메뉴 건너뛰기




Volumn 459, Issue B, 2009, Pages 367-393

Chapter 16 In Vitro Analysis of Type II Polyketide Synthase

Author keywords

[No Author keywords available]

Indexed keywords

ACYL CARRIER PROTEIN; BACTERIAL ENZYME; GLYCOSYLTRANSFERASE; METHYLTRANSFERASE; OXYGENASE; POLYKETIDE SYNTHASE; POLYKETIDE SYNTHASE 2; SCAFFOLD PROTEIN; UNCLASSIFIED DRUG;

EID: 64049110816     PISSN: 00766879     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S0076-6879(09)04616-3     Document Type: Review
Times cited : (21)

References (70)
  • 1
    • 0032532250 scopus 로고    scopus 로고
    • A gene cluster encoding malonyl-CoA decarboxylase (MatA), malonyl-CoA synthetase (MatB). and a putative dicarboxylate carrier protein (MatC). in Rhizobium trifolii-cloning, sequencing, and expression of the enzymes in Escherichia coli
    • An J.H., and Kim Y.S. A gene cluster encoding malonyl-CoA decarboxylase (MatA), malonyl-CoA synthetase (MatB). and a putative dicarboxylate carrier protein (MatC). in Rhizobium trifolii-cloning, sequencing, and expression of the enzymes in Escherichia coli. Eur. J. Biochem. 257 (1998) 395-402
    • (1998) Eur. J. Biochem. , vol.257 , pp. 395-402
    • An, J.H.1    Kim, Y.S.2
  • 3
    • 0033609499 scopus 로고    scopus 로고
    • Purification and properties of the Streptomyces peucetius DpsC beta-ketoacyl:acyl carrier protein synthase III that specifies the propionate-starter unit for type II polyketide biosynthesis
    • Bao W., Sheldon P.J., and Hutchinson C.R. Purification and properties of the Streptomyces peucetius DpsC beta-ketoacyl:acyl carrier protein synthase III that specifies the propionate-starter unit for type II polyketide biosynthesis. Biochemistry 38 (1999) 9752-9757
    • (1999) Biochemistry , vol.38 , pp. 9752-9757
    • Bao, W.1    Sheldon, P.J.2    Hutchinson, C.R.3
  • 5
    • 37249075864 scopus 로고    scopus 로고
    • Dissecting the component reactions catalyzed by the actinorhodin minimal polyketide synthase
    • Beltran-Alvarez P., Cox R.J., Crosby J., and Simpson T.J. Dissecting the component reactions catalyzed by the actinorhodin minimal polyketide synthase. Biochemistry 46 (2007) 14672-14681
    • (2007) Biochemistry , vol.46 , pp. 14672-14681
    • Beltran-Alvarez, P.1    Cox, R.J.2    Crosby, J.3    Simpson, T.J.4
  • 6
    • 0028351394 scopus 로고
    • Cloning, sequencing and deduced functions of a cluster of Streptomyces genes probably encoding biosynthesis of the polyketide antibiotic frenolicin
    • Bibb M.J., Sherman D.H., Omura S., and Hopwood D.A. Cloning, sequencing and deduced functions of a cluster of Streptomyces genes probably encoding biosynthesis of the polyketide antibiotic frenolicin. Gene 142 (1994) 31-39
    • (1994) Gene , vol.142 , pp. 31-39
    • Bibb, M.J.1    Sherman, D.H.2    Omura, S.3    Hopwood, D.A.4
  • 8
    • 0032562124 scopus 로고    scopus 로고
    • Purification and in vitro reconstitution of the essential protein components of an aromatic polyketide synthase
    • Carreras C.W., and Khosla C. Purification and in vitro reconstitution of the essential protein components of an aromatic polyketide synthase. Biochemistry 37 (1998) 2084-2088
    • (1998) Biochemistry , vol.37 , pp. 2084-2088
    • Carreras, C.W.1    Khosla, C.2
  • 9
    • 20444496509 scopus 로고    scopus 로고
    • Functional analyses of oxygenases in jadomycin biosynthesis and identification of JadH as a bifunctional oxygenase/dehydrase
    • Chen Y.H., Wang C.C., Greenwell L., Rix U., Hoffmeister D., Vining L.C., Rohr J., and Yang K.Q. Functional analyses of oxygenases in jadomycin biosynthesis and identification of JadH as a bifunctional oxygenase/dehydrase. J. Biol. Chem. 280 (2005) 22508-22514
    • (2005) J. Biol. Chem. , vol.280 , pp. 22508-22514
    • Chen, Y.H.1    Wang, C.C.2    Greenwell, L.3    Rix, U.4    Hoffmeister, D.5    Vining, L.C.6    Rohr, J.7    Yang, K.Q.8
  • 11
    • 0034973583 scopus 로고    scopus 로고
    • Tetracycline antibiotics: Mode of action, applications, molecular biology, and epidemiology of bacterial resistance
    • Chopra I., and Roberts M. Tetracycline antibiotics: Mode of action, applications, molecular biology, and epidemiology of bacterial resistance. Microbiol. Mol. Biol. Rev. 65 (2001) 232-260
    • (2001) Microbiol. Mol. Biol. Rev. , vol.65 , pp. 232-260
    • Chopra, I.1    Roberts, M.2
  • 12
    • 0036843634 scopus 로고    scopus 로고
    • Expression, purification, and characterization of AknX anthrone oxygenase, which is involved in aklavinone biosynthesis in Streptomyces galilaeus
    • Chung J.Y., Fujii I., Harada S., Sankawa U., and Ebizuka Y. Expression, purification, and characterization of AknX anthrone oxygenase, which is involved in aklavinone biosynthesis in Streptomyces galilaeus. J. Bacteriol. 184 (2002) 6115-6122
    • (2002) J. Bacteriol. , vol.184 , pp. 6115-6122
    • Chung, J.Y.1    Fujii, I.2    Harada, S.3    Sankawa, U.4    Ebizuka, Y.5
  • 13
    • 33750364236 scopus 로고    scopus 로고
    • Dissecting non-ribosomal and polyketide biosynthetic machineries using electrospray ionization Fourier-transform mass spectrometry
    • Dorrestein P.C., and Kelleher N.L. Dissecting non-ribosomal and polyketide biosynthetic machineries using electrospray ionization Fourier-transform mass spectrometry. Nat. Prod. Rep. 23 (2006) 893-918
    • (2006) Nat. Prod. Rep. , vol.23 , pp. 893-918
    • Dorrestein, P.C.1    Kelleher, N.L.2
  • 15
    • 0033609915 scopus 로고    scopus 로고
    • Kinetic analysis of the actinorhodin aromatic polyketide synthase
    • Dreier J., Shah A.N., and Khosla C. Kinetic analysis of the actinorhodin aromatic polyketide synthase. J. Biol. Chem. 274 (1999) 25108-25112
    • (1999) J. Biol. Chem. , vol.274 , pp. 25108-25112
    • Dreier, J.1    Shah, A.N.2    Khosla, C.3
  • 16
    • 29344449110 scopus 로고    scopus 로고
    • Characterization of kinetics and products of the Baeyer-Villiger oxygenase MtmOIV, the key enzyme of the biosynthetic pathway toward the natural product anticancer drug mithramycin from Streptomyces argillaceus
    • Gibson M., Nur-e-alam M., Lipata F., Oliveira M.A., and Rohr J. Characterization of kinetics and products of the Baeyer-Villiger oxygenase MtmOIV, the key enzyme of the biosynthetic pathway toward the natural product anticancer drug mithramycin from Streptomyces argillaceus. J. Am. Chem. Soc. 127 (2005) 17594-17595
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 17594-17595
    • Gibson, M.1    Nur-e-alam, M.2    Lipata, F.3    Oliveira, M.A.4    Rohr, J.5
  • 17
    • 33846923183 scopus 로고    scopus 로고
    • Type II polyketide synthases: Gaining a deeper insight into enzymatic teamwork
    • Hertweck C., Luzhetskyy A., Rebets Y., and Bechthold A. Type II polyketide synthases: Gaining a deeper insight into enzymatic teamwork. Nat. Prod. Rep. 24 (2007) 162-190
    • (2007) Nat. Prod. Rep. , vol.24 , pp. 162-190
    • Hertweck, C.1    Luzhetskyy, A.2    Rebets, Y.3    Bechthold, A.4
  • 18
    • 51449108130 scopus 로고    scopus 로고
    • Incorporation of fluoroacetate into an aromatic polyketide and its influence on the mode of cyclization
    • Hong H., Spiteller D., and Spencer J.B. Incorporation of fluoroacetate into an aromatic polyketide and its influence on the mode of cyclization. Angew. Chem. Int. Ed. 47 (2008) 6028-6032
    • (2008) Angew. Chem. Int. Ed. , vol.47 , pp. 6028-6032
    • Hong, H.1    Spiteller, D.2    Spencer, J.B.3
  • 20
    • 0001747786 scopus 로고    scopus 로고
    • Genetic contributions to understanding polyketide synthases
    • Hopwood D.A. Genetic contributions to understanding polyketide synthases. Chem. Rev. 97 (1997) 2465-2498
    • (1997) Chem. Rev. , vol.97 , pp. 2465-2498
    • Hopwood, D.A.1
  • 21
    • 34447333393 scopus 로고    scopus 로고
    • Actinorhodin biosynthesis: Structural requirements for post-PKS tailoring intermediates revealed by functional analysis of ActVI-ORF1 reductase
    • Itoh T., Taguchi T., Kimberley M.R., Booker-Milburn K.I., Stephenson G.R., Ebizuka Y., and Ichinose K. Actinorhodin biosynthesis: Structural requirements for post-PKS tailoring intermediates revealed by functional analysis of ActVI-ORF1 reductase. Biochemistry 46 (2007) 8181-8188
    • (2007) Biochemistry , vol.46 , pp. 8181-8188
    • Itoh, T.1    Taguchi, T.2    Kimberley, M.R.3    Booker-Milburn, K.I.4    Stephenson, G.R.5    Ebizuka, Y.6    Ichinose, K.7
  • 22
    • 32244443360 scopus 로고    scopus 로고
    • Priming type II polyketide synthases via a type II nonribosomal peptide synthetase mechanism
    • Izumikawa M., Cheng Q., and Moore B.S. Priming type II polyketide synthases via a type II nonribosomal peptide synthetase mechanism. J. Am. Chem. Soc. 128 (2006) 1428-1429
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 1428-1429
    • Izumikawa, M.1    Cheng, Q.2    Moore, B.S.3
  • 23
    • 4644371272 scopus 로고    scopus 로고
    • Crystal structure of a ternary complex of DnrK, a methyltransferase in daunorubicin biosynthesis, with bound products
    • Jansson A., Koskiniemi H., Mantsala P., Niemi J., and Schneider G. Crystal structure of a ternary complex of DnrK, a methyltransferase in daunorubicin biosynthesis, with bound products. J. Biol. Chem. 279 (2004) 41149-41156
    • (2004) J. Biol. Chem. , vol.279 , pp. 41149-41156
    • Jansson, A.1    Koskiniemi, H.2    Mantsala, P.3    Niemi, J.4    Schneider, G.5
  • 24
    • 39149093384 scopus 로고    scopus 로고
    • Sequential action of two flavoenzymes, PgaE and PgaM, in angucycline biosynthesis: Chemoenzymatic synthesis of gaudimycin C
    • Kallio P., Liu Z., Mantsala P., Niemi J., and Metsa-Ketela M. Sequential action of two flavoenzymes, PgaE and PgaM, in angucycline biosynthesis: Chemoenzymatic synthesis of gaudimycin C. Chem. Biol. 15 (2008) 157-166
    • (2008) Chem. Biol. , vol.15 , pp. 157-166
    • Kallio, P.1    Liu, Z.2    Mantsala, P.3    Niemi, J.4    Metsa-Ketela, M.5
  • 25
    • 33644766092 scopus 로고    scopus 로고
    • Crystal structure of the polyketide cyclase AknH with bound substrate and product analogue: Implications for catalytic mechanism and product stereoselectivity
    • Kallio P., Sultana A., Niemi J., Mantsala P., and Schneider G. Crystal structure of the polyketide cyclase AknH with bound substrate and product analogue: Implications for catalytic mechanism and product stereoselectivity. J. Mol. Biol. 357 (2006) 210-220
    • (2006) J. Mol. Biol. , vol.357 , pp. 210-220
    • Kallio, P.1    Sultana, A.2    Niemi, J.3    Mantsala, P.4    Schneider, G.5
  • 27
    • 0030858888 scopus 로고    scopus 로고
    • Identification of a monooxygenase from Streptomyces coelicolor A3(2) involved in biosynthesis of actinorhodin: Purification and characterization of the recombinant enzyme
    • Kendrew S.G., Hopwood D.A., and Marsh E.N. Identification of a monooxygenase from Streptomyces coelicolor A3(2) involved in biosynthesis of actinorhodin: Purification and characterization of the recombinant enzyme. J. Bacteriol. 179 (1997) 4305-4310
    • (1997) J. Bacteriol. , vol.179 , pp. 4305-4310
    • Kendrew, S.G.1    Hopwood, D.A.2    Marsh, E.N.3
  • 28
    • 0033551194 scopus 로고    scopus 로고
    • DnrD cyclase involved in the biosynthesis of doxorubicin: Purification and characterization of the recombinant enzyme
    • Kendrew S.G., Katayama K., Deutsch E., Madduri K., and Hutchinson C.R. DnrD cyclase involved in the biosynthesis of doxorubicin: Purification and characterization of the recombinant enzyme. Biochemistry 38 (1999) 4794-4799
    • (1999) Biochemistry , vol.38 , pp. 4794-4799
    • Kendrew, S.G.1    Katayama, K.2    Deutsch, E.3    Madduri, K.4    Hutchinson, C.R.5
  • 31
    • 0141653942 scopus 로고    scopus 로고
    • Structure-based mutagenesis of the malonyl-CoA:Acyl carrier protein transacylase from Streptomyces coelicolor
    • Koppisch A.T., and Khosla C. Structure-based mutagenesis of the malonyl-CoA:Acyl carrier protein transacylase from Streptomyces coelicolor. Biochemistry 42 (2003) 11057-11064
    • (2003) Biochemistry , vol.42 , pp. 11057-11064
    • Koppisch, A.T.1    Khosla, C.2
  • 32
    • 39649122833 scopus 로고    scopus 로고
    • Inhibition kinetics and emodin cocrystal structure of a type II polyketide ketoreductase
    • Korman T.P., Tan Y.H., Wong J., Luo R., and Tsai S.C. Inhibition kinetics and emodin cocrystal structure of a type II polyketide ketoreductase. Biochemistry 47 (2008) 1837-1847
    • (2008) Biochemistry , vol.47 , pp. 1837-1847
    • Korman, T.P.1    Tan, Y.H.2    Wong, J.3    Luo, R.4    Tsai, S.C.5
  • 34
    • 28244441235 scopus 로고    scopus 로고
    • Orthogonal protein interactions in spore pigment producing and antibiotic producing polyketide synthases
    • Lee T.S., Khosla C., and Tang Y. Orthogonal protein interactions in spore pigment producing and antibiotic producing polyketide synthases. J. Antibiot. (Tokyo) 58 (2005) 663-666
    • (2005) J. Antibiot. (Tokyo) , vol.58 , pp. 663-666
    • Lee, T.S.1    Khosla, C.2    Tang, Y.3
  • 35
    • 34548214188 scopus 로고    scopus 로고
    • Characterization of rhodosaminyl transfer by the AknS/AknT glycosylation complex and its use in reconstituting the biosynthetic pathway of aclacinomycin A
    • Leimkuhler C., Fridman M., Lupoli T., Walker S., Walsh C.T., and Kahne D. Characterization of rhodosaminyl transfer by the AknS/AknT glycosylation complex and its use in reconstituting the biosynthetic pathway of aclacinomycin A. J. Am. Chem. Soc. 129 (2007) 10546-10550
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 10546-10550
    • Leimkuhler, C.1    Fridman, M.2    Lupoli, T.3    Walker, S.4    Walsh, C.T.5    Kahne, D.6
  • 36
    • 0034603167 scopus 로고    scopus 로고
    • Characterization of two polyketide methyltransferases involved in the biosynthesis of the antitumor drug mithramycin by Streptomyces argillaceus
    • Lozano M.J., Remsing L.L., Quiros L.M., Brana A.F., Fernandez E., Sanchez C., Mendez C., Rohr J., and Salas J.A. Characterization of two polyketide methyltransferases involved in the biosynthesis of the antitumor drug mithramycin by Streptomyces argillaceus. J. Biol. Chem. 275 (2000) 3065-3074
    • (2000) J. Biol. Chem. , vol.275 , pp. 3065-3074
    • Lozano, M.J.1    Remsing, L.L.2    Quiros, L.M.3    Brana, A.F.4    Fernandez, E.5    Sanchez, C.6    Mendez, C.7    Rohr, J.8    Salas, J.A.9
  • 37
    • 19544377358 scopus 로고    scopus 로고
    • AknT is an activating protein for the glycosyltransferase AknS in L-aminodeoxysugar transfer to the aglycone of aclacinomycin A
    • Lu W., Leimkuhler C., Gatto Jr. G.J., Kruger R.G., Oberthur M., Kahne D., and Walsh C.T. AknT is an activating protein for the glycosyltransferase AknS in L-aminodeoxysugar transfer to the aglycone of aclacinomycin A. Chem. Biol. 12 (2005) 527-534
    • (2005) Chem. Biol. , vol.12 , pp. 527-534
    • Lu, W.1    Leimkuhler, C.2    Gatto Jr., G.J.3    Kruger, R.G.4    Oberthur, M.5    Kahne, D.6    Walsh, C.T.7
  • 38
    • 4444222040 scopus 로고    scopus 로고
    • AknK is an L-2-deoxyfucosyltransferase in the biosynthesis of the anthracycline aclacinomycin A
    • Lu W., Leimkuhler C., Oberthur M., Kahne D., and Walsh C.T. AknK is an L-2-deoxyfucosyltransferase in the biosynthesis of the anthracycline aclacinomycin A. Biochemistry 43 (2004) 4548-4558
    • (2004) Biochemistry , vol.43 , pp. 4548-4558
    • Lu, W.1    Leimkuhler, C.2    Oberthur, M.3    Kahne, D.4    Walsh, C.T.5
  • 40
    • 0021238139 scopus 로고
    • Molecular cloning of the whole biosynthetic pathway of a Streptomyces antibiotic and its expression in a heterologous host
    • Malpartida F., and Hopwood D.A. Molecular cloning of the whole biosynthetic pathway of a Streptomyces antibiotic and its expression in a heterologous host. Nature 309 (1984) 462-464
    • (1984) Nature , vol.309 , pp. 462-464
    • Malpartida, F.1    Hopwood, D.A.2
  • 42
    • 0029064652 scopus 로고
    • Rational design of aromatic polyketide natural products by recombinant assembly of enzymatic subunits
    • McDaniel R., Ebert-Khosla S., Hopwood D.A., and Khosla C. Rational design of aromatic polyketide natural products by recombinant assembly of enzymatic subunits. Nature 375 (1995) 549-554
    • (1995) Nature , vol.375 , pp. 549-554
    • McDaniel, R.1    Ebert-Khosla, S.2    Hopwood, D.A.3    Khosla, C.4
  • 43
    • 0035846645 scopus 로고    scopus 로고
    • In vitro reconstitution and analysis of the chain initiating enzymes of the R1128 polyketide synthase
    • Meadows E.S., and Khosla C. In vitro reconstitution and analysis of the chain initiating enzymes of the R1128 polyketide synthase. Biochemistry 40 (2001) 14855-14861
    • (2001) Biochemistry , vol.40 , pp. 14855-14861
    • Meadows, E.S.1    Khosla, C.2
  • 44
    • 0037459418 scopus 로고    scopus 로고
    • First in vitro directed biosynthesis of new compounds by a minimal type II polyketide synthase: Evidence for the mechanism of chain length determination
    • Nicholson T.P., Winfield C., Westcott J., Crosby J., Simpson T.J., and Cox R.J. First in vitro directed biosynthesis of new compounds by a minimal type II polyketide synthase: Evidence for the mechanism of chain length determination. Chem. Commun. (Camb.) 6 (2003) 686-687
    • (2003) Chem. Commun. (Camb.) , vol.6 , pp. 686-687
    • Nicholson, T.P.1    Winfield, C.2    Westcott, J.3    Crosby, J.4    Simpson, T.J.5    Cox, R.J.6
  • 47
    • 0035793858 scopus 로고    scopus 로고
    • Biosynthesis of complex polyketides in a metabolically engineered strain of E. coli
    • Pfeifer B.A., Admiraal S.J., Gramajo H., Cane D.E., and Khosla C. Biosynthesis of complex polyketides in a metabolically engineered strain of E. coli. Science 291 (2001) 1790-1792
    • (2001) Science , vol.291 , pp. 1790-1792
    • Pfeifer, B.A.1    Admiraal, S.J.2    Gramajo, H.3    Cane, D.E.4    Khosla, C.5
  • 48
    • 0034521526 scopus 로고    scopus 로고
    • Cloning, sequencing and analysis of the enterocin biosynthesis gene cluster from the marine isolate "Streptomyces maritimus": Evidence for the derailment of an aromatic polyketide synthase
    • Piel J., Hertweck C., Shipley P.R., Hunt D.M., Newman M.S., and Moore B.S. Cloning, sequencing and analysis of the enterocin biosynthesis gene cluster from the marine isolate "Streptomyces maritimus": Evidence for the derailment of an aromatic polyketide synthase. Chem. Biol. 7 (2000) 943-955
    • (2000) Chem. Biol. , vol.7 , pp. 943-955
    • Piel, J.1    Hertweck, C.2    Shipley, P.R.3    Hunt, D.M.4    Newman, M.S.5    Moore, B.S.6
  • 49
    • 0034609696 scopus 로고    scopus 로고
    • Triple hydroxylation of tetracenomycin A2 to tetracenomycin C involving two molecules of O(2) and one molecule of H(2)O
    • Rafanan Jr. E.R., Hutchinson C.R., and Shen B. Triple hydroxylation of tetracenomycin A2 to tetracenomycin C involving two molecules of O(2) and one molecule of H(2)O. Org. Lett. 2 (2000) 3225-3227
    • (2000) Org. Lett. , vol.2 , pp. 3225-3227
    • Rafanan Jr., E.R.1    Hutchinson, C.R.2    Shen, B.3
  • 50
    • 0036774667 scopus 로고    scopus 로고
    • Modification of post-PKS tailoring steps through combinatorial biosynthesis
    • Rix U., Fischer C., Remsing L.L., and Rohr J. Modification of post-PKS tailoring steps through combinatorial biosynthesis. Nat. Prod. Rep. 19 (2002) 542-580
    • (2002) Nat. Prod. Rep. , vol.19 , pp. 542-580
    • Rix, U.1    Fischer, C.2    Remsing, L.L.3    Rohr, J.4
  • 51
    • 0027301951 scopus 로고
    • Tetracenomycin F1 monooxygenase: Oxidation of a naphthacenone to a naphthacenequinone in the biosynthesis of tetracenomycin C in Streptomyces glaucescens
    • Shen B., and Hutchinson C.R. Tetracenomycin F1 monooxygenase: Oxidation of a naphthacenone to a naphthacenequinone in the biosynthesis of tetracenomycin C in Streptomyces glaucescens. Biochemistry 32 (1993) 6656-6663
    • (1993) Biochemistry , vol.32 , pp. 6656-6663
    • Shen, B.1    Hutchinson, C.R.2
  • 52
    • 0028072618 scopus 로고
    • Triple hydroxylation of tetracenomycin A2 to tetracenomycin C in Streptomyces glaucescens. Overexpression of the tcmG gene in Streptomyces lividans and characterization of the tetracenomycin A2 oxygenase
    • Shen B., and Hutchinson C.R. Triple hydroxylation of tetracenomycin A2 to tetracenomycin C in Streptomyces glaucescens. Overexpression of the tcmG gene in Streptomyces lividans and characterization of the tetracenomycin A2 oxygenase. J. Biol. Chem. 269 (1994) 30726-30733
    • (1994) J. Biol. Chem. , vol.269 , pp. 30726-30733
    • Shen, B.1    Hutchinson, C.R.2
  • 53
    • 0029900903 scopus 로고    scopus 로고
    • Deciphering the mechanism for the assembly of aromatic polyketides by a bacterial polyketide synthase
    • Shen B., and Hutchinson C.R. Deciphering the mechanism for the assembly of aromatic polyketides by a bacterial polyketide synthase. Proc. Natl. Acad. Sci. USA 93 (1996) 6600-6604
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 6600-6604
    • Shen, B.1    Hutchinson, C.R.2
  • 54
    • 27744530255 scopus 로고    scopus 로고
    • A method for trapping intermediates of polyketide biosynthesis with a nonhydrolyzable malonyl-coenzyme A analogue
    • Spiteller D., Waterman C.L., and Spencer J.B. A method for trapping intermediates of polyketide biosynthesis with a nonhydrolyzable malonyl-coenzyme A analogue. Angew. Chem. Int. Ed. 44 (2005) 7079-7082
    • (2005) Angew. Chem. Int. Ed. , vol.44 , pp. 7079-7082
    • Spiteller, D.1    Waterman, C.L.2    Spencer, J.B.3
  • 55
    • 3142559476 scopus 로고    scopus 로고
    • Structure of the polyketide cyclase SnoaL reveals a novel mechanism for enzymatic aldol condensation
    • Sultana A., Kallio P., Jansson A., Wang J.S., Niemi J., Mantsala P., and Schneider G. Structure of the polyketide cyclase SnoaL reveals a novel mechanism for enzymatic aldol condensation. EMBO J. 23 (2004) 1911-1921
    • (2004) EMBO J. , vol.23 , pp. 1911-1921
    • Sultana, A.1    Kallio, P.2    Jansson, A.3    Wang, J.S.4    Niemi, J.5    Mantsala, P.6    Schneider, G.7
  • 56
    • 0029125339 scopus 로고
    • Malonyl-coenzyme A:acyl carrier protein acyltransferase of Streptomyces glaucescens: A possible link between fatty acid and polyketide biosynthesis
    • Summers R.G., Ali A., Shen B., Wessel W.A., and Hutchinson C.R. Malonyl-coenzyme A:acyl carrier protein acyltransferase of Streptomyces glaucescens: A possible link between fatty acid and polyketide biosynthesis. Biochemistry 34 (1995) 9389-9402
    • (1995) Biochemistry , vol.34 , pp. 9389-9402
    • Summers, R.G.1    Ali, A.2    Shen, B.3    Wessel, W.A.4    Hutchinson, C.R.5
  • 57
    • 0028867394 scopus 로고
    • Construction of thiostrepton-inducible, high-copy-number expression vectors for use in Streptomyces spp
    • Takano E., White J., Thompson C.J., and Bibb M.J. Construction of thiostrepton-inducible, high-copy-number expression vectors for use in Streptomyces spp. Gene 166 (1995) 133-137
    • (1995) Gene , vol.166 , pp. 133-137
    • Takano, E.1    White, J.2    Thompson, C.J.3    Bibb, M.J.4
  • 58
    • 3242738305 scopus 로고    scopus 로고
    • The acyltransferase homologue from the initiation module of the R1128 polyketide synthase is an acyl-ACP thioesterase that edits acetyl primer units
    • Tang Y., Koppisch A.T., and Khosla C. The acyltransferase homologue from the initiation module of the R1128 polyketide synthase is an acyl-ACP thioesterase that edits acetyl primer units. Biochemistry 43 (2004) 9546-9555
    • (2004) Biochemistry , vol.43 , pp. 9546-9555
    • Tang, Y.1    Koppisch, A.T.2    Khosla, C.3
  • 59
    • 19344369476 scopus 로고    scopus 로고
    • Engineered biosynthesis of regioselectively modified aromatic polyketides using bimodular polyketide synthases
    • Tang Y., Lee T.S., and Khosla C. Engineered biosynthesis of regioselectively modified aromatic polyketides using bimodular polyketide synthases. PLoS Biol. 2 (2004) 227-238
    • (2004) PLoS Biol. , vol.2 , pp. 227-238
    • Tang, Y.1    Lee, T.S.2    Khosla, C.3
  • 60
    • 33751579141 scopus 로고    scopus 로고
    • Structural and functional studies on SCO1815: A beta-ketoacyl-acyl carrier protein reductase from Streptomyces coelicolor A3(2)
    • Tang Y., Lee H.Y., Tang Y., Kim C.Y., Mathews I., and Khosla C. Structural and functional studies on SCO1815: A beta-ketoacyl-acyl carrier protein reductase from Streptomyces coelicolor A3(2). Biochemistry 45 (2006) 14085-14093
    • (2006) Biochemistry , vol.45 , pp. 14085-14093
    • Tang, Y.1    Lee, H.Y.2    Tang, Y.3    Kim, C.Y.4    Mathews, I.5    Khosla, C.6
  • 61
    • 0037714370 scopus 로고    scopus 로고
    • Ketosynthases in the initiation and elongation modules of aromatic polyketide synthases have orthogonal acyl carrier protein specificity
    • Tang Y., Lee T.S., Kobayashi S., and Khosla C. Ketosynthases in the initiation and elongation modules of aromatic polyketide synthases have orthogonal acyl carrier protein specificity. Biochemistry 42 (2003) 6588-6595
    • (2003) Biochemistry , vol.42 , pp. 6588-6595
    • Tang, Y.1    Lee, T.S.2    Kobayashi, S.3    Khosla, C.4
  • 62
    • 0142135988 scopus 로고    scopus 로고
    • Polyketide chain length control by chain length factor
    • Tang Y., Tsai S.C., and Khosla C. Polyketide chain length control by chain length factor. J. Am. Chem. Soc. 125 (2003) 12708-12709
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 12708-12709
    • Tang, Y.1    Tsai, S.C.2    Khosla, C.3
  • 63
    • 4444354273 scopus 로고    scopus 로고
    • Structural and functional analysis of tetracenomycin F2 cyclase from Streptomyces glaucescens. A type II polyketide cyclase
    • Thompson T.B., Katayama K., Watanabe K., Hutchinson C.R., and Rayment I. Structural and functional analysis of tetracenomycin F2 cyclase from Streptomyces glaucescens. A type II polyketide cyclase. J. Biol. Chem. 279 (2004) 37956-37963
    • (2004) J. Biol. Chem. , vol.279 , pp. 37956-37963
    • Thompson, T.B.1    Katayama, K.2    Watanabe, K.3    Hutchinson, C.R.4    Rayment, I.5
  • 64
    • 0032947002 scopus 로고    scopus 로고
    • Purification, properties, and characterization of recombinant Streptomyces sp. strain C5 DoxA, a cytochrome P-450 catalyzing multiple steps in doxorubicin biosynthesis
    • Walczak R.J., Dickens M.L., Priestley N.D., and Strohl W.R. Purification, properties, and characterization of recombinant Streptomyces sp. strain C5 DoxA, a cytochrome P-450 catalyzing multiple steps in doxorubicin biosynthesis. J. Bacteriol. 181 (1999) 298-304
    • (1999) J. Bacteriol. , vol.181 , pp. 298-304
    • Walczak, R.J.1    Dickens, M.L.2    Priestley, N.D.3    Strohl, W.R.4
  • 66
    • 0033200340 scopus 로고    scopus 로고
    • Heterologous expression, purification, reconstitution and kinetic analysis of an extended type II polyketide synthase
    • Zawada R.J., and Khosla C. Heterologous expression, purification, reconstitution and kinetic analysis of an extended type II polyketide synthase. Chem. Biol. 6 (1999) 607-615
    • (1999) Chem. Biol. , vol.6 , pp. 607-615
    • Zawada, R.J.1    Khosla, C.2
  • 67
    • 33646109072 scopus 로고    scopus 로고
    • Engineered biosynthesis of a novel amidated polyketide, using the malonamyl-specific initiation module from the oxytetracycline polyketide synthase
    • Zhang W., Ames B.D., Tsai S.C., and Tang Y. Engineered biosynthesis of a novel amidated polyketide, using the malonamyl-specific initiation module from the oxytetracycline polyketide synthase. Appl. Environ. Microbiol. 72 (2006) 2573-2580
    • (2006) Appl. Environ. Microbiol. , vol.72 , pp. 2573-2580
    • Zhang, W.1    Ames, B.D.2    Tsai, S.C.3    Tang, Y.4
  • 68
    • 43249112810 scopus 로고    scopus 로고
    • Identifying the minimal enzymes required for anhydrotetracycline biosynthesis
    • Zhang W., Watanabe K., Cai X., Jung M.E., Tang Y., and Zhan J. Identifying the minimal enzymes required for anhydrotetracycline biosynthesis. J. Am. Chem. Soc. 130 (2008) 6068-6069
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 6068-6069
    • Zhang, W.1    Watanabe, K.2    Cai, X.3    Jung, M.E.4    Tang, Y.5    Zhan, J.6
  • 69
    • 34548474531 scopus 로고    scopus 로고
    • Investigation of early tailoring reactions in the oxytetracycline biosynthetic pathway
    • Zhang W., Watanabe K., Wang C.C., and Tang Y. Investigation of early tailoring reactions in the oxytetracycline biosynthetic pathway. J. Biol. Chem. 282 (2007) 25717-25725
    • (2007) J. Biol. Chem. , vol.282 , pp. 25717-25725
    • Zhang, W.1    Watanabe, K.2    Wang, C.C.3    Tang, Y.4
  • 70
    • 0032921036 scopus 로고    scopus 로고
    • Recombinant polyketide synthesis in Streptomyces: Engineering of improved host strains
    • Ziermann R., and Betlach M.C. Recombinant polyketide synthesis in Streptomyces: Engineering of improved host strains. Biotechniques 26 (1999) 106-110
    • (1999) Biotechniques , vol.26 , pp. 106-110
    • Ziermann, R.1    Betlach, M.C.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.