메뉴 건너뛰기




Volumn 11, Issue 9, 2004, Pages 888-893

An antibiotic factory caught in action

Author keywords

[No Author keywords available]

Indexed keywords

ACTINORHODINE; ACYLTRANSFERASE; AMPHOPHILE; ANTIBIOTIC AGENT; DOXORUBICIN; KETO SYNTHASE CHAIN LENGTH FACTOR; POLYKETIDE; POLYKETIDE SYNTHASE; POLYMER; TETRACYCLINE; UNCLASSIFIED DRUG;

EID: 4344578939     PISSN: 15459993     EISSN: None     Source Type: Journal    
DOI: 10.1038/nsmb808     Document Type: Article
Times cited : (145)

References (28)
  • 1
    • 0001747786 scopus 로고    scopus 로고
    • Genetic contributions to understanding polyketide syntheses
    • Hopwood, D.A. Genetic contributions to understanding polyketide syntheses. Chem. Rev. 97, 2465-2498 (1997).
    • (1997) Chem. Rev. , vol.97 , pp. 2465-2498
    • Hopwood, D.A.1
  • 2
    • 0033180108 scopus 로고    scopus 로고
    • Biosynthesis of polyketides (other than actinomycete macrolides)
    • Rawlings, B.J. Biosynthesis of polyketides (other than actinomycete macrolides). Nat. Prod. Rep. 16, 425-484 (1999).
    • (1999) Nat. Prod. Rep. , vol.16 , pp. 425-484
    • Rawlings, B.J.1
  • 3
    • 0033609915 scopus 로고    scopus 로고
    • Kinetic analysis of the actinorhodin aromatic polyketide synthase
    • Dreier, J., Shah, A.N. & Khosla, C. Kinetic analysis of the actinorhodin aromatic polyketide synthase. J. Biol. Chem. 274, 25108-25112 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 25108-25112
    • Dreier, J.1    Shah, A.N.2    Khosla, C.3
  • 4
    • 0032562124 scopus 로고    scopus 로고
    • Purification and in vitro reconstitution of the essential protein components of an aromatic polyketide synthase
    • Carreras, C.W. & Khosla, C. Purification and in vitro reconstitution of the essential protein components of an aromatic polyketide synthase. Biochemistry 37, 2084-2088 (1998).
    • (1998) Biochemistry , vol.37 , pp. 2084-2088
    • Carreras, C.W.1    Khosla, C.2
  • 5
    • 0029064652 scopus 로고
    • Rational design of aromatic polyketide natural products by recombinant assembly of enzymatic subunits
    • McDaniel, R., Ebert-Khosla, S., Hopwood, D.A. & Khosla, C. Rational design of aromatic polyketide natural products by recombinant assembly of enzymatic subunits. Nature 375, 549-554 (1995).
    • (1995) Nature , vol.375 , pp. 549-554
    • McDaniel, R.1    Ebert-Khosla, S.2    Hopwood, D.A.3    Khosla, C.4
  • 6
    • 0142135988 scopus 로고    scopus 로고
    • Polyketide chain length control by chain length factor
    • Tang, Y., Tsai, S.C. & Khosla, C. Polyketide chain length control by chain length factor. J. Am. Chem. Soc. 125, 12708-12709 (2003).
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 12708-12709
    • Tang, Y.1    Tsai, S.C.2    Khosla, C.3
  • 7
    • 0343183908 scopus 로고    scopus 로고
    • Structural modeling and site-directed mutagenesis of the actinorhodin β-ketoacyl-acyl carrier protein synthase
    • He, M., Varoglu, M. & Sherman, D.H. Structural modeling and site-directed mutagenesis of the actinorhodin β-ketoacyl-acyl carrier protein synthase. J. Bacteriol. 182, 2619-2623 (2000).
    • (2000) J. Bacteriol. , vol.182 , pp. 2619-2623
    • He, M.1    Varoglu, M.2    Sherman, D.H.3
  • 8
    • 0028174351 scopus 로고
    • The 2.8 Å crystal structure of peroxisomal 3-ketoacyl-CoA thiolase of Saccharomyces cerevisiae: A five-layered αβαβα structure constructed from two core domains of identical topology
    • Mathieu, M. et al. The 2.8 Å crystal structure of peroxisomal 3-ketoacyl-CoA thiolase of Saccharomyces cerevisiae: a five-layered αβαβα structure constructed from two core domains of identical topology. Structure 2, 797-808 (1994).
    • (1994) Structure , vol.2 , pp. 797-808
    • Mathieu, M.1
  • 9
    • 0032473567 scopus 로고    scopus 로고
    • Crystal structure of β-ketoacyl-acyl carrier protein synthase II from E. coli reveals the molecular architecture of condensing enzymes
    • Huang, W. et al. Crystal structure of β-ketoacyl-acyl carrier protein synthase II from E. coli reveals the molecular architecture of condensing enzymes. EMBO J. 17, 1183-1191 (1998).
    • (1998) EMBO J. , vol.17 , pp. 1183-1191
    • Huang, W.1
  • 10
    • 0026738080 scopus 로고
    • Functional replacement of genes for individual polyketide synthase components in Streptomyces coelicolor A 3(2) by heterologous genes from a different polyketide pathway
    • Sherman, D.H., Kim, E.S., Bibb, M.J. & Hopwood, D.A. Functional replacement of genes for individual polyketide synthase components in Streptomyces coelicolor A3(2) by heterologous genes from a different polyketide pathway. J. Bacteriol. 174, 6184-6190 (1992).
    • (1992) J. Bacteriol. , vol.174 , Issue.2 , pp. 6184-6190
    • Sherman, D.H.1    Kim, E.S.2    Bibb, M.J.3    Hopwood, D.A.4
  • 11
    • 0033619244 scopus 로고    scopus 로고
    • A chain initiation factor common to both modular and aromatic polyketide synthases
    • Bisang, C. et al. A chain initiation factor common to both modular and aromatic polyketide synthases. Nature 401, 502-505 (1999).
    • (1999) Nature , vol.401 , pp. 502-505
    • Bisang, C.1
  • 12
    • 0033533388 scopus 로고    scopus 로고
    • Conversion of a β-ketoacyl synthase to a malonyl decarboxylase by replacement of the active-site cysteine with glutamine
    • Witkowski, A., Joshi, A.K., Lindqvist, Y. & Smith, S. Conversion of a β-ketoacyl synthase to a malonyl decarboxylase by replacement of the active-site cysteine with glutamine. Biochemistry 38, 11643-11650 (1999).
    • (1999) Biochemistry , vol.38 , pp. 11643-11650
    • Witkowski, A.1    Joshi, A.K.2    Lindqvist, Y.3    Smith, S.4
  • 13
    • 0026657813 scopus 로고
    • Nucleotide sequence and deduced functions of a set of cotranscribed genes of Streptomyces coelicolor A 3(2) including the polyketide synthase for the antibiotic actinorhodin
    • Fernandez-Moreno, M.A., Martinez, E., Boto L., Hopwood, D.A. & Malpartida, F. Nucleotide sequence and deduced functions of a set of cotranscribed genes of Streptomyces coelicolor A3(2) including the polyketide synthase for the antibiotic actinorhodin. J. Biol. Chem. 267, 19278-19290 (1992).
    • (1992) J. Biol. Chem. , vol.267 , Issue.2 , pp. 19278-19290
    • Fernandez-Moreno, M.A.1    Martinez, E.2    Boto, L.3    Hopwood, D.A.4    Malpartida, F.5
  • 14
    • 0042542833 scopus 로고
    • Biomimetic syntheses of aromatic polyketide metabolites
    • Harris, T.M. & Harris, C.M. Biomimetic syntheses of aromatic polyketide metabolites. Pure Appl. Chem. 58, 283-294 (1986).
    • (1986) Pure Appl. Chem. , vol.58 , pp. 283-294
    • Harris, T.M.1    Harris, C.M.2
  • 15
    • 0034728380 scopus 로고    scopus 로고
    • Mechanistic analysis of a type II polyketide synthase. Role of conserved residues in the β-ketoacyl synthase-chain length factor heterodimer
    • Dreier, J. & Khosla, C. Mechanistic analysis of a type II polyketide synthase. Role of conserved residues in the β-ketoacyl synthase-chain length factor heterodimer. Biochemistry 39, 2088-2095 (2000).
    • (2000) Biochemistry , vol.39 , pp. 2088-2095
    • Dreier, J.1    Khosla, C.2
  • 16
    • 19344369476 scopus 로고    scopus 로고
    • Engineered biosynthesis of regioselectively modified aromatic polyketides using bimodular polyketide synthases
    • Tang, Y., Lee, T.S. & Khosla, C. Engineered biosynthesis of regioselectively modified aromatic polyketides using bimodular polyketide synthases. PLoS Biol. 2, 227-238 (2004).
    • (2004) PLoS Biol. , vol.2 , pp. 227-238
    • Tang, Y.1    Lee, T.S.2    Khosla, C.3
  • 17
    • 0032805888 scopus 로고    scopus 로고
    • Structure of chalcone synthase and the molecular basis of plant polyketide biosynthesis
    • Ferrer, J.L., Jez, J.M., Bowman, M.E., Dixon, R.A. & Noel, J.P. Structure of chalcone synthase and the molecular basis of plant polyketide biosynthesis. Nat. Struct. Biol. 6, 775-784 (1999).
    • (1999) Nat. Struct. Biol. , vol.6 , pp. 775-784
    • Ferrer, J.L.1    Jez, J.M.2    Bowman, M.E.3    Dixon, R.A.4    Noel, J.P.5
  • 18
    • 0027746346 scopus 로고
    • Engineered biosynthesis of novel polyketides: Manipulation and analysis of an aromatic polyketide synthase with unproven catalytic specificities
    • McDaniel, R., Ebert-Khosla, S., Hopwood, D.A. & Khosla, C. Engineered biosynthesis of novel polyketides: manipulation and analysis of an aromatic polyketide synthase with unproven catalytic specificities. J. Am. Chem. Soc. 115, 11671-11675 (1993).
    • (1993) J. Am. Chem. Soc. , vol.115 , pp. 11671-11675
    • McDaniel, R.1    Ebert-Khosla, S.2    Hopwood, D.A.3    Khosla, C.4
  • 19
    • 0027381037 scopus 로고
    • The tcm VI region of the tetracenomycin C biosynthetic gene cluster of Streptomyces glaucescens encodes the tetracenomycin F1 monooxygenase, tetracenomycin F2 cyclase, and, most likely, a second cyclase
    • Summers, R.G., Wendt-Pienkowski, E., Motamedi, H. & Hutchinson, C.R. The tcm VI region of the tetracenomycin C biosynthetic gene cluster of Streptomyces glaucescens encodes the tetracenomycin F1 monooxygenase, tetracenomycin F2 cyclase, and, most likely, a second cyclase. J. Bacteriol. 175, 7571-7580 (1993).
    • (1993) J. Bacteriol. , vol.175 , pp. 7571-7580
    • Summers, R.G.1    Wendt-Pienkowski, E.2    Motamedi, H.3    Hutchinson, C.R.4
  • 20
    • 0031047160 scopus 로고    scopus 로고
    • Rational design and engineered biosynthesis of a novel 18-carbon aromatic polyketide
    • Kramer, P.J. et al. Rational design and engineered biosynthesis of a novel 18-carbon aromatic polyketide. J. Am. Chem. Soc. 119, 635-639 (1997).
    • (1997) J. Am. Chem. Soc. , vol.119 , pp. 635-639
    • Kramer, P.J.1
  • 21
    • 0037314870 scopus 로고    scopus 로고
    • Catalysis, specificity, and ACP docking site of Streptomyces coelicolor malonyl-CoA:ACP transacylase
    • Keatinge-Clay, A.T. et al. Catalysis, specificity, and ACP docking site of Streptomyces coelicolor malonyl-CoA:ACP transacylase. Structure (Camb.) 11, 147-154 (2003).
    • (2003) Structure (Camb.) , vol.11 , pp. 147-154
    • Keatinge-Clay, A.T.1
  • 22
    • 0030972114 scopus 로고    scopus 로고
    • Solution structure of the actinorhodin polyketide synthase acyl carrier protein from Streptomyces coelicolor A 3(2)
    • Crump, M.P. et al. Solution structure of the actinorhodin polyketide synthase acyl carrier protein from Streptomyces coelicolor A3(2). Biochemistry 36, 6000-6008 (1997).
    • (1997) Biochemistry , vol.36 , Issue.2 , pp. 6000-6008
    • Crump, M.P.1
  • 23
    • 0037439266 scopus 로고    scopus 로고
    • The structure of ActVA-Orf 6, a novel type of monooxygenase involved in actinorhodin biosynthesis
    • Sciara, G. et al. The structure of ActVA-Orf6, a novel type of monooxygenase involved in actinorhodin biosynthesis. EMBO J. 22, 205-215 (2003).
    • (2003) EMBO J. , vol.22 , pp. 205-215
    • Sciara, G.1
  • 24
    • 0036848668 scopus 로고    scopus 로고
    • Crystal structure of the priming β-ketosynthase from the R1128 polyketide biosynthetic pathway
    • Pan, H. et al. Crystal structure of the priming β-ketosynthase from the R1128 polyketide biosynthetic pathway. Structure (Camb.) 10, 1559-1568 (2002).
    • (2002) Structure (Camb.) , vol.10 , pp. 1559-1568
    • Pan, H.1
  • 26
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski, Z. & Minor, W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276, 307-326 (1997).
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 27
    • 3543012707 scopus 로고    scopus 로고
    • Crystallography & NMR system: A new software suite for macro-molecular structure determination
    • Brunger, A.T. et al. Crystallography & NMR system: a new software suite for macro-molecular structure determination. Acta Crystallogr. D Biol. Crystallogr. 54, 905-921 (1998).
    • (1998) Acta Crystallogr. D Biol. Crystallogr. , vol.54 , pp. 905-921
    • Brunger, A.T.1
  • 28
    • 0025617140 scopus 로고
    • Appendix 5. Nomenclature for peptide fragment ions (positive ions)
    • Biemann, K. Appendix 5. Nomenclature for peptide fragment ions (positive ions). Methods Enzymol. 193, 886-887 (1990).
    • (1990) Methods Enzymol. , vol.193 , pp. 886-887
    • Biemann, K.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.