메뉴 건너뛰기




Volumn 10, Issue 10, 2003, Pages 939-952

Melithiazol biosynthesis: Further insights into myxobacterial PKS/NRPS systems and evidence for a new subclass of methyl transferases

Author keywords

[No Author keywords available]

Indexed keywords

MELITTANGIUM LICHENICOLA; MYXOCOCCALES; STIGMATELLA; STIGMATELLA AURANTIACA;

EID: 0142167587     PISSN: 10745521     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.chembiol.2003.09.012     Document Type: Article
Times cited : (73)

References (65)
  • 1
    • 0000153104 scopus 로고    scopus 로고
    • Polyketide and nonribosomal polypeptide biosynthesis
    • Cane D.E. Polyketide and nonribosomal polypeptide biosynthesis. Chem. Rev. 97:1997;2463-2464.
    • (1997) Chem. Rev. , vol.97 , pp. 2463-2464
    • Cane, D.E.1
  • 2
    • 0034887171 scopus 로고    scopus 로고
    • Polyketide biosynthesis: A millennium review
    • Staunton J., Weissman K.J. Polyketide biosynthesis. a millennium review Nat. Prod. Rep. 18:2001;380-416.
    • (2001) Nat. Prod. Rep. , vol.18 , pp. 380-416
    • Staunton, J.1    Weissman, K.J.2
  • 3
    • 0033080078 scopus 로고    scopus 로고
    • How do peptide synthetases generate structural diversity?
    • Konz D., Marahiel M.A. How do peptide synthetases generate structural diversity? Chem. Biol. 6:1999;R39-R48.
    • (1999) Chem. Biol. , vol.6
    • Konz, D.1    Marahiel, M.A.2
  • 5
    • 0029883934 scopus 로고    scopus 로고
    • Organisation of the biosynthetic gene cluster for rapamycin in Streptomyces hygroscopicus: Analysis of genes flanking the polyketide synthase
    • Molnar I., Aparicio J.F., Haydock S.F., Khaw L.E., Schwecke T., Konig A., Staunton J., Leadlay P.F. Organisation of the biosynthetic gene cluster for rapamycin in Streptomyces hygroscopicus. analysis of genes flanking the polyketide synthase Gene. 169:1996;1-7.
    • (1996) Gene , vol.169 , pp. 1-7
    • Molnar, I.1    Aparicio, J.F.2    Haydock, S.F.3    Khaw, L.E.4    Schwecke, T.5    Konig, A.6    Staunton, J.7    Leadlay, P.F.8
  • 6
    • 13144258781 scopus 로고    scopus 로고
    • Biosynthesis of the ansamycin antibiotic rifamycin: Deductions from the molecular analysis of the rif biosynthetic gene cluster of Amycolatopsis mediterranei S699
    • August P.R., Tang L., Yoon Y.J., Ning S., Müller R., Yu T.W., Taylor M., Hoffmann D., Kim C.G., Zhang X.et al. Biosynthesis of the ansamycin antibiotic rifamycin. deductions from the molecular analysis of the rif biosynthetic gene cluster of Amycolatopsis mediterranei S699 Chem. Biol. 5:1998;69-79.
    • (1998) Chem. Biol. , vol.5 , pp. 69-79
    • August, P.R.1    Tang, L.2    Yoon, Y.J.3    Ning, S.4    Müller, R.5    Yu, T.W.6    Taylor, M.7    Hoffmann, D.8    Kim, C.G.9    Zhang, X.10
  • 8
    • 0037197692 scopus 로고    scopus 로고
    • Enzymatic assembly of epothilones: The EpoC subunit and reconstitution of the EpoA-ACP/B/C polyketide and nonribosomal peptide interfaces
    • O'Connor S.E., Chen H.W., Walsh C.T. Enzymatic assembly of epothilones. The EpoC subunit and reconstitution of the EpoA-ACP/B/C polyketide and nonribosomal peptide interfaces Biochemistry. 41:2002;5685-5694.
    • (2002) Biochemistry , vol.41 , pp. 5685-5694
    • O'Connor, S.E.1    Chen, H.W.2    Walsh, C.T.3
  • 9
    • 0037161295 scopus 로고    scopus 로고
    • The loading and initial elongation modules of rifamycin synthetase collaborate to produce mixed aryl ketide products-1
    • Admiraal S.J., Khosla C., Walsh C.T. The loading and initial elongation modules of rifamycin synthetase collaborate to produce mixed aryl ketide products-1. Biochemistry. 41:2002;5313-5324.
    • (2002) Biochemistry , vol.41 , pp. 5313-5324
    • Admiraal, S.J.1    Khosla, C.2    Walsh, C.T.3
  • 10
    • 0033485280 scopus 로고    scopus 로고
    • The parallel and convergent universes of polyketide synthases and nonribosomal peptide synthetases
    • Cane D., Walsh C. The parallel and convergent universes of polyketide synthases and nonribosomal peptide synthetases. Chem. Biol. 6:1999;R319-R325.
    • (1999) Chem. Biol. , vol.6
    • Cane, D.1    Walsh, C.2
  • 11
    • 0000701347 scopus 로고    scopus 로고
    • Myxobacteria as producers of secondary metabolites
    • S. Grabley, & R. Thieriecke. Berlin: Springer Verlag. 149-179.pp
    • Reichenbach H., Höfle G. Myxobacteria as producers of secondary metabolites. Grabley S., Thieriecke R. Drug Discovery from Nature. 1999;Springer Verlag, Berlin. 149-179.pp.
    • (1999) Drug Discovery from Nature
    • Reichenbach, H.1    Höfle, G.2
  • 12
    • 0033601178 scopus 로고    scopus 로고
    • New lessons for combinatorial biosynthesis from myxobacteria: The myxothiazol biosynthetic gene cluster of Stigmatella aurantiaca DW4/3-1
    • Silakowski B., Schairer H.U., Ehret H., Kunze B., Weinig S., Nordsiek G., Brandt P., Blöcker H., Höfle G., Beyer S.et al. New lessons for combinatorial biosynthesis from myxobacteria. the myxothiazol biosynthetic gene cluster of Stigmatella aurantiaca DW4/3-1 J. Biol. Chem. 274:1999;37391-37399.
    • (1999) J. Biol. Chem. , vol.274 , pp. 37391-37399
    • Silakowski, B.1    Schairer, H.U.2    Ehret, H.3    Kunze, B.4    Weinig, S.5    Nordsiek, G.6    Brandt, P.7    Blöcker, H.8    Höfle, G.9    Beyer, S.10
  • 13
    • 0033582596 scopus 로고    scopus 로고
    • The first gene in the biosynthesis of the polyketide antibiotic TA of Myxococcus xanthus codes for a unique PKS module coupled to a peptide synthetase
    • Paitan Y., Alon G., Orr E., Ron E.Z., Rosenberg E. The first gene in the biosynthesis of the polyketide antibiotic TA of Myxococcus xanthus codes for a unique PKS module coupled to a peptide synthetase. J. Mol. Biol. 286:1999;465-474.
    • (1999) J. Mol. Biol. , vol.286 , pp. 465-474
    • Paitan, Y.1    Alon, G.2    Orr, E.3    Ron, E.Z.4    Rosenberg, E.5
  • 15
    • 0034673927 scopus 로고    scopus 로고
    • Isolation and characterization of the epothilone biosynthetic gene cluster from Sorangium cellulosum
    • Julien B., Shah S., Ziermann R., Goldman R., Katz L., Khosla C. Isolation and characterization of the epothilone biosynthetic gene cluster from Sorangium cellulosum. Gene. 249:2000;153-160.
    • (2000) Gene , vol.249 , pp. 153-160
    • Julien, B.1    Shah, S.2    Ziermann, R.3    Goldman, R.4    Katz, L.5    Khosla, C.6
  • 16
    • 0033762192 scopus 로고    scopus 로고
    • The myxochelin iron transport regulon of the myxobacterium Stigmatella aurantiaca Sg a15
    • Silakowski B., Kunze B., Nordsiek G., Blöcker H., Höfle G., Müller R. The myxochelin iron transport regulon of the myxobacterium Stigmatella aurantiaca Sg a15. Eur. J. Biochem. 267:2000;6476-6485.
    • (2000) Eur. J. Biochem. , vol.267 , pp. 6476-6485
    • Silakowski, B.1    Kunze, B.2    Nordsiek, G.3    Blöcker, H.4    Höfle, G.5    Müller, R.6
  • 17
    • 0035949602 scopus 로고    scopus 로고
    • In vitro reconstitution of the myxochelin biosynthetic machinery of Stigmatella aurantiaca Sg a15: Biochemical characterization of a reductive release mechanism from nonribosomal peptide synthetases
    • Gaitatzis N., Kunze B., Müller R. In vitro reconstitution of the myxochelin biosynthetic machinery of Stigmatella aurantiaca Sg a15. Biochemical characterization of a reductive release mechanism from nonribosomal peptide synthetases Proc. Natl. Acad. Sci. USA. 98:2001;11136-11141.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 11136-11141
    • Gaitatzis, N.1    Kunze, B.2    Müller, R.3
  • 18
    • 0037066791 scopus 로고    scopus 로고
    • The biosynthesis of the aromatic myxobacterial electron transport inhibitor stigmatellin is directed by a novel type of modular polyketide synthase
    • Gaitatzis N., Silakowski B., Kunze B., Nordsiek G., Blöcker H., Höfle G., Müller R. The biosynthesis of the aromatic myxobacterial electron transport inhibitor stigmatellin is directed by a novel type of modular polyketide synthase. J. Biol. Chem. 277:2002;13082-13090.
    • (2002) J. Biol. Chem. , vol.277 , pp. 13082-13090
    • Gaitatzis, N.1    Silakowski, B.2    Kunze, B.3    Nordsiek, G.4    Blöcker, H.5    Höfle, G.6    Müller, R.7
  • 19
    • 0035113529 scopus 로고    scopus 로고
    • Novel features in a combined polyketide synthase/non-ribosomal peptide synthetase: The myxalamid biosynthetic gene cluster of the myxobacterium Stigmatella aurantiaca Sg a15
    • Silakowski B., Nordsiek G., Kunze B., Blöcker H., Müller R. Novel features in a combined polyketide synthase/non-ribosomal peptide synthetase. The myxalamid biosynthetic gene cluster of the myxobacterium Stigmatella aurantiaca Sg a15 Chem. Biol. 8:2001;59-69.
    • (2001) Chem. Biol. , vol.8 , pp. 59-69
    • Silakowski, B.1    Nordsiek, G.2    Kunze, B.3    Blöcker, H.4    Müller, R.5
  • 20
    • 0034115536 scopus 로고    scopus 로고
    • Polyketide synthase gene coupled to the peptide synthetase module involved in the biosynthesis of the cyclic heptapeptide microcystin
    • Nishizawa T., Ueda A., Asayama M., Fujii K., Harada K., Ochi K., Shirai M. Polyketide synthase gene coupled to the peptide synthetase module involved in the biosynthesis of the cyclic heptapeptide microcystin. J. Biochem. (Tokyo). 127:2000;779-789.
    • (2000) J. Biochem. (Tokyo) , vol.127 , pp. 779-789
    • Nishizawa, T.1    Ueda, A.2    Asayama, M.3    Fujii, K.4    Harada, K.5    Ochi, K.6    Shirai, M.7
  • 21
    • 0033780306 scopus 로고    scopus 로고
    • Structural organization of microcystin biosynthesis in Microcystis aeruginosa PCC7806: An integrated peptide-polyketide synthetase system
    • Tillett D., Dittmann E., Erhard M., von Döhren H., Börner T., Neilan B.A. Structural organization of microcystin biosynthesis in Microcystis aeruginosa PCC7806. an integrated peptide-polyketide synthetase system Chem. Biol. 7:2000;753-764.
    • (2000) Chem. Biol. , vol.7 , pp. 753-764
    • Tillett, D.1    Dittmann, E.2    Erhard, M.3    Von Döhren, H.4    Börner, T.5    Neilan, B.A.6
  • 22
    • 0037151788 scopus 로고    scopus 로고
    • The barbamide biosynthetic gene cluster: A novel marine cyanobacterial system of mixed polyketide synthase (PKS)-non-ribosomal peptide synthetase (NRPS) origin involving an unusual trichloroleucyl starter unit
    • Chang Z.X., Flatt P., Gerwick W.H., Nguyen V.A., Willis C.L., Sherman D.H. The barbamide biosynthetic gene cluster. a novel marine cyanobacterial system of mixed polyketide synthase (PKS)-non-ribosomal peptide synthetase (NRPS) origin involving an unusual trichloroleucyl starter unit Gene. 296:2002;235-247.
    • (2002) Gene , vol.296 , pp. 235-247
    • Chang, Z.X.1    Flatt, P.2    Gerwick, W.H.3    Nguyen, V.A.4    Willis, C.L.5    Sherman, D.H.6
  • 23
    • 0019179407 scopus 로고
    • Myxothiazol, an antibiotic from Myxococcus fulvus (myxobacterales). I. Cultivation, isolation, physico-chemical and biological properties
    • Gerth K., Irschik H., Reichenbach H., Trowitzsch W. Myxothiazol, an antibiotic from Myxococcus fulvus (myxobacterales). I. Cultivation, isolation, physico-chemical and biological properties. J. Antibiot. 33:1980;1474-1479.
    • (1980) J. Antibiot. , vol.33 , pp. 1474-1479
    • Gerth, K.1    Irschik, H.2    Reichenbach, H.3    Trowitzsch, W.4
  • 24
    • 0019138460 scopus 로고
    • Myxothiazol, an antibiotic from Myxococcus fulfus (Myxobacteraoles) II. Structure elucidation
    • Trowitzsch W., Reifenstahl G., Wray V., Höfle G. Myxothiazol, an antibiotic from Myxococcus fulfus (Myxobacteraoles) II. Structure elucidation. J. Antibiot. 33:1980;1480-1490.
    • (1980) J. Antibiot. , vol.33 , pp. 1480-1490
    • Trowitzsch, W.1    Reifenstahl, G.2    Wray, V.3    Höfle, G.4
  • 25
    • 0345363099 scopus 로고    scopus 로고
    • Melithiazols, new β-methoxyacrylate inhibitors of the respiratory chain isolated from myxobacteria-production, isolation, physico-chemical and biological Properties
    • Sasse F., Böhlendorf B., Hermann M., Kunze B., Forche E., Steinmetz H., Höfle G., Reichenbach H. Melithiazols, new β-methoxyacrylate inhibitors of the respiratory chain isolated from myxobacteria-production, isolation, physico-chemical and biological Properties. J. Antibiot. 52:1999;721-729.
    • (1999) J. Antibiot. , vol.52 , pp. 721-729
    • Sasse, F.1    Böhlendorf, B.2    Hermann, M.3    Kunze, B.4    Forche, E.5    Steinmetz, H.6    Höfle, G.7    Reichenbach, H.8
  • 27
    • 0035129234 scopus 로고    scopus 로고
    • The mtaA gene of the myxothiazol biosynthetic gene cluster from Stigmatella aurantiaca DW4/3-1 encodes a phosphopantetheinyl transferase that activates polyketide synthases and polypeptide synthetases
    • Gaitatzis N., Hans A., Müller R., Beyer S. The mtaA gene of the myxothiazol biosynthetic gene cluster from Stigmatella aurantiaca DW4/3-1 encodes a phosphopantetheinyl transferase that activates polyketide synthases and polypeptide synthetases. J. Biochem. 129:2001;119-124.
    • (2001) J. Biochem. , vol.129 , pp. 119-124
    • Gaitatzis, N.1    Hans, A.2    Müller, R.3    Beyer, S.4
  • 28
    • 0035913715 scopus 로고    scopus 로고
    • Multiple hybrid polyketide synthase/non-ribosomal peptide synthetase gene clusters in the myxobacterium Stigmatella aurantiaca
    • Silakowski B., Kunze B., Müller R. Multiple hybrid polyketide synthase/non-ribosomal peptide synthetase gene clusters in the myxobacterium Stigmatella aurantiaca. Gene. 275:2001;233-240.
    • (2001) Gene , vol.275 , pp. 233-240
    • Silakowski, B.1    Kunze, B.2    Müller, R.3
  • 30
    • 0033591447 scopus 로고    scopus 로고
    • Modulation of polyketide synthase activity by accessory proteins during lovastatin biosynthesis
    • Kennedy J., Auclair K., Kendrew S.G., Park C., Vederas J.C., Hutchinson C.R. Modulation of polyketide synthase activity by accessory proteins during lovastatin biosynthesis. Science. 284:1999;1368-1372.
    • (1999) Science , vol.284 , pp. 1368-1372
    • Kennedy, J.1    Auclair, K.2    Kendrew, S.G.3    Park, C.4    Vederas, J.C.5    Hutchinson, C.R.6
  • 31
    • 0034837369 scopus 로고    scopus 로고
    • Epothilone biosynthesis: Assembly of the methylthiazolylcarboxy starter unit on the EpoB subunit
    • Chen H.W., O'Connor S., Cane D.E., Walsh C.T. Epothilone biosynthesis. assembly of the methylthiazolylcarboxy starter unit on the EpoB subunit Chem. Biol. 8:2001;899-912.
    • (2001) Chem. Biol. , vol.8 , pp. 899-912
    • Chen, H.W.1    O'Connor, S.2    Cane, D.E.3    Walsh, C.T.4
  • 33
    • 0026415106 scopus 로고
    • Modular organization of genes required for complex polyketide biosynthesis
    • Donadio S., Staver M.J., McAlpine J.B., Swanson S.J., Katz L. Modular organization of genes required for complex polyketide biosynthesis. Science. 252:1991;675-679.
    • (1991) Science , vol.252 , pp. 675-679
    • Donadio, S.1    Staver, M.J.2    McAlpine, J.B.3    Swanson, S.J.4    Katz, L.5
  • 35
    • 0037840541 scopus 로고    scopus 로고
    • Products of secondary metabolism
    • H. Kleinkauf, & H. von Döhren. Weinheim, Germany: Verlag Chemie. 277-322.pp
    • Kleinkauf H., von Döhren H. Products of secondary metabolism. Kleinkauf H., von Döhren H. Biotechnology. 1997;Verlag Chemie, Weinheim, Germany. 277-322.pp.
    • (1997) Biotechnology
    • Kleinkauf, H.1    Von Döhren, H.2
  • 36
    • 0002802459 scopus 로고
    • The myxobacterial genome
    • M. Dworkin, & D. Kaiser. Washington, D.C.: American Society for Microbiology. 85-108.pp
    • Shimkets L. The myxobacterial genome. Dworkin M., Kaiser D. Myxobacteria II. 1993;American Society for Microbiology, Washington, D.C. 85-108.pp.
    • (1993) Myxobacteria II
    • Shimkets, L.1
  • 38
    • 0037138356 scopus 로고    scopus 로고
    • Characterization of the biosynthetic gene cluster for the antifungal polyketide soraphen A from Sorangium cellulosum So ce26
    • Ligon J., Hill S., Beck J., Zirkle R., Molnar I., Zawodny J., Money S., Schupp T. Characterization of the biosynthetic gene cluster for the antifungal polyketide soraphen A from Sorangium cellulosum So ce26. Gene. 285:2002;257-267.
    • (2002) Gene , vol.285 , pp. 257-267
    • Ligon, J.1    Hill, S.2    Beck, J.3    Zirkle, R.4    Molnar, I.5    Zawodny, J.6    Money, S.7    Schupp, T.8
  • 39
    • 0035542855 scopus 로고    scopus 로고
    • Chain initiation on the soraphen-producing modular polyketide synthase from Sorangium cellulosum
    • Wilkinson C.J., Frost E.J., Staunton J., Leadlay P.F. Chain initiation on the soraphen-producing modular polyketide synthase from Sorangium cellulosum. Chem. Biol. 8:2001;1197-1208.
    • (2001) Chem. Biol. , vol.8 , pp. 1197-1208
    • Wilkinson, C.J.1    Frost, E.J.2    Staunton, J.3    Leadlay, P.F.4
  • 40
    • 0022656999 scopus 로고
    • Antibiotika aus Gleitenden Bakterien, XXVIII: Biosynthese des Myxothiazols in Myxococcus fulvus Mx f16
    • Trowitzsch-Kienast W., Wray V., Gerth K., Reichenbach H., Höfle G. Antibiotika aus Gleitenden Bakterien, XXVIII. Biosynthese des Myxothiazols in Myxococcus fulvus Mx f16 Liebigs Ann. Chem. 10:1986;93-98.
    • (1986) Liebigs Ann. Chem. , vol.10 , pp. 93-98
    • Trowitzsch-Kienast, W.1    Wray, V.2    Gerth, K.3    Reichenbach, H.4    Höfle, G.5
  • 41
    • 0037031883 scopus 로고    scopus 로고
    • A novel biosynthetic pathway providing precursors for fatty acid biosynthesis and secondary metabolite formation in myxobacteria
    • Mahmud T., Bode H.B., Silakowski B., Kroppenstedt R.M., Xu M., Nordhoff S., Höfle G., Müller R. A novel biosynthetic pathway providing precursors for fatty acid biosynthesis and secondary metabolite formation in myxobacteria. J. Biol. Chem. 277:2002;32768-32774.
    • (2002) J. Biol. Chem. , vol.277 , pp. 32768-32774
    • Mahmud, T.1    Bode, H.B.2    Silakowski, B.3    Kroppenstedt, R.M.4    Xu, M.5    Nordhoff, S.6    Höfle, G.7    Müller, R.8
  • 43
    • 0034013269 scopus 로고    scopus 로고
    • Predictive, structure-based model of amino acid recognition by nonribosomal peptide synthetase adenylation domains
    • Challis G., Ravel J., Townsend C. Predictive, structure-based model of amino acid recognition by nonribosomal peptide synthetase adenylation domains. Chem. Biol. 7:2000;211-224.
    • (2000) Chem. Biol. , vol.7 , pp. 211-224
    • Challis, G.1    Ravel, J.2    Townsend, C.3
  • 44
    • 0033179468 scopus 로고    scopus 로고
    • The specificity-conferring code of adenylation domains in nonribosomal peptide synthetases
    • Stachelhaus T., Mootz H.D., Marahiel M.A. The specificity-conferring code of adenylation domains in nonribosomal peptide synthetases. Chem. Biol. 6:1999;493-505.
    • (1999) Chem. Biol. , vol.6 , pp. 493-505
    • Stachelhaus, T.1    Mootz, H.D.2    Marahiel, M.A.3
  • 45
    • 0028557012 scopus 로고
    • The animal fatty acid synthase: One gene, one polypeptide, seven enzymes
    • Smith S. The animal fatty acid synthase. one gene, one polypeptide, seven enzymes FASEB J. 8:1994;1248-1259.
    • (1994) FASEB J. , vol.8 , pp. 1248-1259
    • Smith, S.1
  • 46
    • 0028179364 scopus 로고
    • Widespread occurrence of three sequence motifs in diverse S-adenosylmethionine-dependent methyltransferases suggest a common structure for these enzymes
    • Kagan R.M., Clarke S. Widespread occurrence of three sequence motifs in diverse S-adenosylmethionine-dependent methyltransferases suggest a common structure for these enzymes. Arch. Biochem. Biophys. 310:1994;417-427.
    • (1994) Arch. Biochem. Biophys. , vol.310 , pp. 417-427
    • Kagan, R.M.1    Clarke, S.2
  • 48
    • 0030893178 scopus 로고    scopus 로고
    • Peptides in the locusts, Locusta migratoria and Schistocerca gregaria
    • Schoof L., Veelaert D., Vanden Broeck J., De Loof A. Peptides in the locusts, Locusta migratoria and Schistocerca gregaria. Peptides. 18:1997;145-156.
    • (1997) Peptides , vol.18 , pp. 145-156
    • Schoof, L.1    Veelaert, D.2    Vanden Broeck, J.3    De Loof, A.4
  • 49
  • 50
    • 0034677981 scopus 로고    scopus 로고
    • Biosynthesis of myxothiazol Z, the ester-analog of myxothiazol A in Myxococcus fulvus
    • Steinmetz H., Forche E., Reichenbach H., Höfle G. Biosynthesis of myxothiazol Z, the ester-analog of myxothiazol A in Myxococcus fulvus. Tetrahedron. 56:2000;1681-1684.
    • (2000) Tetrahedron , vol.56 , pp. 1681-1684
    • Steinmetz, H.1    Forche, E.2    Reichenbach, H.3    Höfle, G.4
  • 51
    • 0031569882 scopus 로고    scopus 로고
    • Crystal structure of the chemotaxis receptor methyltransferase CheR suggests a conserved structural motif for binding S-adenosylmethionine
    • Djordjevic S., Stock A. Crystal structure of the chemotaxis receptor methyltransferase CheR suggests a conserved structural motif for binding S-adenosylmethionine. Curr. Biol. 5:1997;545-558.
    • (1997) Curr. Biol. , vol.5 , pp. 545-558
    • Djordjevic, S.1    Stock, A.2
  • 52
    • 0023711337 scopus 로고
    • Chemotaxis as a model second-messenger system
    • Koshland D. Jr. Chemotaxis as a model second-messenger system. Biochemistry. 27:1988;5829-5833.
    • (1988) Biochemistry , vol.27 , pp. 5829-5833
    • Koshland D., Jr.1
  • 53
    • 0035114118 scopus 로고    scopus 로고
    • The nitrilase superfamily: Classification, structure and function
    • 0001-0001.0008.
    • Pace H., Brenner C. The nitrilase superfamily. classification, structure and function Genome Biol. 2:2001;0001. 0001-0001.0008.
    • (2001) Genome Biol. , vol.2 , pp. 0001
    • Pace, H.1    Brenner, C.2
  • 54
    • 0023989064 scopus 로고
    • Improved tools for biological sequence comparison
    • Pearson W.R., Lipman D.J. Improved tools for biological sequence comparison. Proc. Natl. Acad. Sci. USA. 85:1988;2444-2448.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 2444-2448
    • Pearson, W.R.1    Lipman, D.J.2
  • 56
    • 0036917889 scopus 로고    scopus 로고
    • SAM (dependent) I AM: The S-adenosylmethionine-dependent methyltansferase fold
    • Martin J., McMillan F. SAM (dependent) I AM. the S-adenosylmethionine- dependent methyltansferase fold Curr. Opin. Struct. Biol. 12:2002;783-793.
    • (2002) Curr. Opin. Struct. Biol. , vol.12 , pp. 783-793
    • Martin, J.1    McMillan, F.2
  • 57
    • 0033554835 scopus 로고    scopus 로고
    • Purification of porcine brain protein phosphatase 2A leucine carboxyl methyltransferase and cloning of the human homologue
    • De Baere I., Derua R., Janssens V., Van Hoof C., Waelkens E., Merlevede W., Goris J. Purification of porcine brain protein phosphatase 2A leucine carboxyl methyltransferase and cloning of the human homologue. Biochemistry. 38:1999;16539-16547.
    • (1999) Biochemistry , vol.38 , pp. 16539-16547
    • De Baere, I.1    Derua, R.2    Janssens, V.3    Van Hoof, C.4    Waelkens, E.5    Merlevede, W.6    Goris, J.7
  • 58
    • 0031909727 scopus 로고    scopus 로고
    • FbfB, a gene encoding a putative galactose oxidase, is involved in Stigmatella aurantiaca fruiting body formation
    • Silakowski B., Ehret H., Schairer H.U. fbfB, a gene encoding a putative galactose oxidase, is involved in Stigmatella aurantiaca fruiting body formation. J. Bacteriol. 180:1998;1241-1247.
    • (1998) J. Bacteriol. , vol.180 , pp. 1241-1247
    • Silakowski, B.1    Ehret, H.2    Schairer, H.U.3
  • 59
    • 0026805942 scopus 로고
    • Rapid isolation of genomic DNA from Gram negative bacteria
    • Neumann B., Pospiech A., Schairer H.U. Rapid isolation of genomic DNA from Gram negative bacteria. Trends Genet. 8:1992;332-333.
    • (1992) Trends Genet. , vol.8 , pp. 332-333
    • Neumann, B.1    Pospiech, A.2    Schairer, H.U.3
  • 61
    • 0003903343 scopus 로고
    • J. Sambrook, E.F. Fritsch, & T. Maniatis. Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press
    • Sambrook J., Fritsch E.F., Maniatis T. Molecular Cloning. A Laboratory Manual Second Edition:1989;Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
    • (1989) Molecular Cloning: A Laboratory Manual Second Edition
  • 62
    • 0027968068 scopus 로고
    • Clustal w: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson J.D., Higgins D.G., Gibson T.J. Clustal w. Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice Nucleic Acids Res. 22:1994;4673-4680.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 63
    • 0033553579 scopus 로고    scopus 로고
    • Metabolic diversity in myxobacteria - Identification of the myxalamid and the stigmatellin biosynthetic gene cluster of Stigmatella aurantiaca Sg a15 and a combined polyketide- (poly)peptide gene cluster from the epothilon producing strain Sorangium cellulosum So ce90
    • Beyer S., Kunze B., Silakowski B., Müller R. Metabolic diversity in myxobacteria - identification of the myxalamid and the stigmatellin biosynthetic gene cluster of Stigmatella aurantiaca Sg a15 and a combined polyketide- (poly)peptide gene cluster from the epothilon producing strain Sorangium cellulosum So ce90. Biochim. Biophys. Acta. 1445:1999;185-195.
    • (1999) Biochim. Biophys. Acta , vol.1445 , pp. 185-195
    • Beyer, S.1    Kunze, B.2    Silakowski, B.3    Müller, R.4
  • 64
    • 0034926783 scopus 로고    scopus 로고
    • Rapid and sensitive quantitation of antibiotics in fermentations by electrospray mass spectrometry
    • Morgan J., Joyce-Menekse M., Rowlands R., Gilbert I., Lloyd D. Rapid and sensitive quantitation of antibiotics in fermentations by electrospray mass spectrometry. Rapid Commun. Mass Spectrom. 15:2001;1229-1238.
    • (2001) Rapid Commun. Mass Spectrom. , vol.15 , pp. 1229-1238
    • Morgan, J.1    Joyce-Menekse, M.2    Rowlands, R.3    Gilbert, I.4    Lloyd, D.5
  • 65
    • 0142167586 scopus 로고    scopus 로고
    • Markerless mutations in the myxothiazol biosynthetic gene cluster: A delicate megasynthetase with a superfluous nonribosomal peptide synthetase domain
    • Weinig S., Mahmud T., Müller R. Markerless mutations in the myxothiazol biosynthetic gene cluster. a delicate megasynthetase with a superfluous nonribosomal peptide synthetase domain Chem. Biol. 10:2003;953-960., this issue.
    • (2003) Chem. Biol. , vol.10 , Issue.THIS ISSUE , pp. 953-960
    • Weinig, S.1    Mahmud, T.2    Müller, R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.