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Volumn 178, Issue 23, 1996, Pages 6873-6881

Cloning and characterization of the gene encoding 1- cyclohexenylcarbonyl coenzyme A reductase from Streptomyces collinus

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL ENZYME; BACTERIAL PROTEIN; OXIDOREDUCTASE; SHIKIMIC ACID;

EID: 10544222832     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/jb.178.23.6873-6881.1996     Document Type: Article
Times cited : (25)

References (68)
  • 3
    • 0024789309 scopus 로고
    • Isopentenyl diphosphatc: Dimethyl allyl diphosphate isomcrase. An improved purification of the enzyme and isolation of the gene from Saccha- Romyces cerevisiae
    • Anderson, M. S., M. Muehlbacher, I. P. Street, J. Proffitt, and C. D. Poulter. 1989. Isopentenyl diphosphatc: dimethyl allyl diphosphate isomcrase. An improved purification of the enzyme and isolation of the gene from Saccha- romyces cerevisiae. J. Biol. Chem. 264:19169-19175.
    • (1989) J. Biol. Chem. , vol.264 , pp. 19169-19175
    • Anderson, M.S.1    Muehlbacher, M.2    Street, I.P.3    Proffitt, J.4    Poulter, C.D.5
  • 4
    • 0025159314 scopus 로고
    • A common ancestor for human placental 1α-hydroxysteroid dehydrogenase, Streptomyces coelicolor actIII protein, and Drosophila melanogusler alcohol dehydrogenase
    • Baker, M. E. 1990. A common ancestor for human placental 1α-hydroxysteroid dehydrogenase, Streptomyces coelicolor actIII protein, and Drosophila melanogusler alcohol dehydrogenase. FASEB J. 4:222-226.
    • (1990) FASEB J. , vol.4 , pp. 222-226
    • Baker, M.E.1
  • 5
    • 0025308563 scopus 로고
    • Sequence similarity between Pseudomimas dihydrodiol dehydrogenase, part of the gene cluster that metabolizes polychlorinated biphenyls, and dehydrogenases involved in the metabolism of ribitol and glucitol and synthesis of antibiotics and 17α-oestradiol, testosterone, and corticocosterone
    • Baker, M. E. 1990. Sequence similarity between Pseudomimas dihydrodiol dehydrogenase, part of the gene cluster that metabolizes polychlorinated biphenyls, and dehydrogenases involved in the metabolism of ribitol and glucitol and synthesis of antibiotics and 17α-oestradiol, testosterone, and corticocosterone. Biochem. J. 267:839-841.
    • (1990) Biochem. J. , vol.267 , pp. 839-841
    • Baker, M.E.1
  • 6
    • 0025581736 scopus 로고
    • The shikimic pathway-a metabolic tree with many branches
    • Bentley, R. 1990. The shikimic pathway-a metabolic tree with many branches. Crit. Rev. Biochem. Mol. Biol. 25:307-383.
    • (1990) Crit. Rev. Biochem. Mol. Biol. , vol.25 , pp. 307-383
    • Bentley, R.1
  • 7
    • 0020448903 scopus 로고
    • Gene expression in Streptomyces: Construction and amplification of promoter-probe plasmid vectors in Streptomyces lividans
    • Bibb, M. J., and S. N. Cohen. 1982. Gene expression in Streptomyces: construction and amplification of promoter-probe plasmid vectors in Streptomyces lividans. Mol. Gen. Genet. 187:265-277.
    • (1982) Mol. Gen. Genet. , vol.187 , pp. 265-277
    • Bibb, M.J.1    Cohen, S.N.2
  • 8
    • 0021710537 scopus 로고
    • The relationship between base composition and codon usage in bacterial genes and its use for the simple and reliable identification of protein coding sequences
    • Bibb, M. J., P. R. Findlay, and M. J. Johnson. 1984. The relationship between base composition and codon usage in bacterial genes and its use for the simple and reliable identification of protein coding sequences. Gene 30:157-166.
    • (1984) Gene , vol.30 , pp. 157-166
    • Bibb, M.J.1    Findlay, P.R.2    Johnson, M.J.3
  • 9
    • 0021827086 scopus 로고
    • Temperature-sensitive mutants of the Streptomyces plasmid pIJ702
    • Birch, A. W., and J. Cullum. 1985. Temperature-sensitive mutants of the Streptomyces plasmid pIJ702. J. Gen. Microbiol. 131:1299-1303.
    • (1985) J. Gen. Microbiol. , vol.131 , pp. 1299-1303
    • Birch, A.W.1    Cullum, J.2
  • 10
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantification of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. 1976. A rapid and sensitive method for the quantification of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72:248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 11
    • 0019406433 scopus 로고
    • The nucleolide sequence of the cloned rpvD gene for the RNA polymerase sigma subunit from E. coli K12
    • Burton, Z., R. R. Burgess, J. Lin, D. Moore, S. Holder, and C. A. Gross. 1981. The nucleolide sequence of the cloned rpvD gene for the RNA polymerase sigma subunit from E. coli K12. Nucleic Acids Res. 9:2889-2903.
    • (1981) Nucleic Acids Res. , vol.9 , pp. 2889-2903
    • Burton, Z.1    Burgess, R.R.2    Lin, J.3    Moore, D.4    Holder, S.5    Gross, C.A.6
  • 12
    • 0028240983 scopus 로고
    • Pentalene synthase. Purification, molecular cloning, sequencing, and high-level expression in Escherichia coli of a terpenoid cyclase from Streptomyces UC5319
    • Cane, D. E., J.-K. Sonhng, C. R. Lamberson, S. M. Rudnicki, Z. Wu, M. D. Lloyd, J. S. Oliver, and B. R. Hubbard. 1994. Pentalene synthase. Purification, molecular cloning, sequencing, and high-level expression in Escherichia coli of a terpenoid cyclase from Streptomyces UC5319. Biochemistry 33:5846-5857.
    • (1994) Biochemistry , vol.33 , pp. 5846-5857
    • Cane, D.E.1    Sonhng, J.-K.2    Lamberson, C.R.3    Rudnicki, S.M.4    Wu, Z.5    Lloyd, M.D.6    Oliver, J.S.7    Hubbard, B.R.8
  • 13
    • 0004706456 scopus 로고
    • 7N unit and stereochemistry of its conversion to shikimic acid
    • 7N unit and stereochemistry of its conversion to shikimic acid. J. Am. Chem. Soc. 109:8102-8104.
    • (1987) J. Am. Chem. Soc. , vol.109 , pp. 8102-8104
    • Casati, R.1    Beale, J.M.2    Floss, H.G.3
  • 14
    • 0024853921 scopus 로고
    • Homology analysis of the protein sequences of fatty acid synthases from chicken liver, rat mammary gland, and yeast
    • Chang, S.-I., and G. G. Hammes. 1989. Homology analysis of the protein sequences of fatty acid synthases from chicken liver, rat mammary gland, and yeast. Proc. Natl Acad. Sci. USA 86:8373-8376.
    • (1989) Proc. Natl Acad. Sci. USA , vol.86 , pp. 8373-8376
    • Chang, S.-I.1    Hammes, G.G.2
  • 15
    • 0025166586 scopus 로고
    • Site directed mutagenesis of glycine-14 and two critical cysteinyl residues in Drosophila alcohol dehydrogenase
    • then, Z., L. Lu, M. Shirley, W. R. Lee, and S. H. Chang. 1990. Site directed mutagenesis of glycine-14 and two critical cysteinyl residues in Drosophila alcohol dehydrogenase. Biochemistry 29:1112-1118.
    • (1990) Biochemistry , vol.29 , pp. 1112-1118
    • Then, Z.1    Lu, L.2    Shirley, M.3    Lee, W.R.4    Chang, S.H.5
  • 16
    • 0028989612 scopus 로고
    • A second branched-chain a-keto acid dehydrogenase gene cluster (bkdFGH) from Streptomyces avermitilis: Its relationship to avermectin biosynthesis and the construction of a bkdF mutant suitable for the production of novel antiparasitic avermectins
    • Denoya, C. D., R. W. Fedechko, E. W. Hafner, H. A. I. McArthur, M. R. Morgenstern, D. D. Skinner, K. Stutzman-Engwall, R. G. Wax, and W. C. Wernau. 1995. A second branched-chain a-keto acid dehydrogenase gene cluster (bkdFGH) from Streptomyces avermitilis: its relationship to avermectin biosynthesis and the construction of a bkdF mutant suitable for the production of novel antiparasitic avermectins. J. Bacteriol. 177:3504-3511.
    • (1995) J. Bacteriol. , vol.177 , pp. 3504-3511
    • Denoya, C.D.1    Fedechko, R.W.2    Hafner, E.W.3    McArthur, H.A.I.4    Morgenstern, M.R.5    Skinner, D.D.6    Stutzman-Engwall, K.7    Wax, R.G.8    Wernau, W.C.9
  • 17
    • 0027965019 scopus 로고
    • A Streptomyces avermitilis gene encoding a 4-hydroxyphenylpyruvic acid dioxygenase-like protein that directs the production of homogentisic acid and an ochronotic pigment in Escherichia coli
    • Denoya, C. D., D. D. Skinner, and M. R. Morgernstern. 1994. A Streptomyces avermitilis gene encoding a 4-hydroxyphenylpyruvic acid dioxygenase-like protein that directs the production of homogentisic acid and an ochronotic pigment in Escherichia coli. J. Bacteriol. 176:5312-5319.
    • (1994) J. Bacteriol. , vol.176 , pp. 5312-5319
    • Denoya, C.D.1    Skinner, D.D.2    Morgernstern, M.R.3
  • 18
    • 0021760092 scopus 로고
    • A comprehensive set of sequence analysis programs for the VAX
    • Devereux, J., P. Haeberli, and O. Smithies. 1984. A comprehensive set of sequence analysis programs for the VAX. Nucleic Acids Res. 12:387-395.
    • (1984) Nucleic Acids Res. , vol.12 , pp. 387-395
    • Devereux, J.1    Haeberli, P.2    Smithies, O.3
  • 20
    • 0027971383 scopus 로고
    • DNA sequence and functions of the actVI region of the actinorhodin biosynthetic gene cluster of Streptomyces coelicohr A3(2)
    • Fernandez-Moreno, M. A., E. Martinéz, J. Caballero, K. Ichinose, D. A. Hopwood, and F. Malpartida. 1994. DNA sequence and functions of the actVI region of the actinorhodin biosynthetic gene cluster of Streptomyces coelicohr A3(2). J. Biol. Chem. 269:24854-24863.
    • (1994) J. Biol. Chem. , vol.269 , pp. 24854-24863
    • Fernandez-Moreno, M.A.1    Martinéz, E.2    Caballero, J.3    Ichinose, K.4    Hopwood, D.A.5    Malpartida, F.6
  • 21
    • 85035184177 scopus 로고    scopus 로고
    • Personal communication
    • Floss, H. G. Personal communication.
    • Floss, H.G.1
  • 22
    • 0027769777 scopus 로고
    • A novel ancestral protein of Drosophila alcohol dehydrogenase in Streptomyces?
    • Freriksen, A., and P. W. H. Heinstra. 1993. A novel ancestral protein of Drosophila alcohol dehydrogenase in Streptomyces? Biochem. Genet. 31:393-407.
    • (1993) Biochem. Genet. , vol.31 , pp. 393-407
    • Freriksen, A.1    Heinstra, P.W.H.2
  • 23
    • 0022004954 scopus 로고
    • Structure of trienomycin A, a novel cytocidal ansamycin antibiotic
    • Funayama, S., K. Okada, K. Komiyama, and I. Umezawa. 1985. Structure of trienomycin A, a novel cytocidal ansamycin antibiotic. J. Antibiot. 38:1107-1109.
    • (1985) J. Antibiot. , vol.38 , pp. 1107-1109
    • Funayama, S.1    Okada, K.2    Komiyama, K.3    Umezawa, I.4
  • 24
    • 0024393917 scopus 로고
    • Studies on new phosphate ester antibiotics phoslactomycins. II. Structure elucidation of phoslactomycins A to F
    • Fushimi, S., K. Furihala. and H. Seto. 1989. Studies on new phosphate ester antibiotics phoslactomycins. II. Structure elucidation of phoslactomycins A to F. J. Antibiol. 42:1026-1036.
    • (1989) J. Antibiol. , vol.42 , pp. 1026-1036
    • Fushimi, S.1    Furihala, K.2    Seto, H.3
  • 25
    • 0024378164 scopus 로고
    • Studies on new phosphate ester antifungal antibiotics phoslactomycins. I. Taxonomy, fermentation, purification and biological properties
    • Fushimi, S., S. Nishikawa, A. Shimazu, and H. Seto. 1989. Studies on new phosphate ester antifungal antibiotics phoslactomycins. I. Taxonomy, fermentation, purification and biological properties. J. Antibiot. 42:1019-1025.
    • (1989) J. Antibiot. , vol.42 , pp. 1019-1025
    • Fushimi, S.1    Nishikawa, S.2    Shimazu, A.3    Seto, H.4
  • 26
    • 0027399530 scopus 로고
    • Identification of protein coding regions by database similarity searching
    • Gish, W., and D. J. States. 1993. Identification of protein coding regions by database similarity searching. Nat. Genet. 3:266-272.
    • (1993) Nat. Genet. , vol.3 , pp. 266-272
    • Gish, W.1    States, D.J.2
  • 27
    • 0024274121 scopus 로고
    • Nucleotide sequence, transcription and deduced function of a gene involved in polyketide antibiotic biosynthesis in Streptomyces coelicolor
    • Hallam, S. E., F. Malpartida, and D. A. Hopwood. 1988. Nucleotide sequence, transcription and deduced function of a gene involved in polyketide antibiotic biosynthesis in Streptomyces coelicolor. Gene 74:305-320.
    • (1988) Gene , vol.74 , pp. 305-320
    • Hallam, S.E.1    Malpartida, F.2    Hopwood, D.A.3
  • 28
    • 0024287984 scopus 로고
    • Identification and isolation of glucose dehydrogenase genes of Bacillus megaterium M1286 and their expression in Escherichia coli
    • Heilmann, H. J., H. J. Maegert, and H. G. Gassen. 1988. Identification and isolation of glucose dehydrogenase genes of Bacillus megaterium M1286 and their expression in Escherichia coli. Eur. J. Biochem. 174:485-490.
    • (1988) Eur. J. Biochem. , vol.174 , pp. 485-490
    • Heilmann, H.J.1    Maegert, H.J.2    Gassen, H.G.3
  • 29
    • 0026458378 scopus 로고
    • Amino acid substitution matrices from protein blocks
    • Heinkoff, S., and J. G. Heinkoff. 1992. Amino acid substitution matrices from protein blocks. Proc. Natl. Acad. Sci. USA 89:10915-10919.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 10915-10919
    • Heinkoff, S.1    Heinkoff, J.G.2
  • 30
    • 0024391168 scopus 로고
    • Molecular cloning and sequencing of chicken liver fatty acid synthase cDNA
    • Holzer, K. P., W. Lui, and G. G. Hammes, 1989. Molecular cloning and sequencing of chicken liver fatty acid synthase cDNA. Proc. Natl. Acad. Sci. USA 86:4387-4391.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 4387-4391
    • Holzer, K.P.1    Lui, W.2    Hammes, G.G.3
  • 31
    • 0001426181 scopus 로고
    • Regulation of gene expression in antibiotic-producing Streptomyces
    • I. R. Booth and C. F. Higgins (ed.), University of Cambridge Press, Cambridge
    • Hopwood, D. A., M. J. Bibb, K. F. Chater, G. R. Janssen. F. Malpartida, and C. P. Smith. 1986. Regulation of gene expression in antibiotic-producing Streptomyces, p. 251-276. In I. R. Booth and C. F. Higgins (ed.), Regulation of gene expression-25 years on. University of Cambridge Press, Cambridge.
    • (1986) Regulation of Gene Expression-25 Years on , pp. 251-276
    • Hopwood, D.A.1    Bibb, M.J.2    Chater, K.F.3    Janssen, G.R.4    Malpartida, F.5    Smith, C.P.6
  • 33
    • 0000681179 scopus 로고
    • The structure of asukamycin, a possible shunt metabolite from 3-dehydroquininic acid in the shikimate pathway
    • Kakunima, K., N. Ikekama, A. Nakagawa, and S. Omura. 1979. The structure of asukamycin, a possible shunt metabolite from 3-dehydroquininic acid in the shikimate pathway. J. Am. Chem. Soc. 101:3402-3403.
    • (1979) J. Am. Chem. Soc. , vol.101 , pp. 3402-3403
    • Kakunima, K.1    Ikekama, N.2    Nakagawa, A.3    Omura, S.4
  • 34
    • 0025259313 scopus 로고
    • Methods for assessing the statistical significance of molecular sequence features by using general scoring schemes
    • Karlin, S., and S. F. Altschul. 1990. Methods for assessing the statistical significance of molecular sequence features by using general scoring schemes. Proc. Natl. Acad. Sci. USA 87:2264-2268.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 2264-2268
    • Karlin, S.1    Altschul, S.F.2
  • 35
    • 0027175241 scopus 로고
    • Applications and statistics for multiple high-scoring segments in molecular sequences
    • Karlin, S., and S. F. Altschul. 1993. Applications and statistics for multiple high-scoring segments in molecular sequences. Proc. Natl. Acad. Sci. USA 90:5873-5877.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 5873-5877
    • Karlin, S.1    Altschul, S.F.2
  • 36
    • 0028354351 scopus 로고
    • Aspergillus nidulans vesA is required for production of the mycotoxin sterigmatocystin
    • Keller, N. P., N. J. Kantz, and T. H. Adams. 1994. Aspergillus nidulans vesA is required for production of the mycotoxin sterigmatocystin. Appl. Environ. Microbiol. 60:1444-1450.
    • (1994) Appl. Environ. Microbiol. , vol.60 , pp. 1444-1450
    • Keller, N.P.1    Kantz, N.J.2    Adams, T.H.3
  • 37
    • 0025889035 scopus 로고
    • Genetic manipulation of Streptomyces: Integrating vectors and gene replacement
    • Kieser, T., and D. A. Hopwood. 1991. Genetic manipulation of Streptomyces: integrating vectors and gene replacement. Methods Enzymol. 204:430-458.
    • (1991) Methods Enzymol. , vol.204 , pp. 430-458
    • Kieser, T.1    Hopwood, D.A.2
  • 38
    • 0026828603 scopus 로고
    • 11β-hydroxysteroid dehydrogenase and the short chain alcohol dehydrogenase family
    • Krozowski, Z. 1992. 11β-hydroxysteroid dehydrogenase and the short chain alcohol dehydrogenase family. Mol. Cell Endocrinol. 84:25-31.
    • (1992) Mol. Cell Endocrinol. , vol.84 , pp. 25-31
    • Krozowski, Z.1
  • 39
    • 0020691918 scopus 로고
    • Ansatrienin A2 and A3: Minor componenets of the ansamycin complex produced by Streplomyces collinus
    • Lazar, G., H. Zäzhner, M. Damberg, and A. Zeeck. 1982. Ansatrienin A2 and A3: minor componenets of the ansamycin complex produced by Streplomyces collinus. J. Antibiot. 36:187-189.
    • (1982) J. Antibiot. , vol.36 , pp. 187-189
    • Lazar, G.1    Zäzhner, H.2    Damberg, M.3    Zeeck, A.4
  • 43
    • 0001024921 scopus 로고
    • Biosynthesis of the cyclohexanecarhoxylic acid starter unit of ω-cyclohexylfatty acids in Alicyclobacillus acidocaldarius
    • Moore, B. S., K. Poralla, and H. G. Floss. 1993. Biosynthesis of the cyclohexanecarhoxylic acid starter unit of ω-cyclohexylfatty acids in Alicyclobacillus acidocaldarius. J Amer. Chem. Soc. 115:5267-5274.
    • (1993) J Amer. Chem. Soc. , vol.115 , pp. 5267-5274
    • Moore, B.S.1    Poralla, K.2    Floss, H.G.3
  • 44
    • 0026508867 scopus 로고
    • Cis-diol dehydrogenases encoded by the TOL pWWC plasmid xylL gene and the Adnelubacter calcoaceticus chromosomal benD gene are members of the short-chain alcohol dehydrogenasc family
    • Neidle, E. L., C. Hartnett, N. L. Ornston, A. Bairoch, M. Rekik, and S. Harayama. 1992. Cis-diol dehydrogenases encoded by the TOL pWWC) plasmid xylL gene and the Adnelubacter calcoaceticus chromosomal benD gene are members of the short-chain alcohol dehydrogenasc family. Eur. J. Biochem. 204:113-120.
    • (1992) Eur. J. Biochem. , vol.204 , pp. 113-120
    • Neidle, E.L.1    Hartnett, C.2    Ornston, N.L.3    Bairoch, A.4    Rekik, M.5    Harayama, S.6
  • 46
    • 0026703235 scopus 로고
    • The gene encoding Escherichia coli acyl carrier protein lies within a cluster of fatty acid biosynthetic genes
    • Rawlings, M., and J. E. Cronan. 1992. The gene encoding Escherichia coli acyl carrier protein lies within a cluster of fatty acid biosynthetic genes. J.Biol. Chem. 267:5751-5754.
    • (1992) J.Biol. Chem. , vol.267 , pp. 5751-5754
    • Rawlings, M.1    Cronan, J.E.2
  • 47
    • 0027409177 scopus 로고
    • Comparison of two unusual enoyl CoA reductases in Streptomtces collinus
    • Reynolds, K. A. 1993. Comparison of two unusual enoyl CoA reductases in Streptomtces collinus. J. Nat. Prod. 56:175-185.
    • (1993) J. Nat. Prod. , vol.56 , pp. 175-185
    • Reynolds, K.A.1
  • 48
    • 0025821260 scopus 로고
    • Biosynthesis of ansatrienin: Stereochemical course of the final reduction step leading to the cyclohexanecarboxylic acid moiety
    • Reynolds, K. A., K. M. Fox, Z.-M. Yuan, and Y. Lam. 1991. Biosynthesis of ansatrienin: stereochemical course of the final reduction step leading to the cyclohexanecarboxylic acid moiety. J. Am. Chem. Soc. 113:4339-4340.
    • (1991) J. Am. Chem. Soc. , vol.113 , pp. 4339-4340
    • Reynolds, K.A.1    Fox, K.M.2    Yuan, Z.-M.3    Lam, Y.4
  • 49
    • 0027212203 scopus 로고
    • 4-cyclohexenylcarbonyl CoA isomerase catalyzing the penultimate step in the biosynthesis of the cyclohexanecarhoxylic acid moiety of ansatrienin A
    • 4-cyclohexenylcarbonyl CoA isomerase catalyzing the penultimate step in the biosynthesis of the cyclohexanecarhoxylic acid moiety of ansatrienin A. J. Nat. Prod. 56:825-829,
    • (1993) J. Nat. Prod. , vol.56 , pp. 825-829
    • Reynolds, K.A.1    Seaton, N.2    Fox, K.M.3    Warner, K.4    Wang, P.5
  • 50
    • 0026578929 scopus 로고
    • Biosynthesis of ansatrienin by Streptomyces collinus: Cell-free transformations of cyclohexene- And cyclohexadicnecarboxylic acids
    • Reynolds, K. A., P. Wang, K. M. Fox, and H. G. Floss. 1992. Biosynthesis of ansatrienin by Streptomyces collinus: cell-free transformations of cyclohexene- and cyclohexadicnecarboxylic acids. J. Antibiol. 45:645-653.
    • (1992) J. Antibiol. , vol.45 , pp. 645-653
    • Reynolds, K.A.1    Wang, P.2    Fox, K.M.3    Floss, H.G.4
  • 51
    • 0026716021 scopus 로고
    • Purification and characterization of a novel enovl CoA reduclase from Streptomyces collinus
    • Reynolds, K. A., P. Wang, K. M. Fox, M. K. Speedie, Y. Lam, and H. G. Floss. 1992. Purification and characterization of a novel enovl CoA reduclase from Streptomyces collinus. J. Bacteriol. 174:3850-3854.
    • (1992) J. Bacteriol. , vol.174 , pp. 3850-3854
    • Reynolds, K.A.1    Wang, P.2    Fox, K.M.3    Speedie, M.K.4    Lam, Y.5    Floss, H.G.6
  • 55
    • 0027487415 scopus 로고
    • A simple DNA polymerase chain reaction method to locate and define orientation of specific sequences in cloned bacterial genomic fragments
    • Skinner, D. D., and C. D. Denoya. 1993. A simple DNA polymerase chain reaction method to locate and define orientation of specific sequences in cloned bacterial genomic fragments. Microbios 75:125-129.
    • (1993) Microbios , vol.75 , pp. 125-129
    • Skinner, D.D.1    Denoya, C.D.2
  • 56
    • 0026476049 scopus 로고
    • Isolation and characterization of a gene from Aspergillus purasiticus associated with the conversion of versicolorin A to sterigmatocyslin in aflatoxin biosynthesis
    • Skory, C. D., P. K. Chang, J. Cary, and J. E. Linz, 1992. Isolation and characterization of a gene from Aspergillus purasiticus associated with the conversion of versicolorin A to sterigmatocyslin in aflatoxin biosynthesis. Appl. Environ. Microbiol. 58:3527-3537.
    • (1992) Appl. Environ. Microbiol. , vol.58 , pp. 3527-3537
    • Skory, C.D.1    Chang, P.K.2    Cary, J.3    Linz, J.E.4
  • 57
    • 0016700864 scopus 로고
    • Detection of specific sequences among DNA fragments by gel electrophoresis
    • Southern, E. M. 1975. Detection of specific sequences among DNA fragments by gel electrophoresis. J. Mol. Biol. 98:503-517.
    • (1975) J. Mol. Biol. , vol.98 , pp. 503-517
    • Southern, E.M.1
  • 58
    • 0025283867 scopus 로고
    • Use of T7 RNA polymerase to direct expression of cloned genes
    • Studier, F. W., A. H. Rosenberg, and J. J. Dunn. 1990. Use of T7 RNA polymerase to direct expression of cloned genes. Methods Enzymol. 185:60-89.
    • (1990) Methods Enzymol. , vol.185 , pp. 60-89
    • Studier, F.W.1    Rosenberg, A.H.2    Dunn, J.J.3
  • 59
    • 0020376885 scopus 로고
    • Studies on mycotricnin antibiotics, a novel class of ansamycins. I. Taxonomy, fermentation, isolation, and properties of mycotricnins I and II
    • Sugita, M., V. Natori, T. Sasaki, K. Furihata, A. Shimadzu, H. Seto, and N. Otake. 1982. Studies on mycotricnin antibiotics, a novel class of ansamycins. I. Taxonomy, fermentation, isolation, and properties of mycotricnins I and II. J. Antibiot. 35:1460-1466.
    • (1982) J. Antibiot. , vol.35 , pp. 1460-1466
    • Sugita, M.1    Natori, V.2    Sasaki, T.3    Furihata, K.4    Shimadzu, A.5    Seto, H.6    Otake, N.7
  • 60
    • 0021888096 scopus 로고
    • Studies or a novel cytocidal antibiotic, trienomycin: Taxonomy, fermentation, isolation, and physico-chemical and biological characteristics
    • Umezawa, I., S. Funayama, K. Okada, K. Iwasaki, J. Satoh, K. Masuda, and K. Komiyama. 1985. Studies or a novel cytocidal antibiotic, trienomycin: taxonomy, fermentation, isolation, and physico-chemical and biological characteristics. J. Antibiot. 38:699-705.
    • (1985) J. Antibiot. , vol.38 , pp. 699-705
    • Umezawa, I.1    Funayama, S.2    Okada, K.3    Iwasaki, K.4    Satoh, J.5    Masuda, K.6    Komiyama, K.7
  • 61
    • 0028044575 scopus 로고
    • Polyhydroxynapthalene reductase involved in melanin biosynthesis in Magnaporthe grisea. Purification, cDNA cloning and sequencing
    • Vidal-Crox, A., F. Viviani, G. Labesse, M. Boccara, and M, Gaudry. 1994. Polyhydroxynapthalene reductase involved in melanin biosynthesis in Magnaporthe grisea. Purification, cDNA cloning and sequencing. Eur. J. Biochem. 219:985-992.
    • (1994) Eur. J. Biochem. , vol.219 , pp. 985-992
    • Vidal-Crox, A.1    Viviani, F.2    Labesse, G.3    Boccara, M.4    Gaudry, M.5
  • 62
    • 0028808264 scopus 로고
    • Purification of crotonyl-CoA reductase from Streptomyces collinus and cloning, sequencing and expression of the corresponding gene in Escherichia coli
    • Wallace, K. K., Z.-V. Bao, B. Zhao, H. Dai, R. DiGate, G. Schuler, M. K. Speedie, and K. A. Reynolds. 1995. Purification of crotonyl-CoA reductase from Streptomyces collinus and cloning, sequencing and expression of the corresponding gene in Escherichia coli. Eur. J. Biochem. 233:954-962.
    • (1995) Eur. J. Biochem. , vol.233 , pp. 954-962
    • Wallace, K.K.1    Bao, Z.-V.2    Zhao, B.3    Dai, H.4    DiGate, R.5    Schuler, G.6    Speedie, M.K.7    Reynolds, K.A.8
  • 63
    • 0029160904 scopus 로고
    • In vivo analysis of straight-chain and branched-chain fatty acid biosynthesis in three actinomycetes
    • Wallace, K. K., B. Zhao, H. A. I. McArthur, and K. A. Reynolds. 1995. In vivo analysis of straight-chain and branched-chain fatty acid biosynthesis in three actinomycetes. FEMS Microbiol. Lett. 131:227-234.
    • (1995) FEMS Microbiol. Lett. , vol.131 , pp. 227-234
    • Wallace, K.K.1    Zhao, B.2    McArthur, H.A.I.3    Reynolds, K.A.4
  • 64
    • 0019791918 scopus 로고
    • Stofiweehselprodukte von Mikroorganismen. 201. Ansatrienin A und B, fungistatischc Antibiotica aus Streptamyces collinus
    • Weber, W, H. Zähner, M. Damberg, P. Russ, and A. Zeeck. 1981. Stofiweehselprodukte von Mikroorganismen. 201. Ansatrienin A und B, fungistatischc Antibiotica aus Streptamyces collinus. Zentralbl. Bakteriol. Hyg. I Abl. Orig. C C2:122-124.
    • (1981) Zentralbl. Bakteriol. Hyg. I Abl. Orig. C , vol.C2 , pp. 122-124
    • Weber, W.1    Zähner, H.2    Damberg, M.3    Russ, P.4    Zeeck, A.5
  • 65
    • 0026597059 scopus 로고
    • Codon usage in the G+C rich Streplomyces genome
    • Wright, F., and M. Bibb. 1992. Codon usage in the G+C rich Streplomyces genome. Gene 113:55-65.
    • (1992) Gene , vol.113 , pp. 55-65
    • Wright, F.1    Bibb, M.2
  • 66
    • 0025903406 scopus 로고
    • Cloning and sequencing of the 7α-hydroxysleroid dehydrogenase gene from Escherichia coli HB101 and characterization of the expressed protein
    • Yoshimoto, T., H. Higashi, A. Kanatani, X. S. Lin, H. Nagai, H. Oyama, K. Kurazono, and D. Tsuru. 1991. Cloning and sequencing of the 7α-hydroxysleroid dehydrogenase gene from Escherichia coli HB101 and characterization of the expressed protein. J. Bacteriol. 173:2173-2179.
    • (1991) J. Bacteriol. , vol.173 , pp. 2173-2179
    • Yoshimoto, T.1    Higashi, H.2    Kanatani, A.3    Lin, X.S.4    Nagai, H.5    Oyama, H.6    Kurazono, K.7    Tsuru, D.8
  • 67
    • 0023731139 scopus 로고
    • Molecular cloning and sequencing of DNA complementary to chicken liver fatty acid synthase m RNA
    • Yuan, Z., W. Liu, and G. G. Hammes. 1988. Molecular cloning and sequencing of DNA complementary to chicken liver fatty acid synthase m RNA. Proc. Natl. Acad. Sci. USA 85:6328-6331.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 6328-6331
    • Yuan, Z.1    Liu, W.2    Hammes, G.G.3
  • 68
    • 0024284037 scopus 로고
    • Double stranded DNA sequencing as a choice for DNA sequencing
    • Zhang, H., R. Scholl, J. Browse, and C. Somerville. 1988. Double stranded DNA sequencing as a choice for DNA sequencing. Nucleic Acids Res. 16:1220.
    • (1988) Nucleic Acids Res. , vol.16 , pp. 1220
    • Zhang, H.1    Scholl, R.2    Browse, J.3    Somerville, C.4


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