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Volumn 267, Issue 2, 2000, Pages 520-526

Efficient purification and kinetic characterization of a bimodular derivative of the erythromycin polyketide synthase

Author keywords

6 deoxyerythronolide B synthase 1 thioesterase (DEBS 1 TE); Kinetic characterization; Polyketide synthase; Purification

Indexed keywords

AMMONIUM SULFATE; CARRIER PROTEIN; ERYTHROMYCIN DERIVATIVE; POLYKETIDE SYNTHASE;

EID: 0001059115     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1327.2000.01025.x     Document Type: Article
Times cited : (22)

References (47)
  • 2
    • 0025081416 scopus 로고
    • An unusually large multifunctional polypeptide in the erythromycin-producing polyketide synthase of Saccharopolyspora erythraea
    • 2. Cortés, J., Haydock, S.F., Roberts, G.A., Bevitt, D.J. & Leadlay, P.F. (1990) An unusually large multifunctional polypeptide in the erythromycin-producing polyketide synthase of Saccharopolyspora erythraea. Nature 348, 176-178.
    • (1990) Nature , vol.348 , pp. 176-178
    • Cortés, J.1    Haydock, S.F.2    Roberts, G.A.3    Bevitt, D.J.4    Leadlay, P.F.5
  • 3
    • 0026415106 scopus 로고
    • Modular organization of genes required for complex polyketide biosynthesis
    • 3. Donadio, S., Staver, M.J., McAlpine, J.B., Swanson, S.J. & Katz, L. (1991) Modular organization of genes required for complex polyketide biosynthesis. Science 252, 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
  • 4
    • 0026667294 scopus 로고
    • Complex organization of the Streptomyces avermitilis genes encoding the avermectin polyketide synthase
    • 4. MacNeil, D.J., Occi, J.L., Gewain, K.M., MacNeil, T., Gibbons, P.H., Ruby, C.L. & Danis, S.J. (1992) Complex organization of the Streptomyces avermitilis genes encoding the avermectin polyketide synthase. Gene 115, 119-125.
    • (1992) Gene , vol.115 , pp. 119-125
    • MacNeil, D.J.1    Occi, J.L.2    Gewain, K.M.3    MacNeil, T.4    Gibbons, P.H.5    Ruby, C.L.6    Danis, S.J.7
  • 5
    • 0028246348 scopus 로고
    • Correlation of the avermectin polyketide synthase genes to the avermectin structure - Implications for designing novel avermectins
    • 5. MacNeil, D.J., Occi, J.L., Gewain, K.M., MacNeil, T., Gibbons, P.H., Ruby, C.L. & Danis, S.J. (1994) Correlation of the avermectin polyketide synthase genes to the avermectin structure - implications for designing novel avermectins. Ann. N.Y. Acad. Sci. 721, 123-132.
    • (1994) Ann. N.Y. Acad. Sci. , vol.721 , pp. 123-132
    • MacNeil, D.J.1    Occi, J.L.2    Gewain, K.M.3    MacNeil, T.4    Gibbons, P.H.5    Ruby, C.L.6    Danis, S.J.7
  • 6
    • 0026511543 scopus 로고
    • 6-Deoxyerythronolide B synthase 2 from Saccharopolyspora erythraea. Cloning of the structural gene, sequence analysis and inferred domain structure of the multifunctional enzyme
    • 6. Bevitt, D.J., Cortés, J., Haydock, S.F. & Leadlay, P.F. (1992) 6-Deoxyerythronolide B synthase 2 from Saccharopolyspora erythraea. Cloning of the structural gene, sequence analysis and inferred domain structure of the multifunctional enzyme. Eur. J. Biochem. 204, 39-49.
    • (1992) Eur. J. Biochem. , vol.204 , pp. 39-49
    • Bevitt, D.J.1    Cortés, J.2    Haydock, S.F.3    Leadlay, P.F.4
  • 7
    • 0028044628 scopus 로고
    • Characterization of a Streptomyces antibioticus gene encoding a type I polyketide synthase which has an unusual coding sequence
    • 7. Swan, D.G., Rodriguez, A.M., Vilches, C., Mendez, C. & Salas, J.A. (1994) Characterization of a Streptomyces antibioticus gene encoding a type I polyketide synthase which has an unusual coding sequence. Mol. Gen. Genet. 242, 358-362.
    • (1994) Mol. Gen. Genet. , vol.242 , pp. 358-362
    • Swan, D.G.1    Rodriguez, A.M.2    Vilches, C.3    Mendez, C.4    Salas, J.A.5
  • 9
    • 0029872079 scopus 로고    scopus 로고
    • Organization of the biosynthetic gene cluster for rapamycin in Streptomyces hygroscopicus: Analysis of the enzymatic domains in the modular polyketide synthase
    • 9. Aparicio, J.F., Molnár, I., Schwecke, T., König, A., Haydock, S.F., Khaw, L.E., Staunton, J. & Leadlay, P.F. (1996) Organization of the biosynthetic gene cluster for rapamycin in Streptomyces hygroscopicus: analysis of the enzymatic domains in the modular polyketide synthase. Gene 169, 9-16.
    • (1996) Gene , vol.169 , pp. 9-16
    • Aparicio, J.F.1    Molnár, I.2    Schwecke, T.3    König, A.4    Haydock, S.F.5    Khaw, L.E.6    Staunton, J.7    Leadlay, P.F.8
  • 10
    • 0026697224 scopus 로고
    • Identification of DEBS 1, DEBS 2 and DEBS 3, the multienzyme polypeptides of the erythromycin producing polyketide synthase from Saccharopolyspora erythraea
    • 10. Caffrey, P., Bevitt, D.J., Staunton, J. & Leadlay, P.F. (1992) Identification of DEBS 1, DEBS 2 and DEBS 3, the multienzyme polypeptides of the erythromycin producing polyketide synthase from Saccharopolyspora erythraea. FEBS Lett. 304, 225-228.
    • (1992) FEBS Lett. , vol.304 , pp. 225-228
    • Caffrey, P.1    Bevitt, D.J.2    Staunton, J.3    Leadlay, P.F.4
  • 11
    • 0030249160 scopus 로고    scopus 로고
    • Generation of polyketide libraries via combinatorial synthesis
    • 11. Khosla, C. & Zawada, R.J.X. (1996) Generation of polyketide libraries via combinatorial synthesis. Trends Biotechnol. 14, 335-341.
    • (1996) Trends Biotechnol. , vol.14 , pp. 335-341
    • Khosla, C.1    Zawada, R.J.X.2
  • 12
    • 0028811381 scopus 로고
    • Polyketide synthase gene manipulation. A structure-function approach in engineering novel antibiotics
    • 12. Hutchinson, C.R. & Fujii, I. (1995) Polyketide synthase gene manipulation. A structure-function approach in engineering novel antibiotics. Annu. Rev. Microbiol. 49, 201-238.
    • (1995) Annu. Rev. Microbiol. , vol.49 , pp. 201-238
    • Hutchinson, C.R.1    Fujii, I.2
  • 13
    • 0031197020 scopus 로고    scopus 로고
    • Combinatorial approaches to polyketide biosynthesis
    • 13. Leadlay, P.F. (1997) Combinatorial approaches to polyketide biosynthesis. Curr. Opin. Chem. Biol. 1, 162-168.
    • (1997) Curr. Opin. Chem. Biol. , vol.1 , pp. 162-168
    • Leadlay, P.F.1
  • 14
    • 0032086275 scopus 로고    scopus 로고
    • Combinatorial biosynthesis of erythromycin and complex polyketides
    • 14. Staunton, J. (1998) Combinatorial biosynthesis of erythromycin and complex polyketides. Curr. Opin. Chem. Biol. 2, 339-345.
    • (1998) Curr. Opin. Chem. Biol. , vol.2 , pp. 339-345
    • Staunton, J.1
  • 15
    • 0029027352 scopus 로고
    • Repositioning of a domain in a modular polyketide synthase to promote specific chain cleavage
    • 15. Cortés, J., Wiesmann, K.E.H., Roberts, G.A., Brown, M.J.B., Staunton, J. & Leadlay, P.F. (1995) Repositioning of a domain in a modular polyketide synthase to promote specific chain cleavage. Science 268, 1487-1489.
    • (1995) Science , vol.268 , pp. 1487-1489
    • Cortés, J.1    Wiesmann, K.E.H.2    Roberts, G.A.3    Brown, M.J.B.4    Staunton, J.5    Leadlay, P.F.6
  • 16
    • 0028857296 scopus 로고
    • Manipulation of macrolide ring size by directed mutagenesis of a modular polyketide synthase
    • 16. Kao, C.M., Luo, G., Katz, L., Cane, D.E. & Khosla, C. (1995) Manipulation of macrolide ring size by directed mutagenesis of a modular polyketide synthase. J. Am. Chem. Soc. 117, 9105-9106.
    • (1995) J. Am. Chem. Soc. , vol.117 , pp. 9105-9106
    • Kao, C.M.1    Luo, G.2    Katz, L.3    Cane, D.E.4    Khosla, C.5
  • 17
    • 0028895939 scopus 로고
    • Remarkably broad substrate specificity of a modular polyketide synthase in a cell-free system
    • 17. Pieper, R., Luo, G., Cane, D.E. & Khosla, C. (1995) Remarkably broad substrate specificity of a modular polyketide synthase in a cell-free system. J. Am. Chem. Soc. 117, 11373-11374.
    • (1995) J. Am. Chem. Soc. , vol.117 , pp. 11373-11374
    • Pieper, R.1    Luo, G.2    Cane, D.E.3    Khosla, C.4
  • 19
    • 0030678504 scopus 로고    scopus 로고
    • The molecular basis of Celmer's rules: The stereochemistry of the condensation step in chain extension on the erythromycin polyketide synthase
    • 19. Weissman, K.J., Timoney, M., Bycroft, M., Grice, P., Hanefeld, U., Staunton, J. & Leadlay, P.F. (1997) The molecular basis of Celmer's rules: the stereochemistry of the condensation step in chain extension on the erythromycin polyketide synthase. Biochemistry 36, 13849-13855.
    • (1997) Biochemistry , vol.36 , pp. 13849-13855
    • Weissman, K.J.1    Timoney, M.2    Bycroft, M.3    Grice, P.4    Hanefeld, U.5    Staunton, J.6    Leadlay, P.F.7
  • 20
    • 0031259679 scopus 로고    scopus 로고
    • Molecular recognition of diketide substrates by a β-keto-acyl carrier protein synthase domain within a bimodular polyketide synthase
    • 20. Chuck, J.-A., McPherson, M., Huang, H., Jacobsen, J.R., Khosla, C. & Cane, D.E. (1997) Molecular recognition of diketide substrates by a β-keto-acyl carrier protein synthase domain within a bimodular polyketide synthase. Chem. Biol. 4, 757-766.
    • (1997) Chem. Biol. , vol.4 , pp. 757-766
    • Chuck, J.-A.1    McPherson, M.2    Huang, H.3    Jacobsen, J.R.4    Khosla, C.5    Cane, D.E.6
  • 22
    • 0033117371 scopus 로고    scopus 로고
    • Molecular basis of Celmer's rules: The role of two ketoreductase domains in the control of chirality by the erythromycin modular polyketide synthase
    • 22. Holzbaur, I.E., Harris, R.C., Bycroft, M., Cortés, J., Bisang, C., Staunton, J., Rudd, B.A.M. & Leadlay, P.F. (1999) Molecular basis of Celmer's rules: the role of two ketoreductase domains in the control of chirality by the erythromycin modular polyketide synthase. Chem. Biol. 6, 189-195.
    • (1999) Chem. Biol. , vol.6 , pp. 189-195
    • Holzbaur, I.E.1    Harris, R.C.2    Bycroft, M.3    Cortés, J.4    Bisang, C.5    Staunton, J.6    Rudd, B.A.M.7    Leadlay, P.F.8
  • 23
    • 0029797581 scopus 로고    scopus 로고
    • Evidence for two catalytically independent clusters of active sites in a functional modular polyketide synthase
    • 23. Kao, C.M., Pieper, R., Cane, D.E. & Khosla, C. (1996) Evidence for two catalytically independent clusters of active sites in a functional modular polyketide synthase. Biochemistry 35, 12363-12368.
    • (1996) Biochemistry , vol.35 , pp. 12363-12368
    • Kao, C.M.1    Pieper, R.2    Cane, D.E.3    Khosla, C.4
  • 24
    • 0032562129 scopus 로고    scopus 로고
    • Functional orientation of the acyltransferase domain in a module of the erythromycin polyketide synthase
    • 24. Gokhale, R.S., Lau, J., Cane, D.E. & Khosla, C. (1998) Functional orientation of the acyltransferase domain in a module of the erythromycin polyketide synthase. Biochemistry 37, 2524-2528.
    • (1998) Biochemistry , vol.37 , pp. 2524-2528
    • Gokhale, R.S.1    Lau, J.2    Cane, D.E.3    Khosla, C.4
  • 25
    • 0030049982 scopus 로고    scopus 로고
    • Erythromycin biosynthesis: Kinetic studies on a fully active modular polyketide synthase using natural and unnatural substrates
    • 25. Pieper, R., Ebert-Khosla, S., Cane, D.E. & Khosla, C. (1996) Erythromycin biosynthesis: kinetic studies on a fully active modular polyketide synthase using natural and unnatural substrates. Biochemistry 35, 2054-2060.
    • (1996) Biochemistry , vol.35 , pp. 2054-2060
    • Pieper, R.1    Ebert-Khosla, S.2    Cane, D.E.3    Khosla, C.4
  • 26
    • 0029856517 scopus 로고    scopus 로고
    • 6-Deoxyerythronolide B synthase 1 is specifically acylated by a diketide intermediate at the β-ketoacyl carrier protein synthase domain of module 2
    • 26. Tsukamoto, N., Chuck, J.-A., Luo, G., Kao, C.M., Khosla, C. & Cane, D.E. (1996) 6-Deoxyerythronolide B synthase 1 is specifically acylated by a diketide intermediate at the β-ketoacyl carrier protein synthase domain of module 2. Biochemistry 35, 15244-15248.
    • (1996) Biochemistry , vol.35 , pp. 15244-15248
    • Tsukamoto, N.1    Chuck, J.-A.2    Luo, G.3    Kao, C.M.4    Khosla, C.5    Cane, D.E.6
  • 27
    • 17344392088 scopus 로고    scopus 로고
    • Erythromycin biosynthesis: Exploiting the catalytic versatility of the modular polyketide synthase
    • 27. Luo, G.L., Pieper, R., Rosa, A., Khosla, C. & Cane, D.E. (1996) Erythromycin biosynthesis: exploiting the catalytic versatility of the modular polyketide synthase. Bioorg. Med. Chem. 4, 995-999.
    • (1996) Bioorg. Med. Chem. , vol.4 , pp. 995-999
    • Luo, G.L.1    Pieper, R.2    Rosa, A.3    Khosla, C.4    Cane, D.E.5
  • 28
    • 0032492685 scopus 로고    scopus 로고
    • Spontaneous priming of a downstream module in 6-deoxyerythonolide B synthase leads to polyketide biosynthesis
    • 28. Jacobsen, J.R., Cane, D.E. & Khosla, C. (1998) Spontaneous priming of a downstream module in 6-deoxyerythonolide B synthase leads to polyketide biosynthesis. Biochemistry 37, 4928-4934.
    • (1998) Biochemistry , vol.37 , pp. 4928-4934
    • Jacobsen, J.R.1    Cane, D.E.2    Khosla, C.3
  • 29
    • 0032495764 scopus 로고    scopus 로고
    • Erythromycin biosynthesis: The β-ketoreductase domains catalyze the stereospecific transfer of the 4-pro-S hydride of NADPH
    • 29. McPherson, M., Khosla, C. & Cane, D.E. (1998) Erythromycin biosynthesis: the β-ketoreductase domains catalyze the stereospecific transfer of the 4-pro-S hydride of NADPH. J. Am. Chem. Soc. 120, 3267-3268.
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 3267-3268
    • McPherson, M.1    Khosla, C.2    Cane, D.E.3
  • 30
    • 0031036573 scopus 로고    scopus 로고
    • Purification and characterization of bimodular and trimodular derivatives of the erythromycin polyketide synthase
    • 30. Pieper, R., Gokhale, R.S., Luo, G., Cane, D.E. & Khosla, C. (1997) Purification and characterization of bimodular and trimodular derivatives of the erythromycin polyketide synthase. Biochemistry 36, 1846-1851.
    • (1997) Biochemistry , vol.36 , pp. 1846-1851
    • Pieper, R.1    Gokhale, R.S.2    Luo, G.3    Cane, D.E.4    Khosla, C.5
  • 31
    • 0031931702 scopus 로고    scopus 로고
    • Catalytic self-acylation of type II polyketide synthase acyl carrier proteins
    • 31. Hitchman, T.S., Crosby, J., Byrom, K.J., Cox, R.J. & Simpson, T.J. (1998) Catalytic self-acylation of type II polyketide synthase acyl carrier proteins. Chem. Biol. 5, 35-47.
    • (1998) Chem. Biol. , vol.5 , pp. 35-47
    • Hitchman, T.S.1    Crosby, J.2    Byrom, K.J.3    Cox, R.J.4    Simpson, T.J.5
  • 32
    • 0027318089 scopus 로고
    • Heterologous expression in Escherichia coli of an intact multienzyme component of the erythromycin-producing polyketide synthase
    • 32. Roberts, G.A., Staunton, J. & Leadlay, P.F. (1993) Heterologous expression in Escherichia coli of an intact multienzyme component of the erythromycin-producing polyketide synthase. FEBS Lett. 306-311.
    • (1993) FEBS Lett. , pp. 306-311
    • Roberts, G.A.1    Staunton, J.2    Leadlay, P.F.3
  • 33
    • 0028365063 scopus 로고
    • Limited proteolysis and active site studies of the first multienzyme component of the erythromycin-producing polyketide synthase
    • 33. Aparicio, J.F., Caffrey, P., Marsden, A.F.A., Staunton, J. & Leadlay, P.F. (1994) Limited proteolysis and active site studies of the first multienzyme component of the erythromycin-producing polyketide synthase. J. Biol. Chem. 269, 8524-8528.
    • (1994) J. Biol. Chem. , vol.269 , pp. 8524-8528
    • Aparicio, J.F.1    Caffrey, P.2    Marsden, A.F.A.3    Staunton, J.4    Leadlay, P.F.5
  • 34
    • 0032541316 scopus 로고    scopus 로고
    • Construction of new vectors for high-level expression in actinomycetes
    • 34. Rowe, C.J., Cortés, J., Gaisser, S., Staunton, J. & Leadlay, P.F. (1998) Construction of new vectors for high-level expression in actinomycetes. Gene 216, 215-223.
    • (1998) Gene , vol.216 , pp. 215-223
    • Rowe, C.J.1    Cortés, J.2    Gaisser, S.3    Staunton, J.4    Leadlay, P.F.5
  • 35
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • 35. Bradford, M.M. (1976) A rapid and sensitive method for the quantitation of microgram quantities 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
  • 39
    • 0032483126 scopus 로고    scopus 로고
    • Origin of starter units for erythromycin biosynthesis
    • 39. Weissman, K.J., Bycroft, M., Staunton, J. & Leadlay, P.F. (1998) Origin of starter units for erythromycin biosynthesis. Biochemistry 37, 11012-11017.
    • (1998) Biochemistry , vol.37 , pp. 11012-11017
    • Weissman, K.J.1    Bycroft, M.2    Staunton, J.3    Leadlay, P.F.4
  • 41
    • 0031888940 scopus 로고    scopus 로고
    • The loading domain of the erythromycin polyketide synthase is not essential for erythromycin biosynthesis in Saccharopolyspora erythraea
    • 41. Pereda, A., Summers, R., Stassi, D. & Katz, L. (1998) The loading domain of the erythromycin polyketide synthase is not essential for erythromycin biosynthesis in Saccharopolyspora erythraea. Microbiology 144, 543-553.
    • (1998) Microbiology , vol.144 , pp. 543-553
    • Pereda, A.1    Summers, R.2    Stassi, D.3    Katz, L.4
  • 43
    • 0033079834 scopus 로고    scopus 로고
    • Mechanism and specificity of the terminal thioesterase domain from the erythromycin polyketide synthase
    • 43. Gokhale, R.S., Hunziker, D., Cane, D.E. & Khosla, C. (1999) Mechanism and specificity of the terminal thioesterase domain from the erythromycin polyketide synthase. Chem. Biol. 6, 117-125.
    • (1999) Chem. Biol. , vol.6 , pp. 117-125
    • Gokhale, R.S.1    Hunziker, D.2    Cane, D.E.3    Khosla, C.4
  • 44
    • 0029092263 scopus 로고
    • The thioesterase of the erythromycin-producing polyketide synthase: Mechanistic studies in vitro to investigate its mode of action and substrate specificity
    • 44. Aggarwal, R., Caffrey, P., Leadlay, P.F., Smith, C.J. & Staunton, J. (1995) The thioesterase of the erythromycin-producing polyketide synthase: mechanistic studies in vitro to investigate its mode of action and substrate specificity. J. Chem. Soc. Chem. Commun. 1519-1520.
    • (1995) J. Chem. Soc. Chem. Commun. , pp. 1519-1520
    • Aggarwal, R.1    Caffrey, P.2    Leadlay, P.F.3    Smith, C.J.4    Staunton, J.5
  • 45
    • 0032486328 scopus 로고    scopus 로고
    • The thioesterase of the erythromycin-producing polyketide synthase: Influence of acyl chain structure on the mode of release of substrate analogues from the acyl enzyme intermediates
    • 45. Weissman, K.J., Smith, C.J., Hanefeld, U., Aggarwal, R., Bycroft, M., Staunton, J. & Leadlay, P.F. (1998) The thioesterase of the erythromycin-producing polyketide synthase: influence of acyl chain structure on the mode of release of substrate analogues from the acyl enzyme intermediates. Angew. Chem. Int. Ed. 37, 1437-1440.
    • (1998) Angew. Chem. Int. Ed. , vol.37 , pp. 1437-1440
    • Weissman, K.J.1    Smith, C.J.2    Hanefeld, U.3    Aggarwal, R.4    Bycroft, M.5    Staunton, J.6    Leadlay, P.F.7
  • 46
    • 0032401977 scopus 로고    scopus 로고
    • MCAT is not required for in vitro polyketide synthesis in a minimal actinorhodin polyketide synthase from Streptomyces coelicolor
    • 46. Matharu, A.-L., Cox, R.J., Crosby, J., Byrom, K.J. & Simpson, T.J. (1998) MCAT is not required for in vitro polyketide synthesis in a minimal actinorhodin polyketide synthase from Streptomyces coelicolor. Chem. Biol. 5, 699-712.
    • (1998) Chem. Biol. , vol.5 , pp. 699-712
    • Matharu, A.-L.1    Cox, R.J.2    Crosby, J.3    Byrom, K.J.4    Simpson, T.J.5
  • 47
    • 0030723673 scopus 로고    scopus 로고
    • Gain-of-function mutagenesis of the erythromycin polyketide synthase. 2. Engineered biosynthesis of an eight-membered ring tetraketide lactone
    • 47. Kao, C.M., McPherson, M., McDaniel, R.N., Fu, H., Cane, D.E. & Khosla, C. (1997) Gain-of-function mutagenesis of the erythromycin polyketide synthase. 2. Engineered biosynthesis of an eight-membered ring tetraketide lactone. J. Am. Chem. Soc. 119, 11339-11340.
    • (1997) J. Am. Chem. Soc. , vol.119 , pp. 11339-11340
    • Kao, C.M.1    McPherson, M.2    McDaniel, R.N.3    Fu, H.4    Cane, D.E.5    Khosla, C.6


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