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Volumn 22, Issue 6, 2015, Pages 745-754

Iterative Mechanism of Macrodiolide Formation in the Anticancer Compound Conglobatin

Author keywords

[No Author keywords available]

Indexed keywords

ANTINEOPLASTIC AGENT; CONGLOBATIN; DIMER; MONOMER; POLYKETIDE SYNTHASE; UNCLASSIFIED DRUG; OXAZOLE DERIVATIVE;

EID: 84935021723     PISSN: 10745521     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.chembiol.2015.05.010     Document Type: Article
Times cited : (61)

References (54)
  • 2
    • 0026645203 scopus 로고
    • Plasmid cloning vectors for the conjugal transfer of DNA from Escherichia coli to Streptomyces spp
    • M. Bierman, R. Logan, K. O'Brien, E.T. Seno, R.N. Rao, and B.E. Schoner Plasmid cloning vectors for the conjugal transfer of DNA from Escherichia coli to Streptomyces spp Gene 116 1992 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
  • 3
    • 0242417573 scopus 로고    scopus 로고
    • Epothilone C macrolactonization and hydrolysis are catalyzed by the isolated thioesterase domain of epothilone polyketide synthase
    • C.N. Boddy, T.L. Scheider, K. Hotta, C.T. Walsh, and C. Khosla Epothilone C macrolactonization and hydrolysis are catalyzed by the isolated thioesterase domain of epothilone polyketide synthase J. Am. Chem. Soc. 125 2003 3428 3429
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 3428-3429
    • Boddy, C.N.1    Scheider, T.L.2    Hotta, K.3    Walsh, C.T.4    Khosla, C.5
  • 4
    • 0028559230 scopus 로고
    • A P-loop-like motif in a widespread ATP pyrophosphatase domain: Implications for the evolution of sequence motifs and enzyme activity
    • P. Bork, and E.V. Koonin A P-loop-like motif in a widespread ATP pyrophosphatase domain: implications for the evolution of sequence motifs and enzyme activity Proteins 20 1994 347 355
    • (1994) Proteins , vol.20 , pp. 347-355
    • Bork, P.1    Koonin, E.V.2
  • 5
    • 0042307438 scopus 로고    scopus 로고
    • Conserved amino acid residues correlating with ketoreductase stereospecificity in modular polyketide synthases
    • P. Caffrey Conserved amino acid residues correlating with ketoreductase stereospecificity in modular polyketide synthases ChemBioChem 4 2003 649 662
    • (2003) ChemBioChem , vol.4 , pp. 649-662
    • Caffrey, P.1
  • 7
    • 84861308350 scopus 로고    scopus 로고
    • YcaO domains utilize ATP to activate amide backbones during peptide cyclodehydrations
    • K.L. Dunbar, J.O. Melby, and D.A. Mitchell YcaO domains utilize ATP to activate amide backbones during peptide cyclodehydrations Nat. Chem. Biol. 8 2012 569 575
    • (2012) Nat. Chem. Biol. , vol.8 , pp. 569-575
    • Dunbar, K.L.1    Melby, J.O.2    Mitchell, D.A.3
  • 9
    • 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
    • N. Gaitatzis, B. Silakowski, B. Kunze, G. Nordsiek, H. Blöcker, G. Höfle, and R. Müller 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
  • 10
    • 79954598176 scopus 로고    scopus 로고
    • Terminal alkene formation by the thioesterase of curacin A biosynthesis: Structure of a decarboxylating thioesterase
    • J.J. Gehret, L. Gu, W.H. Gerwick, P. Wipf, D.H. Sherman, and J.L. Smith Terminal alkene formation by the thioesterase of curacin A biosynthesis: structure of a decarboxylating thioesterase J. Biol. Chem. 286 2011 14445 14454
    • (2011) J. Biol. Chem. , vol.286 , pp. 14445-14454
    • Gehret, J.J.1    Gu, L.2    Gerwick, W.H.3    Wipf, P.4    Sherman, D.H.5    Smith, J.L.6
  • 12
    • 33748785161 scopus 로고    scopus 로고
    • Structural and mechanistic insights into polyketide macrolactonization from polyketide-based affinity labels
    • J.W. Giraldes, D.L. Akey, J.D. Kittendorf, D.H. Sherman, J.L. Smith, and R.A. Fecik Structural and mechanistic insights into polyketide macrolactonization from polyketide-based affinity labels Nat. Chem. Biol. 2 2006 531 536
    • (2006) Nat. Chem. Biol. , vol.2 , pp. 531-536
    • Giraldes, J.W.1    Akey, D.L.2    Kittendorf, J.D.3    Sherman, D.H.4    Smith, J.L.5    Fecik, R.A.6
  • 13
    • 79951846247 scopus 로고    scopus 로고
    • Engineering Streptomyces coelicolor for heterologous expression of secondary metabolite gene clusters
    • J.P. Gomez-Escribano, and M.J. Bibb Engineering Streptomyces coelicolor for heterologous expression of secondary metabolite gene clusters Microb. Biotechnol. 4 2011 207 215
    • (2011) Microb. Biotechnol. , vol.4 , pp. 207-215
    • Gomez-Escribano, J.P.1    Bibb, M.J.2
  • 14
    • 0028841535 scopus 로고
    • Divergent sequence motifs correlated with the substrate specificity of (methyl)malonyl-CoA:acyl carrier protein transacylase domains in modular polyketide synthases
    • S.F. Haydock, J.F. Aparicio, I. Molnár, T. Schwecke, L.E. Khaw, A. König, A.F. Marsden, I.S. Galloway, J. Staunton, and P.F. Leadlay Divergent sequence motifs correlated with the substrate specificity of (methyl)malonyl-CoA:acyl carrier protein transacylase domains in modular polyketide synthases FEBS Lett. 374 1995 246 248
    • (1995) FEBS Lett. , vol.374 , pp. 246-248
    • Haydock, S.F.1    Aparicio, J.F.2    Molnár, I.3    Schwecke, T.4    Khaw, L.E.5    König, A.6    Marsden, A.F.7    Galloway, I.S.8    Staunton, J.9    Leadlay, P.F.10
  • 15
    • 0346968190 scopus 로고    scopus 로고
    • Iteration as programmed event during polyketide assembly; Molecular analysis of the aureothin biosynthesis gene cluster
    • J. He, and C. Hertweck Iteration as programmed event during polyketide assembly; molecular analysis of the aureothin biosynthesis gene cluster Chem. Biol. 10 2003 1225 1232
    • (2003) Chem. Biol. , vol.10 , pp. 1225-1232
    • He, J.1    Hertweck, C.2
  • 16
    • 84986637292 scopus 로고
    • Sekundärstoffe aus dem chemischen Screening, 16. Inthomycine, neue Oxazol-triene aus Streptomyces sp
    • T. Henkel, and A. Zeeck Sekundärstoffe aus dem chemischen Screening, 16. Inthomycine, neue Oxazol-triene aus Streptomyces sp Liebigs Ann. Chem. 1991 1991 367 373
    • (1991) Liebigs Ann. Chem. , vol.1991 , pp. 367-373
    • Henkel, T.1    Zeeck, A.2
  • 17
    • 84957104073 scopus 로고    scopus 로고
    • Polyketide synthase and non-ribosomal peptide synthetase thioesterase selectivity: Logic gate or a victim of fate?
    • [Epub ahead of print]
    • M.E. Horsman, T.P. Hari, and C.N. Boddy Polyketide synthase and non-ribosomal peptide synthetase thioesterase selectivity: logic gate or a victim of fate? Nat. Prod. Rep. 2015 [Epub ahead of print]
    • (2015) Nat. Prod. Rep.
    • Horsman, M.E.1    Hari, T.P.2    Boddy, C.N.3
  • 18
    • 33846296304 scopus 로고    scopus 로고
    • The iterative gramicidin S thioesterase catalyzes peptide ligation and cyclization
    • K.M. Hoyer, C. Mahlert, and M.A. Marahiel The iterative gramicidin S thioesterase catalyzes peptide ligation and cyclization Chem. Biol. 14 2007 13 22
    • (2007) Chem. Biol. , vol.14 , pp. 13-22
    • Hoyer, K.M.1    Mahlert, C.2    Marahiel, M.A.3
  • 19
    • 84902044721 scopus 로고    scopus 로고
    • FW-04-806 inhibits proliferation and induces apoptosis in human breast cancer cells by binding to N-terminus of Hsp90 and disrupting Hsp90-Cdc37 complex formation
    • W. Huang, M. Ye, L.R. Zhang, Q.D. Wu, M. Zhang, J.H. Xu, and W. Zheng FW-04-806 inhibits proliferation and induces apoptosis in human breast cancer cells by binding to N-terminus of Hsp90 and disrupting Hsp90-Cdc37 complex formation Mol. Cancer 13 2014 150 162
    • (2014) Mol. Cancer , vol.13 , pp. 150-162
    • Huang, W.1    Ye, M.2    Zhang, L.R.3    Wu, Q.D.4    Zhang, M.5    Xu, J.H.6    Zheng, W.7
  • 20
    • 84919480571 scopus 로고    scopus 로고
    • Novel Hsp90 inhibitor FW-04-806 displays potent antitumor effects in HER2-positive breast cancer cells as a single agent or in combination with lapatinib
    • W. Huang, Q. Wu, M. Zhang, Y. Kong, P. Cao, W. Zheng, J. Xu, and M. Ye Novel Hsp90 inhibitor FW-04-806 displays potent antitumor effects in HER2-positive breast cancer cells as a single agent or in combination with lapatinib Cancer Lett. 356 2015 862 871
    • (2015) Cancer Lett. , vol.356 , pp. 862-871
    • Huang, W.1    Wu, Q.2    Zhang, M.3    Kong, Y.4    Cao, P.5    Zheng, W.6    Xu, J.7    Ye, M.8
  • 21
    • 34547945950 scopus 로고    scopus 로고
    • A tylosin ketoreductase reveals how chirality is determined in polyketides
    • A.T. Keatinge-Clay A tylosin ketoreductase reveals how chirality is determined in polyketides Chem. Biol. 14 2007 898 908
    • (2007) Chem. Biol. , vol.14 , pp. 898-908
    • Keatinge-Clay, A.T.1
  • 22
    • 63849246525 scopus 로고    scopus 로고
    • Protein structure prediction on the web: A case study using the Phyre server
    • L.A. Kelley, and M.J.E. Sternberg Protein structure prediction on the web: a case study using the Phyre server Nat. Protoc. 4 2009 363 371
    • (2009) Nat. Protoc. , vol.4 , pp. 363-371
    • Kelley, L.A.1    Sternberg, M.J.E.2
  • 24
    • 77956942908 scopus 로고    scopus 로고
    • Mutagenesis of a modular polyketide synthase enoylreductase domain reveals insights into catalysis and stereospecificity
    • D.H. Kwan, and P.F. Leadlay Mutagenesis of a modular polyketide synthase enoylreductase domain reveals insights into catalysis and stereospecificity ACS Chem. Biol. 59 2010 829 838
    • (2010) ACS Chem. Biol. , vol.59 , pp. 829-838
    • Kwan, D.H.1    Leadlay, P.F.2
  • 26
    • 84904662326 scopus 로고    scopus 로고
    • Biosynthesis of crocacin involves an unusual hydrolytic release domain showing similarity to condensation domains
    • S. Müller, S. Rachid, T. Hoffmann, F. Surup, C. Volz, N. Zaburannyi, and R. Müller Biosynthesis of crocacin involves an unusual hydrolytic release domain showing similarity to condensation domains Chem. Biol. 21 2014 855 865
    • (2014) Chem. Biol. , vol.21 , pp. 855-865
    • Müller, S.1    Rachid, S.2    Hoffmann, T.3    Surup, F.4    Volz, C.5    Zaburannyi, N.6    Müller, R.7
  • 28
    • 0344099408 scopus 로고    scopus 로고
    • Evidence from engineered gene fusions for the repeated use of a module in a modular polyketide synthase
    • C. Olano, B. Wilkinson, S.J. Moss, A.F. Braña, C. Méndez, P.F. Leadlay, and J.A. Salas Evidence from engineered gene fusions for the repeated use of a module in a modular polyketide synthase Chem. Commun. 2003 2003 2780 2782
    • (2003) Chem. Commun. , vol.2003 , pp. 2780-2782
    • Olano, C.1    Wilkinson, B.2    Moss, S.J.3    Braña, A.F.4    Méndez, C.5    Leadlay, P.F.6    Salas, J.A.7
  • 29
    • 0025043113 scopus 로고
    • Phthoxazolin, a specific inhibitor of cellulose biosynthesis, produced by a strain of Streptomyces sp
    • S. Omura, Y. Tanaka, I. Kanaya, M. Shinose, and Y. Takahashi Phthoxazolin, a specific inhibitor of cellulose biosynthesis, produced by a strain of Streptomyces sp J. Antibiot. 43 1990 1034 1036
    • (1990) J. Antibiot. , vol.43 , pp. 1034-1036
    • Omura, S.1    Tanaka, Y.2    Kanaya, I.3    Shinose, M.4    Takahashi, Y.5
  • 30
    • 33846294808 scopus 로고    scopus 로고
    • A gene cluster encoding rhizoxin biosynthesis in "burkholderia rhizoxina", the bacterial symbiont of the fungus Rhizopus microsporus
    • L.P. Partida-Martinez, and C. Hertweck A gene cluster encoding rhizoxin biosynthesis in "Burkholderia rhizoxina", the bacterial symbiont of the fungus Rhizopus microsporus ChemBioChem 8 2007 41 45
    • (2007) ChemBioChem , vol.8 , pp. 41-45
    • Partida-Martinez, L.P.1    Hertweck, C.2
  • 31
    • 84860629118 scopus 로고    scopus 로고
    • 6-deoxyerythronolide B synthase thioesterase-catalyzed macrocyclization is highly stereoselective
    • A. Pinto, M. Wang, M. Horsman, and C.N. Boddy 6-deoxyerythronolide B synthase thioesterase-catalyzed macrocyclization is highly stereoselective Org. Lett. 14 2012 2278 2281
    • (2012) Org. Lett. , vol.14 , pp. 2278-2281
    • Pinto, A.1    Wang, M.2    Horsman, M.3    Boddy, C.N.4
  • 32
    • 84856560505 scopus 로고    scopus 로고
    • Discovery of the rhizopodin biosynthetic gene cluster in Stigmatella aurantiaca Sg a15 by genome mining
    • D. Pistorius, and R. Müller Discovery of the rhizopodin biosynthetic gene cluster in Stigmatella aurantiaca Sg a15 by genome mining ChemBioChem 13 2012 416 426
    • (2012) ChemBioChem , vol.13 , pp. 416-426
    • Pistorius, D.1    Müller, R.2
  • 34
    • 61349111371 scopus 로고    scopus 로고
    • TioS T-TE - A prototypical thioesterase responsible for cyclodimerization of the quinoline- and quinoxaline-type class of chromodepsipeptides
    • L. Robbel, K.M. Hoyer, and M.A. Marahiel TioS T-TE - a prototypical thioesterase responsible for cyclodimerization of the quinoline- and quinoxaline-type class of chromodepsipeptides FEBS J. 276 2009 1641 1653
    • (2009) FEBS J. , vol.276 , pp. 1641-1653
    • Robbel, L.1    Hoyer, K.M.2    Marahiel, M.A.3
  • 39
    • 0042242569 scopus 로고    scopus 로고
    • Oxidase domains in epothilone and bleomycin biosynthesis: Thiazoline to thiazole oxidation during chain elongation
    • T.L. Schneider, B. Shen, and C.T. Walsh Oxidase domains in epothilone and bleomycin biosynthesis: thiazoline to thiazole oxidation during chain elongation Biochemistry 42 2003 9722 9730
    • (2003) Biochemistry , vol.42 , pp. 9722-9730
    • Schneider, T.L.1    Shen, B.2    Walsh, C.T.3
  • 40
    • 33745017396 scopus 로고    scopus 로고
    • Formylation domain: An essential modifying enzyme for the nonribosomal biosynthesis of linear gramicidin
    • G. Schönafinger, N. Schracke, U. Linne, and M.A. Marahiel Formylation domain: an essential modifying enzyme for the nonribosomal biosynthesis of linear gramicidin J. Am. Chem. Soc. 128 2006 7406 7407
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 7406-7407
    • Schönafinger, G.1    Schracke, N.2    Linne, U.3    Marahiel, M.A.4
  • 41
    • 0003513025 scopus 로고
    • Synthesis and determination of the absolute configuration of the macrodiolide (+)-conglobatin
    • C. Schregenberger, and D. Seebach Synthesis and determination of the absolute configuration of the macrodiolide (+)-conglobatin Tetrahedron Lett. 25 1984 5881 5884
    • (1984) Tetrahedron Lett. , vol.25 , pp. 5881-5884
    • Schregenberger, C.1    Seebach, D.2
  • 42
    • 0023058912 scopus 로고
    • Purification and characterization of aminoimidazole ribonucleotide synthetase from Escherichia coli
    • J.L. Schrimsher, F.J. Schenmdel, J. Stubbe, and J.M. Smith Purification and characterization of aminoimidazole ribonucleotide synthetase from Escherichia coli Biochemistry 25 1986 4366 4371
    • (1986) Biochemistry , vol.25 , pp. 4366-4371
    • Schrimsher, J.L.1    Schenmdel, F.J.2    Stubbe, J.3    Smith, J.M.4
  • 43
    • 0033150199 scopus 로고    scopus 로고
    • Assembly line enzymology by multimodular nonribosomal peptide synthetases: The thioesterase domain of E. Coli EntF catalyzes both elongation and cyclolactonization
    • C.A. Shaw-Reid, N.L. Kelleher, H.C. Losey, A.M. Gehring, C. Berg, and C.T. Walsh Assembly line enzymology by multimodular nonribosomal peptide synthetases: the thioesterase domain of E. coli EntF catalyzes both elongation and cyclolactonization Chem. Biol. 6 1999 385 400
    • (1999) Chem. Biol. , vol.6 , pp. 385-400
    • Shaw-Reid, C.A.1    Kelleher, N.L.2    Losey, H.C.3    Gehring, A.M.4    Berg, C.5    Walsh, C.T.6
  • 45
    • 0027234550 scopus 로고
    • Phthoxazolin A, a specific inhibitor of cellulose biosynthesis from microbial origin i
    • Y. Tanaka, I. Kanaya, K. Shiomi, H. Tanaka, and S. Omura Phthoxazolin A, a specific inhibitor of cellulose biosynthesis from microbial origin I J. Antibiot. 46 1993 1214 1218
    • (1993) J. Antibiot. , vol.46 , pp. 1214-1218
    • Tanaka, Y.1    Kanaya, I.2    Shiomi, K.3    Tanaka, H.4    Omura, S.5
  • 46
    • 44049097046 scopus 로고    scopus 로고
    • Covalent linkage mediates communication between ACP and TE domains in modular polyketide synthases
    • L. Tran, M. Tosin, J.B. Spencer, P.F. Leadlay, and K.J. Weissman Covalent linkage mediates communication between ACP and TE domains in modular polyketide synthases ChemBioChem 9 2008 905 915
    • (2008) ChemBioChem , vol.9 , pp. 905-915
    • Tran, L.1    Tosin, M.2    Spencer, J.B.3    Leadlay, P.F.4    Weissman, K.J.5
  • 47
    • 0037159232 scopus 로고    scopus 로고
    • Insights into channel architecture and substrate specificity from crystal structures of two macrocycle-forming thioesterases of modular polyketide synthases
    • S.-C. Tsai, H. Lu, D.E. Cane, C. Khosla, and R.M. Stroud Insights into channel architecture and substrate specificity from crystal structures of two macrocycle-forming thioesterases of modular polyketide synthases Biochemistry 41 2002 12598 12606
    • (2002) Biochemistry , vol.41 , pp. 12598-12606
    • Tsai, S.-C.1    Lu, H.2    Cane, D.E.3    Khosla, C.4    Stroud, R.M.5
  • 48
    • 67650066485 scopus 로고    scopus 로고
    • A thioesterase from an iterative fungal polyketide synthase shows macrocyclization and cross coupling activity and may play a role in controlling iterative cycling through product offloading
    • M. Wang, H. Zhou, M. Wirz, Y. Tang, and C.N. Boddy A thioesterase from an iterative fungal polyketide synthase shows macrocyclization and cross coupling activity and may play a role in controlling iterative cycling through product offloading Biochemistry 48 2009 6288 6290
    • (2009) Biochemistry , vol.48 , pp. 6288-6290
    • Wang, M.1    Zhou, H.2    Wirz, M.3    Tang, Y.4    Boddy, C.N.5
  • 49
    • 0018620143 scopus 로고
    • Conglobatin, a novel macrolide dilactone from Streptomyces conglobatus ATCC 31005
    • J.W. Westley, C.M. Liu, R.H. Evans, and J.F. Blount Conglobatin, a novel macrolide dilactone from Streptomyces conglobatus ATCC 31005 J. Antibiot. 32 1979 874 877
    • (1979) J. Antibiot. , vol.32 , pp. 874-877
    • Westley, J.W.1    Liu, C.M.2    Evans, R.H.3    Blount, J.F.4
  • 51
    • 0037466331 scopus 로고    scopus 로고
    • Computational approach for prediction of domain organization and substrate specificity of modular polyketide synthases
    • G. Yadav, R.S. Gokhale, and D. Mohanty Computational approach for prediction of domain organization and substrate specificity of modular polyketide synthases J. Mol. Biol. 328 2003 335 363
    • (2003) J. Mol. Biol. , vol.328 , pp. 335-363
    • Yadav, G.1    Gokhale, R.S.2    Mohanty, D.3
  • 52
    • 84923566436 scopus 로고    scopus 로고
    • Production of the antibiotic FR-008/candicidin in Streptomyces sp. FR-008 is co-regulated by two regulators, FscRI and FscRIV, from different transcription factor families
    • P. Zhang, Z. Zhao, H. Li, X.L. Chen, Z. Deng, L. Bai, and X. Pang Production of the antibiotic FR-008/candicidin in Streptomyces sp. FR-008 is co-regulated by two regulators, FscRI and FscRIV, from different transcription factor families Microbiology 161 2015 539 552
    • (2015) Microbiology , vol.161 , pp. 539-552
    • Zhang, P.1    Zhao, Z.2    Li, H.3    Chen, X.L.4    Deng, Z.5    Bai, L.6    Pang, X.7
  • 53
    • 77953799129 scopus 로고    scopus 로고
    • Oxazolomycin biosynthesis in Streptomyces albus JA3453 featuring an "acyltransferase-less" type i polyketide synthase that incorporates two distinct extender units
    • C. Zhao, J.M. Coughlin, J. Ju, D. Zhu, E. Wendt-Pienkowski, X. Zhou, Z. Wang, B. Shen, and Z. Deng Oxazolomycin biosynthesis in Streptomyces albus JA3453 featuring an "acyltransferase-less" type I polyketide synthase that incorporates two distinct extender units J. Biol. Chem. 285 2010 20097 20108
    • (2010) J. Biol. Chem. , vol.285 , pp. 20097-20108
    • Zhao, C.1    Coughlin, J.M.2    Ju, J.3    Zhu, D.4    Wendt-Pienkowski, E.5    Zhou, X.6    Wang, Z.7    Shen, B.8    Deng, Z.9


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