메뉴 건너뛰기




Volumn 18, Issue 6, 2008, Pages 1101-1108

Characterization of tailoring genes involved in the modification of geldanamycin polyketide in Streptomyces hygroscopicus JCM4427

Author keywords

Biosynthesis; Geldanamycin; Polyketide; Streptomyces

Indexed keywords

2,4 DIHYDROGELDANAMYCIN; BACTERIAL PROTEIN; GELDANAMYCIN; POLYKETIDE SYNTHASE; PROTEIN GEL1; PROTEIN GEL16; PROTEIN GEL7; PROTEIN GEL8; UNCLASSIFIED DRUG; BENZOQUINONE DERIVATIVE; MACROCYCLIC LACTAM;

EID: 53149091352     PISSN: 10177825     EISSN: 17388872     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (38)

References (27)
  • 1
    • 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., L. Tang, Y. J. Yoon, S. Ning, R. Muller, T. W. Yu, et al. 1998. Biosynthesis of the ansamycin antibiotic rifamycin: Deductions from the molecular analysis of the rif biosynthetic gene cluster of Amycolatopsis mediterranei S699. Chem. Biol. 5: 69-79.
    • (1998) Chem. Biol , vol.5 , pp. 69-79
    • August, P.R.1    Tang, L.2    Yoon, Y.J.3    Ning, S.4    Muller, R.5    Yu, T.W.6
  • 2
    • 0020836369 scopus 로고
    • 3-Amino-5-hydroxybenzoic acid in antibiotic biosynthesis. VI. Directed biosynthesis studies with ansamycin antibiotics
    • Becker, A. M., A. J. Herlt, G. L. Hilton, J. J. Kibby, and R. W. Rickards. 1983. 3-Amino-5-hydroxybenzoic acid in antibiotic biosynthesis. VI. Directed biosynthesis studies with ansamycin antibiotics. J. Antibiot. 36: 1323-1328.
    • (1983) J. Antibiot , vol.36 , pp. 1323-1328
    • Becker, A.M.1    Herlt, A.J.2    Hilton, G.L.3    Kibby, J.J.4    Rickards, R.W.5
  • 3
    • 0028079724 scopus 로고
    • The mRNA for the 23S rRNA methylase encoded by the ermE gene of Saccharopolyspora erythraea is translated in the absence of a conventional ribosome-binding site
    • Bibb, M. J., J. White, J. M. Ward, and G. R. Janssen. 1994. The mRNA for the 23S rRNA methylase encoded by the ermE gene of Saccharopolyspora erythraea is translated in the absence of a conventional ribosome-binding site. Mol. Microbiol. 14: 533-545.
    • (1994) Mol. Microbiol , vol.14 , pp. 533-545
    • Bibb, M.J.1    White, J.2    Ward, J.M.3    Janssen, G.R.4
  • 4
    • 0026645203 scopus 로고
    • Plasmid cloning vectors for the conjugal transfer of DNA from Escherichia coli to Streptomyces spp
    • Bierman, M., R. Logan, K. O'Brien, E. T. Seno, R. N. Rao, and B. E. Schoner. 1992. Plasmid cloning vectors for the conjugal transfer of DNA from Escherichia coli to Streptomyces spp. Gene 116: 43-49.
    • (1992) Gene , vol.116 , pp. 43-49
    • Bierman, M.1    Logan, R.2    O'Brien, K.3    Seno, E.T.4    Rao, R.N.5    Schoner, B.E.6
  • 5
    • 0029586252 scopus 로고
    • Structure of cytochrome P450eryF involved in erythromycin biosynthesis
    • Cupp-Vickery, J. R. and T. L. Poulos. 1995. Structure of cytochrome P450eryF involved in erythromycin biosynthesis. Nat. Struct. Biol. 2: 144-153.
    • (1995) Nat. Struct. Biol , vol.2 , pp. 144-153
    • Cupp-Vickery, J.R.1    Poulos, T.L.2
  • 6
    • 0025864623 scopus 로고    scopus 로고
    • Denis, F. and R. Brzezinski. 1991. An improved aminoglycoside resistance gene cassette for use in Gram-negative bacteria and Streptomyces. FEMS Microbiol. Lett. 81: 261-264.
    • Denis, F. and R. Brzezinski. 1991. An improved aminoglycoside resistance gene cassette for use in Gram-negative bacteria and Streptomyces. FEMS Microbiol. Lett. 81: 261-264.
  • 7
    • 0032524753 scopus 로고    scopus 로고
    • The crystal structure of phenol hydroxylase in complex with FAD and phenol provides evidence for a concerted conformational change in the enzyme and its cofactor during catalysis
    • Enroth, C., H. Neujahr, G. Schneider, and Y. Lindqvist. 1998. The crystal structure of phenol hydroxylase in complex with FAD and phenol provides evidence for a concerted conformational change in the enzyme and its cofactor during catalysis. Structure 6: 605-617.
    • (1998) Structure , vol.6 , pp. 605-617
    • Enroth, C.1    Neujahr, H.2    Schneider, G.3    Lindqvist, Y.4
  • 8
    • 0030716522 scopus 로고    scopus 로고
    • Identification of a novel conserved sequence motif in flavoprotein hydroxylases with a putative dual function in FAD/NAD(P)H binding
    • Eppink, M. H., H. A. Schreuder, and W. J. Van Berkel. 1997. Identification of a novel conserved sequence motif in flavoprotein hydroxylases with a putative dual function in FAD/NAD(P)H binding. Protein Sci. 6: 2454-2458.
    • (1997) Protein Sci , vol.6 , pp. 2454-2458
    • Eppink, M.H.1    Schreuder, H.A.2    Van Berkel, W.J.3
  • 9
    • 77349086625 scopus 로고    scopus 로고
    • Characterization of NovP and NovN: Completion of novobiocin biosynthesis by sequential tailoring of the noviosyl ring
    • Freel Meyers, C. L., M. Oberthur, H. Xu, L. Heide, D. Kahne, and C. T. Walsh. 2004. Characterization of NovP and NovN: Completion of novobiocin biosynthesis by sequential tailoring of the noviosyl ring. Angew Chem. Int. Ed. Engl. 43: 67-70.
    • (2004) Angew Chem. Int. Ed. Engl , vol.43 , pp. 67-70
    • Freel Meyers, C.L.1    Oberthur, M.2    Xu, H.3    Heide, L.4    Kahne, D.5    Walsh, C.T.6
  • 10
    • 0031918678 scopus 로고    scopus 로고
    • Cytochrome P450-dependent desaturation of lauric acid: Isoform selectivity and mechanism of formation of 11-dodecenoic acid
    • Guan. X., M. B. Fisher, D. H. Lang, Y.-M. Zheng, D. R. Koop, and A. E. Rettie. 1998. Cytochrome P450-dependent desaturation of lauric acid: Isoform selectivity and mechanism of formation of 11-dodecenoic acid. Chem. Biol. Interact. 110: 103-121.
    • (1998) Chem. Biol. Interact , vol.110 , pp. 103-121
    • Guan, X.1    Fisher, M.B.2    Lang, D.H.3    Zheng, Y.-M.4    Koop, D.R.5    Rettie, A.E.6
  • 11
    • 0034973773 scopus 로고    scopus 로고
    • Common and uncommon cytochrome P450 reactions related to metabolism and chemical toxicity
    • Guengerich, F. P. 2001. Common and uncommon cytochrome P450 reactions related to metabolism and chemical toxicity. Chem. Res. Toxicol. 14: 611-650.
    • (2001) Chem. Res. Toxicol , vol.14 , pp. 611-650
    • Guengerich, F.P.1
  • 13
    • 4544307538 scopus 로고    scopus 로고
    • Inactivation of the carbamoyltransferase gene refines post-polyketide synthase modification steps in the biosynthesis of the antitumor agent geldanamycin
    • Hong, Y.-S., D. Lee, W. Kim, J. K. Jeong, C. G. Kim, J. K. Sohng, J. H. Lee, S. G. Paik, and J. J. Lee. 2004. Inactivation of the carbamoyltransferase gene refines post-polyketide synthase modification steps in the biosynthesis of the antitumor agent geldanamycin. J. Am. Chem. Soc. 126: 11142-11143.
    • (2004) J. Am. Chem. Soc , vol.126 , pp. 11142-11143
    • Hong, Y.-S.1    Lee, D.2    Kim, W.3    Jeong, J.K.4    Kim, C.G.5    Sohng, J.K.6    Lee, J.H.7    Paik, S.G.8    Lee, J.J.9
  • 15
    • 0016393109 scopus 로고
    • Geldanamycin biosynthesis and carbon magnetic resonance
    • Johnson, R. D., A. Haber, and K. L. Rinehart Jr. 1974. Geldanamycin biosynthesis and carbon magnetic resonance. J. Am. Chem. Soc. 96: 3316-3317.
    • (1974) J. Am. Chem. Soc , vol.96 , pp. 3316-3317
    • Johnson, R.D.1    Haber, A.2    Rinehart Jr., K.L.3
  • 16
    • 34250194296 scopus 로고    scopus 로고
    • Cloning, sequencing, and characterization of the pradimicin biosynthetic genes cluster of Actinomadura hibisca
    • Kim, B. C., J. M. Lee., J. S. Ahn, and B. S. Kim. 2007. Cloning, sequencing, and characterization of the pradimicin biosynthetic genes cluster of Actinomadura hibisca. J. Microbiol. Biotechnol. 17: 830-839.
    • (2007) J. Microbiol. Biotechnol , vol.17 , pp. 830-839
    • Kim, B.C.1    Lee, J.M.2    Ahn, J.S.3    Kim, B.S.4
  • 17
    • 33846480486 scopus 로고    scopus 로고
    • Analysis of a prodigiocin biosynthetic gene cluster from the marine bacterium Hahella chejuensis KCTC 2396
    • Kim, D. Y., Y. K. Park, J. S. Lee, J. H. Kim, H. Y. Jeong, B. S. Kim, and C. H. Lee. 2006. Analysis of a prodigiocin biosynthetic gene cluster from the marine bacterium Hahella chejuensis KCTC 2396. J. Microbiol. Biotechnol. 16: 1912-1918.
    • (2006) J. Microbiol. Biotechnol , vol.16 , pp. 1912-1918
    • Kim, D.Y.1    Park, Y.K.2    Lee, J.S.3    Kim, J.H.4    Jeong, H.Y.5    Kim, B.S.6    Lee, C.H.7
  • 18
    • 32344449220 scopus 로고    scopus 로고
    • Biosynthesis of the heat-shock protein 90 inhibitor geldanamycin: New insight into the formation of the benzoquinone moiety
    • Lee, D., K. Lee, X. F. Cai, N. T. Dat, S. K. Boovanahalli, M. Lee, et al. 2006. Biosynthesis of the heat-shock protein 90 inhibitor geldanamycin: New insight into the formation of the benzoquinone moiety. ChemBioChem 7: 246-248.
    • (2006) ChemBioChem , vol.7 , pp. 246-248
    • Lee, D.1    Lee, K.2    Cai, X.F.3    Dat, N.T.4    Boovanahalli, S.K.5    Lee, M.6
  • 19
    • 33745624271 scopus 로고    scopus 로고
    • Hydroxylation of indole by PikC cytochrome P450 from Streptomyces venezuelae and engineering its catalytic activity by site-directed mutagenesis
    • Lee, S. K., J. W. Park, S. R. Park, J. S. Ahn, C. Y. Choi, and Y. J. Yoon. 2006. Hydroxylation of indole by PikC cytochrome P450 from Streptomyces venezuelae and engineering its catalytic activity by site-directed mutagenesis. J. Microbiol. Biotechnol. 16: 974-978.
    • (2006) J. Microbiol. Biotechnol , vol.16 , pp. 974-978
    • Lee, S.K.1    Park, J.W.2    Park, S.R.3    Ahn, J.S.4    Choi, C.Y.5    Yoon, Y.J.6
  • 20
    • 14344264703 scopus 로고    scopus 로고
    • Heat-shock protein 90 inhibitors as novel cancer chemotherapeutics - an update
    • Neckers, L. and K. Neckers. 2005. Heat-shock protein 90 inhibitors as novel cancer chemotherapeutics - an update. Expert Opin. Emerg. Drugs 10: 137-149.
    • (2005) Expert Opin. Emerg. Drugs , vol.10 , pp. 137-149
    • Neckers, L.1    Neckers, K.2
  • 21
    • 33646674860 scopus 로고    scopus 로고
    • Heterologous expression of novel cytochrome P450 hydroxylase genes from Sebekia benihana
    • Park, N. S., H. J. Park, K. B. Han, and E. S. Kim. 2006. Heterologous expression of novel cytochrome P450 hydroxylase genes from Sebekia benihana. J. Microbiol. Biotechnol. 16: 295-298
    • (2006) J. Microbiol. Biotechnol , vol.16 , pp. 295-298
    • Park, N.S.1    Park, H.J.2    Han, K.B.3    Kim, E.S.4
  • 22
    • 0031444238 scopus 로고    scopus 로고
    • Identification and structural characterization of the ATP/ADP-binding site in the Hsp90 molecular chaperone
    • Prodromou, C., S. M. Roe, R. O'Brien, J. E. Ladbury, P. W. Piper, and L. H. Pearl. 1997. Identification and structural characterization of the ATP/ADP-binding site in the Hsp90 molecular chaperone. Cell 90: 65-75.
    • (1997) Cell , vol.90 , pp. 65-75
    • Prodromou, C.1    Roe, S.M.2    O'Brien, R.3    Ladbury, J.E.4    Piper, P.W.5    Pearl, L.H.6
  • 23
    • 23744448109 scopus 로고    scopus 로고
    • Insights into the biosynthesis of the benzoquinone ansamycins geldanamycin and herbimycin, obtained by gene sequencing and disruption
    • Rascher, A., Z. Hu, G. O. Buchanan, R. Reid, and C. R. Hutchinson. 2005. Insights into the biosynthesis of the benzoquinone ansamycins geldanamycin and herbimycin, obtained by gene sequencing and disruption. Appl. Environ. Microbiol. 71: 4862-4871.
    • (2005) Appl. Environ. Microbiol , vol.71 , pp. 4862-4871
    • Rascher, A.1    Hu, Z.2    Buchanan, G.O.3    Reid, R.4    Hutchinson, C.R.5
  • 26
    • 23844557104 scopus 로고    scopus 로고
    • Identification of tailoring genes involved in the modification of the polyketide backbone of rifamycin B by Amycolatopsis mediterranei S699
    • Xu, J., E. Wan, C. J. Kim, H. G. Floss, and T. Mahmud. 2005. Identification of tailoring genes involved in the modification of the polyketide backbone of rifamycin B by Amycolatopsis mediterranei S699. Microbiology 151: 2515-2528.
    • (2005) Microbiology , vol.151 , pp. 2515-2528
    • Xu, J.1    Wan, E.2    Kim, C.J.3    Floss, H.G.4    Mahmud, T.5
  • 27
    • 0037062404 scopus 로고    scopus 로고
    • The biosynthetic gene cluster of the maytansinoid antitumor agent ansamitocin from Actinosynnema pretiosum
    • Yu, T. W., L. Bai, D. Clade, D. Hoffmann, S. Toelzer, K. Q. Trinh, et al. 2002. The biosynthetic gene cluster of the maytansinoid antitumor agent ansamitocin from Actinosynnema pretiosum. Proc. Natl. Acad. Sci. USA 99: 7968-7973.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 7968-7973
    • Yu, T.W.1    Bai, L.2    Clade, D.3    Hoffmann, D.4    Toelzer, S.5    Trinh, K.Q.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.