Godfrey, O.W.2
  • 80
    • 0021962032 scopus 로고
    • Selective accumulation of unsulfated carbapenem antibiotics by sulfate transport-negative mutants of Streptomyces griseus subsp. Cryophilus C-19393
    • Kitano K, Nozaki Y, Imada A (1985) Selective accumulation of unsulfated carbapenem antibiotics by sulfate transport-negative mutants of Streptomyces griseus subsp. cryophilus C-19393. Agric Biol Chem 49:677-684
    • (1985) Agric Biol Chem , vol.49 , pp. 677-684
    • Kitano, K.1    Nozaki, Y.2    Imada, A.3
  • 81
    • 0024617758 scopus 로고
    • Cascading regulation of histidine ammonia-lyase activity from Streptomyces griseus
    • Kroening TA, Kendrick KE (1989) Cascading regulation of histidine ammonia-lyase activity from Streptomyces griseus. J Bacteriol 171:1100-1105
    • (1989) J Bacteriol , vol.171 , pp. 1100-1105
    • Kroening, T.A.1    Kendrick, K.E.2
  • 82
    • 0017734670 scopus 로고
    • Selection of a chemically defined medium for submerged cultivation of Streptomyces aureofaciens with high extracellular caseinolytic activity
    • Laluce C, Molinari R (1977) Selection of a chemically defined medium for submerged cultivation of Streptomyces aureofaciens with high extracellular caseinolytic activity. Biotechnol Bioeng 19:1863-1884
    • (1977) Biotechnol Bioeng , vol.19 , pp. 1863-1884
    • Laluce, C.1    Molinari, R.2
  • 83
    • 0027413345 scopus 로고
    • Aspartate aminotransferase and tylosin biosynthesis in Streptomyces fra-diae
    • Lee SH, Lee KJ (1993) Aspartate aminotransferase and tylosin biosynthesis in Streptomyces fra-diae. Appl Environ Microbiol 59:822-827
    • (1993) Appl Environ Microbiol , vol.59 , pp. 822-827
    • Lee, S.H.1    Lee, K.J.2
  • 84
    • 6444226377 scopus 로고    scopus 로고
    • Crotonyl-coenzyme A reductase provides methylmalonyl-CoA precursors for monensin biosynthesis by Streptomyces cinnamonensis in an oil-based extended fermentation
    • Li CX, Florova G, Akopiants K, Reynolds KA (2004) Crotonyl-coenzyme A reductase provides methylmalonyl-CoA precursors for monensin biosynthesis by Streptomyces cinnamonensis in an oil-based extended fermentation. Microbiology 150:3463-3472
    • (2004) Microbiology , vol.150 , pp. 3463-3472
    • Li, C.X.1    Florova, G.2    Akopiants, K.3    Reynolds, K.A.4
  • 85
    • 0029555906 scopus 로고
    • Regulation of valine catabolism by ammonium in Streptomyces ambofaciens, producer of spiramycin
    • Lounes A, Lebrihi A, Benslimane C et al (1995) Regulation of valine catabolism by ammonium in Streptomyces ambofaciens, producer of spiramycin. Can J microbial 31:304-311
    • (1995) Can J Microbial , vol.31 , pp. 304-311
    • Lounes, A.1    Lebrihi, A.2    Benslimane, C.3
  • 86
  • 87
    • 0024486867 scopus 로고
    • Lysine catabolism in Streptomyces spp is primarily through cadaverine: ß-lactam producers also make a-aminoadipate
    • Madduri K, Stuttard C, Vining LC (1989) Lysine catabolism in Streptomyces spp is primarily through cadaverine: ß-lactam producers also make a-aminoadipate. J Bacterial 171:299-302
    • (1989) J Bacterial , vol.171 , pp. 299-302
    • Madduri, K.1    Stuttard, C.2    Vining, L.C.3
  • 88
    • 65549121502 scopus 로고    scopus 로고
    • Streptomyces development in colonies and soils
    • Manteca A, Sanchez J (2009) Streptomyces development in colonies and soils. Appl Environ Microbiol 75:2920-2924
    • (2009) Appl Environ Microbiol , vol.75 , pp. 2920-2924
    • Manteca, A.1    Sanchez, J.2
  • 89
    • 0019292120 scopus 로고
    • Control of antibiotic synthesis
    • Martín JF, Demain AL (1980) Control of antibiotic synthesis. Microbiol Rev 44:230-251
    • (1980) Microbiol Rev , vol.44 , pp. 230-251
    • Martín, J.F.1    Demain, A.L.2
  • 90
    • 0030780265 scopus 로고
    • A glgC gene essential only for the first two spatially distinct phases of glycogen synthesis in Streptomyces coelicolor A3(2)
    • Martin MC, Schneider D, Bruton CJ et al (1977) A glgC gene essential only for the first two spatially distinct phases of glycogen synthesis in Streptomyces coelicolor A3(2). J Bacteriol 179:7784-7789
    • (1977) J Bacteriol , vol.179 , pp. 7784-7789
    • Martin, M.C.1    Schneider, D.2    Bruton, C.J.3
  • 91
    • 0023442378 scopus 로고
    • Metabolism of endogenous trehalose by Streptomyces griseus spores and by spores or cells of other actinomycetes
    • McBride MJ, Ensign JC (1987) Metabolism of endogenous trehalose by Streptomyces griseus spores and by spores or cells of other actinomycetes. J Bacteriol 169:5002-5007
    • (1987) J Bacteriol , vol.169 , pp. 5002-5007
    • McBride, M.J.1    Ensign, J.C.2
  • 92
    • 0020062322 scopus 로고
    • Regulation of cephamycin C synthesis, aspartokinase, dihydrodipicolinic acid synthase and homoserine dehydrogenase by aspartic acid family amino acids in Streptomyces clavuligerus
    • Mendelovitz S, Aharonowitz Y (1982) Regulation of cephamycin C synthesis, aspartokinase, dihydrodipicolinic acid synthase and homoserine dehydrogenase by aspartic acid family amino acids in Streptomyces clavuligerus. Antimicrob Agents Chemother 21:74-84
    • (1982) Antimicrob Agents Chemother , vol.21 , pp. 74-84
    • Mendelovitz, S.1    Aharonowitz, Y.2
  • 93
  • 95
    • 0036094071 scopus 로고    scopus 로고
    • The structure of a pyrophosphate-dependent phosphofructokinase from the Lyme disease spirochete Borrelia burgdorferi
    • Moore SA, Ronimus RS, Roberson RS, Morgan HW (2002) The structure of a pyrophosphate-dependent phosphofructokinase from the Lyme disease spirochete Borrelia burgdorferi. Structure (Camb) 10:659-671
    • (2002) Structure (Camb) , vol.10 , pp. 659-671
    • Moore, S.A.1    Ronimus, R.S.2    Roberson, R.S.3    Morgan, H.W.4
  • 96
    • 0018353273 scopus 로고
    • Production of L-asparaginase by Streptomyces karnatakensis and Streptomyces venezuelae
    • Mostafa SA (1979) production of L-asparaginase by Streptomyces karnatakensis and Streptomyces venezuelae. Zbl Bakt II Abt 134:429-436
    • (1979) Zbl Bakt II Abt , vol.134 , pp. 429-436
    • Mostafa, S.A.1
  • 97
    • 0019164545 scopus 로고
    • Regulatory control of 3-deoxy-D-arabino-heptulosonic acid 7-phosphate synthetase in Streptomyces antibioticus
    • Murphy MF, Katz E (1980) regulatory control of 3-deoxy-D-arabino-heptulosonic acid 7-phosphate synthetase in Streptomyces antibioticus. Can J Microbiol 26:874-880
    • (1980) Can J Microbiol , vol.26 , pp. 874-880
    • Murphy, M.F.1    Katz, E.2
  • 98
    • 85042441189 scopus 로고
    • Cystathionine y-lyase of Streptomyces phaeochromo-genes: The occurrence of cystathionine y-lyase in filamentous bacteria and its purification and characterization
    • Nagawasa T, Kanzaki H, Yamada H (1984) Cystathionine y-lyase of Streptomyces phaeochromo-genes: the occurrence of cystathionine y-lyase in filamentous bacteria and its purification and characterization. J Biol Chem 252:5267-5273
    • (1984) J Biol Chem , vol.252 , pp. 5267-5273
    • Nagawasa, T.1    Kanzaki, H.2    Yamada, H.3
  • 99
    • 0030791783 scopus 로고    scopus 로고
    • Amylase and chitinase genes in Streptomyces lividans are regulated by reg1, a pleiotropic regulatory gene
    • Nguyen KT, Frabcou F, Virolle MJ, Guerineau M (1997) Amylase and chitinase genes in Streptomyces lividans are regulated by reg1, a pleiotropic regulatory gene. J Bacteriol 179:6383-6390
    • (1997) J Bacteriol , vol.179 , pp. 6383-6390
    • Nguyen, K.T.1    Frabcou, F.2    Virolle, M.J.3    Guerineau, M.4
  • 100
    • 0028922107 scopus 로고
    • The induction of valine dehydrogenase activity from Streptomyces by L-valine is not repressed by ammonium
    • Nguyen KT, Nguyen LT, Behal V (1995) The induction of valine dehydrogenase activity from Streptomyces by L-valine is not repressed by ammonium. Biotechnol Lett 17:31-34
    • (1995) Biotechnol Lett , vol.17 , pp. 31-34
    • Nguyen, K.T.1    Nguyen, L.T.2    Behal, V.3
  • 101
    • 0029799660 scopus 로고    scopus 로고
    • An oligopeptide permesase responsible for the import of an extracellular signal governing aerial mycelium formation in Streptomyces coelicolor
    • Nodwell JR, McGovern K, Losick R (1996) An oligopeptide permesase responsible for the import of an extracellular signal governing aerial mycelium formation in Streptomyces coelicolor. Mol Microbiol 22:881-893
    • (1996) Mol Microbiol , vol.22 , pp. 881-893
    • Nodwell, J.R.1    McGovern, K.2    Losick, R.3
  • 102
    • 0030891706 scopus 로고    scopus 로고
    • Nitrogen source regulates expression of alanine dehydrogenase isoenzymes in Streptomyces avermitilis in a chemically defined medium
    • Novak J, Kopecky J, Vanek Z (1997) Nitrogen source regulates expression of alanine dehydrogenase isoenzymes in Streptomyces avermitilis in a chemically defined medium. Can J Microbiol 43:189-193
    • (1997) Can J Microbiol , vol.43 , pp. 189-193
    • Novak, J.1    Kopecky, J.2    Vanek, Z.3
  • 103
    • 0028821817 scopus 로고
    • The biosynthesis of monensin-A: Thymine, ß-aminoisobutyrate and methacrylate metabolism in Streptomyces cinnamonensis
    • O’Hagan D, Rogers SV, Duffin GR, Reynolds KA (1995) The biosynthesis of monensin-A: thymine, ß-aminoisobutyrate and methacrylate metabolism in Streptomyces cinnamonensis. J Antibiot 48:1280-1287
    • (1995) J Antibiot , vol.48 , pp. 1280-1287
    • O’Hagan, D.1    Rogers, S.V.2    Duffin, G.R.3    Reynolds, K.A.4
  • 104
    • 0017409948 scopus 로고
    • Effect of glucose and ammonium on the formation of xanthine dehydrogenase of Streptomyces sp. (Studies on the control of purine base metabolism in Streptomyces. Part II)
    • Ohe T, Watanabe Y (1977) Effect of glucose and ammonium on the formation of xanthine dehydrogenase of Streptomyces sp. (Studies on the control of purine base metabolism in Streptomyces. Part II). Agric Biol Chem 41:1161-1170
    • (1977) Agric Biol Chem , vol.41 , pp. 1161-1170
    • Ohe, T.1    Watanabe, Y.2
  • 105
    • 50249084003 scopus 로고    scopus 로고
    • Improving production of bioactive secondary metabolites in actinomycetes by metabolic engineering
    • Olano C, Lombo F, Mendez C, Salas JA (2008) Improving production of bioactive secondary metabolites in actinomycetes by metabolic engineering. Metab Eng 10:281-292
    • (2008) Metab Eng , vol.10 , pp. 281-292
    • Olano, C.1    Lombo, F.2    Mendez, C.3    Salas, J.A.4
  • 106
    • 0027191883 scopus 로고
    • Location of the genes for anthranilate synthase in Streptomyces venezuelae ISP5230: Genetic mapping after integration of the cloned genes
    • Paradkar AS, Stuttard C, vining LC (1993) Location of the genes for anthranilate synthase in Streptomyces venezuelae ISP5230: genetic mapping after integration of the cloned genes. J Gen Microbiol 139:687-694
    • (1993) J Gen Microbiol , vol.139 , pp. 687-694
    • Paradkar, A.S.1    Stuttard, C.2    Vining, L.C.3
  • 107
    • 26844505090 scopus 로고    scopus 로고
    • From dormant to germinating spores of Streptomyces coelicolor A3(2): New perspectives from the crp null mutant
    • Piette A, Derouaux A, Gerkens P et al (2005) From dormant to germinating spores of Streptomyces coelicolor A3(2): new perspectives from the crp null mutant. J Proteome Res 4:1699-1708
    • (2005) J Proteome Res , vol.4 , pp. 1699-1708
    • Piette, A.1    Derouaux, A.2    Gerkens, P.3
  • 108
    • 0013571685 scopus 로고
    • Streptomyces rimosus extracellular proteases. 1: Characterization and evaluation of various crude preparartions
    • Pokorny M, Lj V, Turk V et al (1979) Streptomyces rimosus extracellular proteases. 1: Characterization and evaluation of various crude preparartions. Eur J Appl Microbiol 8:81-90
    • (1979) Eur J Appl Microbiol , vol.8 , pp. 81-90
    • Pokorny, M.1    Lj, V.2    Turk, V.3
  • 110
    • 79953265166 scopus 로고    scopus 로고
    • Genome-wide analysis of the role of GlnR in Streptomyces venezuelae provides new insights into global nitrogen regulation in actinomycetes
    • Pullan T, Chandra G, Bibb MJ, Merrick M (2011) Genome-wide analysis of the role of GlnR in Streptomyces venezuelae provides new insights into global nitrogen regulation in actinomycetes. BMC Genomics 12:175. doi:10.1186/1471-2164-12-175
    • (2011) BMC Genomics , vol.12 , pp. 175
    • Pullan, T.1    Chandra, G.2    Bibb, M.J.3    Merrick, M.4
  • 112
    • 0037469308 scopus 로고    scopus 로고
    • Cloning and characterization of a gene cluster for geldanamycin production in Streptomyces hygroscopicus NRRL 3602
    • Rascher A, Hu Z, Viswanathan N et al (2003) Cloning and characterization of a gene cluster for geldanamycin production in Streptomyces hygroscopicus NRRL 3602. FEMS Microbiol Lett 218:223-230
    • (2003) FEMS Microbiol Lett , vol.218 , pp. 223-230
    • Rascher, A.1    Hu, Z.2    Viswanathan, N.3
  • 113
    • 33845740146 scopus 로고    scopus 로고
    • Nitrogen metabolism in Streptomyces coelicolor: Transcriptional and post-translational regulation
    • Reuther J, Wohlleben W (2007) Nitrogen metabolism in Streptomyces coelicolor: transcriptional and post-translational regulation. J Mol Microbiol Biotechnol 12:139-146
    • (2007) J Mol Microbiol Biotechnol , vol.12 , pp. 139-146
    • Reuther, J.1    Wohlleben, W.2
  • 114
    • 37049080276 scopus 로고
    • Butyrate metabolism in streptomycetes. Characterization of an intramolecular vicinal interchange rearrangement linking isobutyrate and butyrate in Streptomyces cinnamonensis
    • Reynolds KA, O’Hagan D, Gani D, Robinson JA (1988) Butyrate metabolism in streptomycetes. Characterization of an intramolecular vicinal interchange rearrangement linking isobutyrate and butyrate in Streptomyces cinnamonensis. J Chem Soc Perkin Trans 1:3195-3207
    • (1988) J Chem Soc Perkin Trans , vol.1 , pp. 3195-3207
    • Reynolds, K.A.1    O’Hagan, D.2    Gani, D.3    Robinson, J.A.4
  • 115
    • 46449120734 scopus 로고    scopus 로고
    • Hopwood DA, van Wezel GP (2008) feast or famine: The global regulator DasR links nutrient stress to antibiotic production by Streptomyces
    • Rigali S, Titgemeyer F, Barends S, Mulder S, Thomae AW, Hopwood DA, van Wezel GP (2008) feast or famine: the global regulator DasR links nutrient stress to antibiotic production by Streptomyces. EMBO Rep 9:670-675
    • EMBO Rep , vol.9 , pp. 670-675
    • Rigali, S.1    Titgemeyer, F.2    Barends, S.3    Mulder, S.4    Thomae, A.W.5
  • 116
    • 0017756171 scopus 로고
    • Stimulation of active uptake of 2-aminobutyric acid in Streptomyces hydrogenans by exogenous dibutyryl cyclic AMP
    • Ring K, Foit B, Ehle H (1977) Stimulation of active uptake of 2-aminobutyric acid in Streptomyces hydrogenans by exogenous dibutyryl cyclic AMP. FEMS Microbiol Lett 2:27-30
    • (1977) FEMS Microbiol Lett , vol.2 , pp. 27-30
    • Ring, K.1    Foit, B.2    Ehle, H.3
  • 117
    • 0030296996 scopus 로고    scopus 로고
    • Induction of L-lysine e-aminotransferase by L-lysine in Streptomyces clavuligerus, producer of cephalosporins
    • Rius N, Maeda K, Demain AL (1996) Induction of L-lysine e-aminotransferase by L-lysine in Streptomyces clavuligerus, producer of cephalosporins. FEMS Microbiol Lett 144:207-211
    • (1996) FEMS Microbiol Lett , vol.144 , pp. 207-211
    • Rius, N.1    Maeda, K.2    Demain, A.L.3
  • 118
    • 0026517235 scopus 로고
    • Cloning and high-level expression of chitinase-encoding gene of Streptomyces plicatus
    • Robbins PW, Overbye K, Albright C et al (1992) Cloning and high-level expression of chitinase-encoding gene of Streptomyces plicatus. Gene 111:69-76
    • (1992) Gene , vol.111 , pp. 69-76
    • Robbins, P.W.1    Overbye, K.2    Albright, C.3
  • 119
    • 34547144162 scopus 로고    scopus 로고
    • Genome-wide transcriptomic and proteomic analysis of the primary response to phosphate limitation in Streptomyces coelicolor M145 and in a AphoP mutant
    • Rodríguez-García A, Barreiro C, Santos-Beneit F, Sola-Landa A, Martín JF (2007) Genome-wide transcriptomic and proteomic analysis of the primary response to phosphate limitation in Streptomyces coelicolor M145 and in a AphoP mutant. Proteomics 7:2410-2429
    • (2007) Proteomics , vol.7 , pp. 2410-2429
    • Rodríguez-García, A.1    Barreiro, C.2    Santos-Beneit, F.3    Sola-Landa, A.4    Martín, J.F.5
  • 120
    • 67249083329 scopus 로고    scopus 로고
    • Phosphate control over nitrogen metabolism in Streptomyces coelicolor: Direct and indirect negative control of glnR, glnA, glnII and amtB expression by the response regulator PhoP
    • Rodríguez-García A., Sola-Landa A, Apel K., Santos Beneit and Martín J.F. (2009) Phosphate control over nitrogen metabolism in Streptomyces coelicolor: direct and indirect negative control of glnR, glnA, glnII and amtB expression by the response regulator PhoP. Nucl. Acids Res 37: 3230-3242
    • (2009) Nucl. Acids Res , vol.37 , pp. 3230-3242
    • Rodríguez-García, A.1    Sola-Landa, A.2    Apel, K.3    Beneit, S.4    Martín, J.F.5
  • 121
    • 0017521785 scopus 로고
    • Two systems for the uptake of phosphate in Escherichia coli
    • Rosenberg H, Gerdes RG, Chegwidden K (1977) Two systems for the uptake of phosphate in Escherichia coli. J Bacteriol 131:505-511
    • (1977) J Bacteriol , vol.131 , pp. 505-511
    • Rosenberg, H.1    Gerdes, R.G.2    Chegwidden, K.3
  • 122
    • 0018387840 scopus 로고
    • Energy coupling to the transport of inorganic phosphate in Escherichia coli K12
    • Rosenberg H, Gerdes RG, Harold FM (1979) Energy coupling to the transport of inorganic phosphate in Escherichia coli K12. Biochem J 178:133-137
    • (1979) Biochem J , vol.178 , pp. 133-137
    • Rosenberg, H.1    Gerdes, R.G.2    Harold, F.M.3
  • 123
    • 33750969392 scopus 로고    scopus 로고
    • Engineering of primary carbohydrate metabolism for increased production of actinorhodin in Streptomyces coelicolor
    • Ryu YG, Butler MJ, Chater KF, Lee KJ (2006) Engineering of primary carbohydrate metabolism for increased production of actinorhodin in Streptomyces coelicolor. Appl Environ Microbiol 72:7132-7139
    • (2006) Appl Environ Microbiol , vol.72 , pp. 7132-7139
    • Ryu, Y.G.1    Butler, M.J.2    Chater, K.F.3    Lee, K.J.4
  • 124
    • 0028104094 scopus 로고
    • The bacterial phosphotransferase system: New frontiers 30 years later
    • Saier MH Jr, Reizer J (1994) The bacterial phosphotransferase system: new frontiers 30 years later. Mol Microbiol 13:755-764
    • (1994) Mol Microbiol , vol.13 , pp. 755-764
    • Saier, M.H.1    Reizer, J.2
  • 125
    • 0037010892 scopus 로고    scopus 로고
    • Metabolic regulation of fermentation processes
    • Sanchez S, Demain AL (2002) Metabolic regulation of fermentation processes. Enz Microbial Technol 31:895-906
    • (2002) Enz Microbial Technol , vol.31 , pp. 895-906
    • Sanchez, S.1    Demain, A.L.2
  • 126
    • 51149094964 scopus 로고    scopus 로고
    • Phosphate-dependent regulation of the low- and high-affinity transport systems in the model actinomycete Streptomyces coelicolor
    • Santos-Beneit F, Rodríguez-García A, Franco-Domínguez E, Martín JF (2008) Phosphate-dependent regulation of the low- and high-affinity transport systems in the model actinomycete Streptomyces coelicolor. Microbiology 154:2356-2370
    • (2008) Microbiology , vol.154 , pp. 2356-2370
    • Santos-Beneit, F.1    Rodríguez-García, A.2    Franco-Domínguez, E.3    Martín, J.F.4
  • 127
    • 0017592582 scopus 로고
    • Biosynthesis of streptothricin antibiotics. VI: Mechanisms of ß-lysine and its peptide formation
    • Sawada Y, Nakashima S, Taniyama H (1977) Biosynthesis of streptothricin antibiotics. VI: mechanisms of ß-lysine and its peptide formation. Chem Pharm Bull 25:3210-3217
    • (1977) Chem Pharm Bull , vol.25 , pp. 3210-3217
    • Sawada, Y.1    Nakashima, S.2    Taniyama, H.3
  • 128
    • 0030896572 scopus 로고    scopus 로고
    • The Streptomyces ATP binding component MsiK assists in cellobiose and maltose transport
    • Schloesser A, Kampers T, Schrempf H (1997) The Streptomyces ATP binding component MsiK assists in cellobiose and maltose transport. J Bacteriol 179:2092-2095
    • (1997) J Bacteriol , vol.179 , pp. 2092-2095
    • Schloesser, A.1    Kampers, T.2    Schrempf, H.3
  • 129
    • 0020536753 scopus 로고
    • Glycerol catabolic enzymes and their regulation in wild-type and mutant strains of Streptomyces coelicolor A3(2)
    • Seno ET, Chater KF (1983) Glycerol catabolic enzymes and their regulation in wild-type and mutant strains of Streptomyces coelicolor A3(2). J Gen Microbiol 129:1403-1413
    • (1983) J Gen Microbiol , vol.129 , pp. 1403-1413
    • Seno, E.T.1    Chater, K.F.2
  • 130
    • 0021134260 scopus 로고
    • Suppression of nitrate utilization by ammonium and its relationship to chloramphenicol production in Streptomyces venezuelae
    • Shapiro S, Vining LC (1984) Suppression of nitrate utilization by ammonium and its relationship to chloramphenicol production in Streptomyces venezuelae. Can J Microbiol 30:798-804
    • (1984) Can J Microbiol , vol.30 , pp. 798-804
    • Shapiro, S.1    Vining, L.C.2
  • 131
    • 1842412960 scopus 로고
    • Regulation of extracellular alkaline protease biosynthesis in a strain of Streptomyces sp. Kor
    • Shin H-S, Lee KJ (1986) Regulation of extracellular alkaline protease biosynthesis in a strain of Streptomyces sp. Kor. J Microbiol 24:32-37
    • (1986) J Microbiol , vol.24 , pp. 32-37
    • Shin, H.-S.1    Lee, K.J.2
  • 132
    • 65649111759 scopus 로고    scopus 로고
    • Engineered Streptomyces platensis strains that overproduce antibiotics platensimycin and platencin
    • Smanski MJ, Peterson RM, Rajski SR, Shen B (2009) Engineered Streptomyces platensis strains that overproduce antibiotics platensimycin and platencin. Antimicrob Agents Chemother 53:1299-1304
    • (2009) Antimicrob Agents Chemother , vol.53 , pp. 1299-1304
    • Smanski, M.J.1    Peterson, R.M.2    Rajski, S.R.3    Shen, B.4
  • 133
    • 0029094244 scopus 로고
    • Interaction between primary and secondary metabolism in Streptomyces coelicolor A3(2): Role of pyrroline-5-carboxylate dehydrogenase
    • Smith DDS, Wood NJ, Hodgson DA (1995) Interaction between primary and secondary metabolism in Streptomyces coelicolor A3(2): role of pyrroline-5-carboxylate dehydrogenase. Microbiology 141:1739-1744
    • (1995) Microbiology , vol.141 , pp. 1739-1744
    • Smith, D.1    Wood, N.J.2    Hodgson, D.A.3
  • 134
    • 0038284769 scopus 로고    scopus 로고
    • The two-component PhoR-PhoP system controls both primary metabolism and secondary metabolite biosynthesis in Streptomyces lividans
    • Sola-Landa A, Moura RS, Martín JF (2003) The two-component PhoR-PhoP system controls both primary metabolism and secondary metabolite biosynthesis in Streptomyces lividans. Proc Natl Acad Sci U S A 100:6133-6138
    • (2003) Proc Natl Acad Sci U S A , vol.100 , pp. 6133-6138
    • Sola-Landa, A.1    Moura, R.S.2    Martín, J.F.3
  • 136
    • 19944370498 scopus 로고    scopus 로고
    • Binding of PhoP to promoters of phosphate-regulated genes in Streptomyces coelicolor: Identification of PHO boxes
    • Sola-Landa A, Rodríguez-García A, Franco-Domínguez E, Martín JF (2005) Binding of PhoP to promoters of phosphate-regulated genes in Streptomyces coelicolor: identification of PHO boxes. Mol Microbiol 56:1373-1385
    • (2005) Mol Microbiol , vol.56 , pp. 1373-1385
    • Sola-Landa, A.1    Rodríguez-García, A.2    Franco-Domínguez, E.3    Martín, J.F.4
  • 137
    • 33744552662 scopus 로고    scopus 로고
    • Y-butyrolactones: Streptomyces signaling molecules regulating antibiotic production and differentiation
    • Takano E (2006) y-butyrolactones: Streptomyces signaling molecules regulating antibiotic production and differentiation. Curr Op Microbiol 9:287-294
    • (2006) Curr Op Microbiol , vol.9 , pp. 287-294
    • Takano, E.1
  • 138
    • 79952535833 scopus 로고    scopus 로고
    • Proteomic analysis of the GlnR-mediated response to nitrogen limitation in Streptomyces coelicolor M145
    • Tiffert Y, Franz-Wachtel M, Fladerer C et al (2011) Proteomic analysis of the GlnR-mediated response to nitrogen limitation in Streptomyces coelicolor M145. Appl Microbiol Biotechnol 89:1149-1159
    • (2011) Appl Microbiol Biotechnol , vol.89 , pp. 1149-1159
    • Tiffert, Y.1    Franz-Wachtel, M.2    Fladerer, C.3
  • 139
    • 38449097896 scopus 로고    scopus 로고
    • The Streptomyces coeli-color GlnR regulon: Identification of new GlnR targets and evidence for a central role of GlnR in nitrogen metabolism in actinomycetes
    • Tiffert Y, Supra P, Wurm R, Wohlleben W, Wagner R, Reuther J (2008) The Streptomyces coeli-color GlnR regulon: Identification of new GlnR targets and evidence for a central role of GlnR in nitrogen metabolism in actinomycetes. Mol Biol 67:861-880
    • (2008) Mol Biol , vol.67 , pp. 861-880
    • Tiffert, Y.1    Supra, P.2    Wurm, R.3    Wohlleben, W.4    Wagner, R.5    Reuther, J.6
  • 140
    • 0028000790 scopus 로고
    • Evolutionary relationships between sugar kinases and transcriptional repressors in bacteria
    • Titgemeyer F, Reizer J, Reizer A, Saier MH Jr (1994) Evolutionary relationships between sugar kinases and transcriptional repressors in bacteria. Microbiology 140:2349-2354
    • (1994) Microbiology , vol.140 , pp. 2349-2354
    • Titgemeyer, F.1    Reizer, J.2    Reizer, A.3    Saier, M.H.4
  • 141
    • 0025822796 scopus 로고
    • Purification and characterization of Streptomyces griseus metalloendopeptidases I and II
    • Tsuyuki H, Kajiwara K, Fujita A et al (1991) Purification and characterization of Streptomyces griseus metalloendopeptidases I and II. J Biochem 110:339-344
    • (1991) J Biochem , vol.110 , pp. 339-344
    • Tsuyuki, H.1    Kajiwara, K.2    Fujita, A.3
  • 142
    • 0017831978 scopus 로고
    • Regulation of the assimilation of nitrogen compounds
    • Tyler B (1978) Regulation of the assimilation of nitrogen compounds. Annu Rev Biochem 47:1127-1162
    • (1978) Annu Rev Biochem , vol.47 , pp. 1127-1162
    • Tyler, B.1
  • 143
    • 0013824537 scopus 로고
    • Pathway specific patter of control of arginine biosynthesis in bacteria
    • Udaka S (1966) Pathway specific patter of control of arginine biosynthesis in bacteria. J Bacteriol 91:617-621
    • (1966) J Bacteriol , vol.91 , pp. 617-621
    • Udaka, S.1
  • 144
    • 0015904927 scopus 로고
    • Production of aminopeptidase and carboxypeptidase by Streptomycespeptidofaciens
    • Uwajima T, Yoshikawa N, Terada O (1973) Production of aminopeptidase and carboxypeptidase by Streptomycespeptidofaciens. Agric Biol Chem 37:1517-1523
    • (1973) Agric Biol Chem , vol.37 , pp. 1517-1523
    • Uwajima, T.1    Yoshikawa, N.2    Terada, O.3
  • 145
    • 80052077061 scopus 로고    scopus 로고
    • The regulation of the secondary metabolism of Streptomyces: New links and experimental advances
    • Van Wezel G, McDowall KJ (2011) The regulation of the secondary metabolism of Streptomyces: new links and experimental advances. Nat Prod Rep 28:1311-1333
    • (2011) Nat Prod Rep , vol.28 , pp. 1311-1333
    • Van Wezel, G.1    McDowall, K.J.2
  • 146
    • 0023571781 scopus 로고
    • Effect of ammonium on the composition of fatty acids in Streptomyces fradiae, producer of tylosin
    • Vancura A, Rezanka T, Marsalek J et al (1987) Effect of ammonium on the composition of fatty acids in Streptomyces fradiae, producer of tylosin. FEMS Microbiol Lett 48:357-260
    • (1987) FEMS Microbiol Lett , vol.48 , pp. 260-357
    • Vancura, A.1    Rezanka, T.2    Marsalek, J.3
  • 147
    • 0023870430 scopus 로고
    • Metabolism of threonine and fatty acids and tylosin biosynthesis in Streptomyces fradiae
    • Vancura A, Rezanka T, Marsalek J et al (1988) Metabolism of threonine and fatty acids and tylosin biosynthesis in Streptomyces fradiae. FEMS Microbiol Lett 49:411-415
    • (1988) FEMS Microbiol Lett , vol.49 , pp. 411-415
    • Vancura, A.1    Rezanka, T.2    Marsalek, J.3
  • 148
    • 0024270115 scopus 로고
    • Cloning, characterization and regulation of an a-amylase gene from Streptomyces venezuelae
    • Virolle MJ, Long CM, Chang S, Bibb MJ (1988) Cloning, characterization and regulation of an a-amylase gene from Streptomyces venezuelae. Gene 74:321-334
    • (1988) Gene , vol.74 , pp. 321-334
    • Virolle, M.J.1    Long, C.M.2    Chang, S.3    Bibb, M.J.4
  • 149
    • 0014457657 scopus 로고
    • Regulation of biosynthesis of secondary metabolites. IV: Purification and properties of phosphoenolpyruvate carboxylase in Streptomyces aureofaciens
    • Vorisek J, Powell AJ, Vanek Z (1969) regulation of biosynthesis of secondary metabolites. IV: Purification and properties of phosphoenolpyruvate carboxylase in Streptomyces aureofaciens. Folia Microbiol 14:398-405
    • (1969) Folia Microbiol , vol.14 , pp. 398-405
    • Vorisek, J.1    Powell, A.J.2    Vanek, Z.3
  • 150
    • 0018264520 scopus 로고
    • Proteolytic enzymes of the K-1 strain of Streptomyces griseus obtained from a commercial preparation (Pronase)
    • Vosbeck KD, Greenberg BD, Ochoa MS et al (1978) Proteolytic enzymes of the K-1 strain of Streptomyces griseus obtained from a commercial preparation (pronase). J Biol Chem 253:257-260
    • (1978) J Biol Chem , vol.253 , pp. 257-260
    • Vosbeck, K.D.1    Greenberg, B.D.2    Ochoa, M.S.3
  • 151
    • 0016658549 scopus 로고
    • S-adenosylhomocysteine metabolism in various species
    • Walker RD, Duerre JA (1975) S-adenosylhomocysteine metabolism in various species. Can J Biochem 53:312-319
    • (1975) Can J Biochem , vol.53 , pp. 312-319
    • Walker, R.D.1    Duerre, J.A.2
  • 152
    • 78651155487 scopus 로고
    • Developmental changes in arginine: X amiotransferase activity in streptomycin-producing strains of Streptomyces
    • Walker JD, Hnilica VS (1964) Developmental changes in arginine: X amiotransferase activity in streptomycin-producing strains of Streptomyces. Biochim Biophys Acta 89:473-482
    • (1964) Biochim Biophys Acta , vol.89 , pp. 473-482
    • Walker, J.D.1    Hnilica, V.S.2
  • 153
    • 33845751000 scopus 로고    scopus 로고
    • A new piece of an old jigsaw: Glucose kinase is activated posttranslationally in a glucose transport-dependent manner in Streptomyces coelicolor A3(2)
    • van Wezel G, Konig M, Mahr K, Nothaft H, Thomae AW, Bibb M, Titgemeyer F (2007) A new piece of an old jigsaw: glucose kinase is activated posttranslationally in a glucose transport-dependent manner in Streptomyces coelicolor A3(2). J Mol Microbiol Biotechnol 12:67-74
    • (2007) J Mol Microbiol Biotechnol , vol.12 , pp. 67-74
    • Van Wezel, G.1    Konig, M.2    Mahr, K.3    Nothaft, H.4    Thomae, A.W.5    Bibb, M.6    Titgemeyer, F.7
  • 155
    • 0031018158 scopus 로고    scopus 로고
    • Substrate induction and glucose repression of maltose utilization by Streptomyces coelicolor A3(2) is controlled by malR, a member of the lacl-galR family of regulatory genes
    • van Wezel GP, White J, Young P, Postma PW, Bibb MJ (1997) Substrate induction and glucose repression of maltose utilization by Streptomyces coelicolor A3(2) is controlled by malR, a member of the lacl-galR family of regulatory genes. Mol Microbiol 23:537-549
    • (1997) Mol Microbiol , vol.23 , pp. 537-549
    • Van Wezel, G.P.1    White, J.2    Young, P.3    Postma, P.W.4    Bibb, M.J.5
  • 156
    • 0025176821 scopus 로고
    • The purification and characterization of 3-dehydroquinase from Streptomyces coelicolor
    • White PJ, Young J, Hunter IS, Nimmo HG, Coggins JR (1990) The purification and characterization of 3-dehydroquinase from Streptomyces coelicolor. Biochemical Journal 265:735-738
    • (1990) Biochemical Journal , vol.265 , pp. 735-738
    • White, P.J.1    Young, J.2    Hunter, I.S.3    Nimmo, H.G.4    Coggins, J.R.5
  • 157
    • 0001906438 scopus 로고
    • Oligotrophy in soil: Fact or fiction
    • Fletcher M, Floodgate GD, Academic Press, London
    • Williams ST (1985) Oligotrophy in soil: fact or fiction. In: Fletcher M, Floodgate GD (eds) Bacteria in their natural environments. Academic Press, London, pp 81-110
    • (1985) Bacteria in Their Natural Environments , pp. 81-110
    • Williams, S.T.1
  • 158
    • 0035031304 scopus 로고    scopus 로고
    • Characterization and analysis of the PikD regulatory factor in the pikromycin biosynthetic pathway of Streptomyces venezuelae
    • Wilson DJ, Xue YQ, Reynolds KA, Sherman DH (2001) Characterization and analysis of the PikD regulatory factor in the pikromycin biosynthetic pathway of Streptomyces venezuelae. J Bacteriol 183:3468-3475
    • (2001) J Bacteriol , vol.183 , pp. 3468-3475
    • Wilson, D.J.1    Xue, Y.Q.2    Reynolds, K.A.3    Sherman, D.H.4
  • 159
    • 84863029633 scopus 로고    scopus 로고
    • Regulation of nitrogen assimilation in streptomycetes and other actinobacteria
    • Dyson P, Caister Academic Press, Norfolk, UK
    • Wohlleben W, Mast Y, Reuthler J (2011) Regulation of nitrogen assimilation in streptomycetes and other actinobacteria. In: Dyson P (ed) Streptomyces: molecular biology and biotechnology. Caister Academic Press, Norfolk, UK, pp 125-136
    • (2011) Streptomyces: Molecular Biology and Biotechnology , pp. 125-136
    • Wohlleben, W.1    Mast, Y.2    Reuthler, J.3
  • 160
    • 0025720228 scopus 로고
    • Genetic organization and regulation of the xylose degradation genes in Streptomyces rubiginosus
    • Wong HC, Ting Y, Lin HC et al (1991) Genetic organization and regulation of the xylose degradation genes in Streptomyces rubiginosus. J Bacteriol 173:6849-6858
    • (1991) J Bacteriol , vol.173 , pp. 6849-6858
    • Wong, H.C.1    Ting, Y.2    Lin, H.C.3
  • 161
    • 0024269834 scopus 로고    scopus 로고
    • Cloning and nucleotide sequence of the Streptomyces coelicolor gene encoding glutamine synthetase
    • Wray LV Jr, Fisher SH (1998) Cloning and nucleotide sequence of the Streptomyces coelicolor gene encoding glutamine synthetase. Gene 71:247-256
    • (1998) Gene , vol.71 , pp. 247-256
    • Wray, L.V.1    Fisher, S.H.2


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