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Volumn 17, Issue 3, 2010, Pages 296-309

Discovery of 23 Natural Tubulysins from Angiococcus disciformis An d48 and Cystobacter SBCb004

Author keywords

CHEMBIO

Indexed keywords

BACTERIAL DNA; DNA; OLIGOPEPTIDE; PIPECOLIC ACID; PIPECOLIC ACID DERIVATIVE;

EID: 77949558085     PISSN: 10745521     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.chembiol.2010.01.016     Document Type: Article
Times cited : (55)

References (50)
  • 4
    • 60549108795 scopus 로고    scopus 로고
    • Total synthesis and biological evaluation of tubulysin U, tubulysin V, and their analogues
    • Balasubramanian R., Raghavan B., Begaye A., Sackett D.L., and Fecik R.A. Total synthesis and biological evaluation of tubulysin U, tubulysin V, and their analogues. J. Med. Chem. 52 (2009) 238-240
    • (2009) J. Med. Chem. , vol.52 , pp. 238-240
    • Balasubramanian, R.1    Raghavan, B.2    Begaye, A.3    Sackett, D.L.4    Fecik, R.A.5
  • 5
    • 27744519951 scopus 로고    scopus 로고
    • Generation of D-amino acid residues in assembly of arthrofactin by dual condensation/epimerization domains
    • Balibar C.J., Vaillancourt F.H., and Walsh C.T. Generation of D-amino acid residues in assembly of arthrofactin by dual condensation/epimerization domains. Chem. Biol. 12 (2005) 1189-1200
    • (2005) Chem. Biol. , vol.12 , pp. 1189-1200
    • Balibar, C.J.1    Vaillancourt, F.H.2    Walsh, C.T.3
  • 6
    • 1642365547 scopus 로고    scopus 로고
    • Patatin-like proteins: a new family of lipolytic enzymes present in bacteria?
    • Banerji S., and Flieger A. Patatin-like proteins: a new family of lipolytic enzymes present in bacteria?. Microbiology 150 (2004) 522-525
    • (2004) Microbiology , vol.150 , pp. 522-525
    • Banerji, S.1    Flieger, A.2
  • 7
    • 33745018355 scopus 로고    scopus 로고
    • Analysis of myxobacterial secondary metabolism goes molecular
    • Bode H.B., and Müller R. Analysis of myxobacterial secondary metabolism goes molecular. J. Ind. Microbiol. Biotechnol. 33 (2006) 577-588
    • (2006) J. Ind. Microbiol. Biotechnol. , vol.33 , pp. 577-588
    • Bode, H.B.1    Müller, R.2
  • 8
    • 25144520542 scopus 로고    scopus 로고
    • The biosynthetic genes for disorazoles, potent cytotoxic compounds that disrupt microtubule formation
    • Carvalho R., Reid R., Viswanathan N., Gramajo H., and Julien B. The biosynthetic genes for disorazoles, potent cytotoxic compounds that disrupt microtubule formation. Gene 359 (2005) 91-98
    • (2005) Gene , vol.359 , pp. 91-98
    • Carvalho, R.1    Reid, R.2    Viswanathan, N.3    Gramajo, H.4    Julien, B.5
  • 9
    • 0028807689 scopus 로고
    • Multienzymatic non ribosomal peptide biosynthesis: identification of the functional domains catalysing peptide elongation and epimerisation
    • De Crecy-Lagard V., Marliere P., and Saurin W. Multienzymatic non ribosomal peptide biosynthesis: identification of the functional domains catalysing peptide elongation and epimerisation. C. R. Acad. Sci. III 318 (1995) 927-936
    • (1995) C. R. Acad. Sci. III , vol.318 , pp. 927-936
    • De Crecy-Lagard, V.1    Marliere, P.2    Saurin, W.3
  • 10
    • 15444370602 scopus 로고    scopus 로고
    • Myxobacterial epothilones and tubulysins as promising anticancer agents
    • Dömling A., and Richter W. Myxobacterial epothilones and tubulysins as promising anticancer agents. Mol. Divers. 9 (2005) 141-147
    • (2005) Mol. Divers. , vol.9 , pp. 141-147
    • Dömling, A.1    Richter, W.2
  • 12
    • 51149089478 scopus 로고    scopus 로고
    • Genetic and functional characterization of the gene cluster directing the biosynthesis of putisolvin I and II in Pseudomonas putida strain PCL1445
    • Dubern J.F., Coppoolse E.R., Stiekema W.J., and Bloemberg G.V. Genetic and functional characterization of the gene cluster directing the biosynthesis of putisolvin I and II in Pseudomonas putida strain PCL1445. Microbiology 154 (2008) 2070-2083
    • (2008) Microbiology , vol.154 , pp. 2070-2083
    • Dubern, J.F.1    Coppoolse, E.R.2    Stiekema, W.J.3    Bloemberg, G.V.4
  • 13
    • 0042975166 scopus 로고    scopus 로고
    • Natural products - a simple model to explain chemical diversity
    • Firn R.D., and Jones C.G. Natural products - a simple model to explain chemical diversity. Nat. Prod. Rep. 20 (2003) 382-391
    • (2003) Nat. Prod. Rep. , vol.20 , pp. 382-391
    • Firn, R.D.1    Jones, C.G.2
  • 15
    • 33645392725 scopus 로고    scopus 로고
    • Biosynthesis of pipecolic acid by RapL, a lysine cyclodeaminase encoded in the rapamycin gene cluster
    • Gatto G.J., Boyne M.T., Kelleher N.L., and Walsh C.T. Biosynthesis of pipecolic acid by RapL, a lysine cyclodeaminase encoded in the rapamycin gene cluster. J. Am. Chem. Soc. 128 (2006) 3838-3847
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 3838-3847
    • Gatto, G.J.1    Boyne, M.T.2    Kelleher, N.L.3    Walsh, C.T.4
  • 16
    • 1542763298 scopus 로고
    • Ring-closing metathesis and related processes in organic synthesis
    • Grubbs R.H., Miller S.J., and Fu G.C. Ring-closing metathesis and related processes in organic synthesis. Acc. Chem. Res. 28 (1995) 446-452
    • (1995) Acc. Chem. Res. , vol.28 , pp. 446-452
    • Grubbs, R.H.1    Miller, S.J.2    Fu, G.C.3
  • 17
    • 0022472378 scopus 로고
    • 2 analogs modified at the prolyl residue and evaluation of their effects on the receptor-binding activity of the central dopamine receptor agonist, ADTN
    • 2 analogs modified at the prolyl residue and evaluation of their effects on the receptor-binding activity of the central dopamine receptor agonist, ADTN. J. Med. Chem. 29 (1986) 2104-2107
    • (1986) J. Med. Chem. , vol.29 , pp. 2104-2107
    • Johnson, R.L.1    Rajakumar, G.2    Yu, K.L.3    Mishra, R.K.4
  • 19
    • 0031706012 scopus 로고    scopus 로고
    • Application of the asymmetric chelate enolate Claisen rearrangement to the synthesis of unsaturated polyhydroxylated amino acids
    • Kazmaier U., and Schneider C. Application of the asymmetric chelate enolate Claisen rearrangement to the synthesis of unsaturated polyhydroxylated amino acids. Synthesis (1998) 1321-1326
    • (1998) Synthesis , pp. 1321-1326
    • Kazmaier, U.1    Schneider, C.2
  • 20
  • 21
    • 2642591970 scopus 로고    scopus 로고
    • Mutational biosynthesis of novel rapamycins by a strain of Streptomyces hygroscopicus NRRL 5491 disrupted in rapL, encoding a putative lysine cyclodeaminase
    • Khaw L.E., Bohm G.A., Metcalfe S., Staunton J., and Leadlay P.F. Mutational biosynthesis of novel rapamycins by a strain of Streptomyces hygroscopicus NRRL 5491 disrupted in rapL, encoding a putative lysine cyclodeaminase. J. Bacteriol. 180 (1998) 809-814
    • (1998) J. Bacteriol. , vol.180 , pp. 809-814
    • Khaw, L.E.1    Bohm, G.A.2    Metcalfe, S.3    Staunton, J.4    Leadlay, P.F.5
  • 22
    • 34547953900 scopus 로고    scopus 로고
    • Interrogating the molecular basis for multiple macrolactone ring formation by the pikromycin polyketide synthase
    • Kittendorf J.D., Beck B.J., Buchholz T.J., Seufert W., and Sherman D.H. Interrogating the molecular basis for multiple macrolactone ring formation by the pikromycin polyketide synthase. Chem. Biol. 14 (2007) 944-954
    • (2007) Chem. Biol. , vol.14 , pp. 944-954
    • Kittendorf, J.D.1    Beck, B.J.2    Buchholz, T.J.3    Seufert, W.4    Sherman, D.H.5
  • 23
    • 22144451059 scopus 로고    scopus 로고
    • Production of the tubulin destabilizer disorazol in Sorangium cellulosum: biosynthetic machinery and regulatory genes
    • Kopp M., Irschik H., Pradella S., and Müller R. Production of the tubulin destabilizer disorazol in Sorangium cellulosum: biosynthetic machinery and regulatory genes. ChemBioChem 6 (2005) 1277-1286
    • (2005) ChemBioChem , vol.6 , pp. 1277-1286
    • Kopp, M.1    Irschik, H.2    Pradella, S.3    Müller, R.4
  • 24
    • 0035951102 scopus 로고    scopus 로고
    • Portability of epimerization domain and role of peptidyl carrier protein on epimerization activity in nonribosomal peptide synthetases
    • Linne U., Doekel S., and Marahiel M.A. Portability of epimerization domain and role of peptidyl carrier protein on epimerization activity in nonribosomal peptide synthetases. Biochemistry 40 (2001) 15824-15834
    • (2001) Biochemistry , vol.40 , pp. 15824-15834
    • Linne, U.1    Doekel, S.2    Marahiel, M.A.3
  • 25
    • 0037162408 scopus 로고    scopus 로고
    • Timing of epimerization and condensation reactions in nonribosomal peptide assembly lines: kinetic analysis of phenylalanine activating elongation modules of tyrocidine synthetase B
    • Luo L., Kohli R.M., Onishi M., Linne U., Marahiel M.A., and Walsh C.T. Timing of epimerization and condensation reactions in nonribosomal peptide assembly lines: kinetic analysis of phenylalanine activating elongation modules of tyrocidine synthetase B. Biochemistry 41 (2002) 9184-9196
    • (2002) Biochemistry , vol.41 , pp. 9184-9196
    • Luo, L.1    Kohli, R.M.2    Onishi, M.3    Linne, U.4    Marahiel, M.A.5    Walsh, C.T.6
  • 27
    • 49449110566 scopus 로고    scopus 로고
    • DKxanthene biosynthesis - understanding the basis for diversity-oriented synthesis in myxobacterial secondary metabolism
    • Meiser P., Weissman K.J., Bode H.B., Krug D., Dickschat J.S., Sandmann A., and Müller R. DKxanthene biosynthesis - understanding the basis for diversity-oriented synthesis in myxobacterial secondary metabolism. Chem. Biol. 15 (2008) 771-781
    • (2008) Chem. Biol. , vol.15 , pp. 771-781
    • Meiser, P.1    Weissman, K.J.2    Bode, H.B.3    Krug, D.4    Dickschat, J.S.5    Sandmann, A.6    Müller, R.7
  • 28
    • 0001603361 scopus 로고    scopus 로고
    • Stereoselective synthesis of functionalized carbocycles and heterocycles via an ester enolate Claisen/ring-closing metathesis manifold
    • Miller J.F., Termin A., Koch K., and Piscopio A.D. Stereoselective synthesis of functionalized carbocycles and heterocycles via an ester enolate Claisen/ring-closing metathesis manifold. J. Org. Chem. 63 (1998) 3158-3159
    • (1998) J. Org. Chem. , vol.63 , pp. 3158-3159
    • Miller, J.F.1    Termin, A.2    Koch, K.3    Piscopio, A.D.4
  • 29
    • 34247847842 scopus 로고    scopus 로고
    • Lipolytic enzymes in Myxococcus xanthus
    • Moraleda-Munoz A., and Shimkets L.J. Lipolytic enzymes in Myxococcus xanthus. J. Bacteriol. 189 (2007) 3072-3080
    • (2007) J. Bacteriol. , vol.189 , pp. 3072-3080
    • Moraleda-Munoz, A.1    Shimkets, L.J.2
  • 31
    • 36649010399 scopus 로고    scopus 로고
    • Design, synthesis, and biological properties of highly potent tubulysin D analogues
    • Patterson A.W., Peltier H.M., Sasse F., and Ellman J.A. Design, synthesis, and biological properties of highly potent tubulysin D analogues. Chemistry 13 (2007) 9534-9541
    • (2007) Chemistry , vol.13 , pp. 9534-9541
    • Patterson, A.W.1    Peltier, H.M.2    Sasse, F.3    Ellman, J.A.4
  • 32
    • 45249085481 scopus 로고    scopus 로고
    • Expedient synthesis of N-methyl tubulysin analogues with high cytotoxicity
    • Patterson A.W., Peltier H.M., and Ellman J.A. Expedient synthesis of N-methyl tubulysin analogues with high cytotoxicity. J. Org. Chem. 73 (2008) 4362-4369
    • (2008) J. Org. Chem. , vol.73 , pp. 4362-4369
    • Patterson, A.W.1    Peltier, H.M.2    Ellman, J.A.3
  • 33
    • 29844452482 scopus 로고    scopus 로고
    • Identification and analysis of the chivosazol biosynthetic gene cluster from the myxobacterial model strain Sorangium cellulosum So ce56
    • Perlova O., Gerth K., Hans A., Kaiser O., and Müller R. Identification and analysis of the chivosazol biosynthetic gene cluster from the myxobacterial model strain Sorangium cellulosum So ce56. J. Biotechnol. 121 (2006) 174-191
    • (2006) J. Biotechnol. , vol.121 , pp. 174-191
    • Perlova, O.1    Gerth, K.2    Hans, A.3    Kaiser, O.4    Müller, R.5
  • 35
    • 34250710858 scopus 로고    scopus 로고
    • Phylogenetic analysis of condensation domains in NRPS sheds light on their functional evolution
    • Rausch C., Hoof I., Weber T., Wohlleben W., and Huson D.H. Phylogenetic analysis of condensation domains in NRPS sheds light on their functional evolution. BMC Evol. Biol. 7 (2007) 78-92
    • (2007) BMC Evol. Biol. , vol.7 , pp. 78-92
    • Rausch, C.1    Hoof, I.2    Weber, T.3    Wohlleben, W.4    Huson, D.H.5
  • 36
    • 53649100100 scopus 로고    scopus 로고
    • The development and impact of 454 sequencing
    • Rothberg J.M., and Leamon J.H. The development and impact of 454 sequencing. Nat. Biotechnol. 26 (2008) 1117-1124
    • (2008) Nat. Biotechnol. , vol.26 , pp. 1117-1124
    • Rothberg, J.M.1    Leamon, J.H.2
  • 37
    • 4344669553 scopus 로고    scopus 로고
    • Identification and analysis of the core biosynthetic machinery of tubulysin, a potent cytotoxin with potential anticancer activity
    • Sandmann A., Sasse F., and Müller R. Identification and analysis of the core biosynthetic machinery of tubulysin, a potent cytotoxin with potential anticancer activity. Chem. Biol. 11 (2004) 1071-1079
    • (2004) Chem. Biol. , vol.11 , pp. 1071-1079
    • Sandmann, A.1    Sasse, F.2    Müller, R.3
  • 39
    • 0033779074 scopus 로고    scopus 로고
    • Tubulysins, new cytostatic peptides from myxobacteria acting on microtubuli: production, isolation, physico-chemical and biological properties
    • Sasse F., Steinmetz H., Heil J., Höfle G., and Reichenbach H. Tubulysins, new cytostatic peptides from myxobacteria acting on microtubuli: production, isolation, physico-chemical and biological properties. J. Antibiot. (Tokyo) 53 (2000) 879-885
    • (2000) J. Antibiot. (Tokyo) , vol.53 , pp. 879-885
    • Sasse, F.1    Steinmetz, H.2    Heil, J.3    Höfle, G.4    Reichenbach, H.5
  • 40
    • 0031682189 scopus 로고    scopus 로고
    • Asymmetric syntheses of chiral allylic alcohols
    • Schneider C., and Kazmaier U. Asymmetric syntheses of chiral allylic alcohols. Synthesis (1998) 1314-1320
    • (1998) Synthesis , pp. 1314-1320
    • Schneider, C.1    Kazmaier, U.2
  • 42
    • 0034673983 scopus 로고    scopus 로고
    • Mutational analysis of the epimerization domain in the initiation module PheATE of gramicidin S synthetase
    • Stachelhaus T., and Walsh C.T. Mutational analysis of the epimerization domain in the initiation module PheATE of gramicidin S synthetase. Biochemistry 39 (2000) 5775-5787
    • (2000) Biochemistry , vol.39 , pp. 5775-5787
    • Stachelhaus, T.1    Walsh, C.T.2
  • 43
    • 4344689901 scopus 로고    scopus 로고
    • Isolation, crystal and solution structure determination, and biosynthesis of tubulysins-powerful inhibitors of tubulin polymerization from myxobacteria
    • Steinmetz H., Glaser N., Herdtweck E., Sasse F., Reichenbach H., and Höfle G. Isolation, crystal and solution structure determination, and biosynthesis of tubulysins-powerful inhibitors of tubulin polymerization from myxobacteria. Angew. Chem. Int. Ed. Engl. 43 (2004) 4888-4892
    • (2004) Angew. Chem. Int. Ed. Engl. , vol.43 , pp. 4888-4892
    • Steinmetz, H.1    Glaser, N.2    Herdtweck, E.3    Sasse, F.4    Reichenbach, H.5    Höfle, G.6
  • 46
    • 62149114480 scopus 로고    scopus 로고
    • A brief tour of myxobacterial secondary metabolism
    • Weissman K.J., and Müller R. A brief tour of myxobacterial secondary metabolism. Bioorg. Med. Chem. 17 (2008) 2121-2136
    • (2008) Bioorg. Med. Chem. , vol.17 , pp. 2121-2136
    • Weissman, K.J.1    Müller, R.2
  • 47
    • 27844461167 scopus 로고    scopus 로고
    • Recent developments towards the heterologous expression of complex bacterial natural product biosynthetic pathways
    • Wenzel S.C., and Müller R. Recent developments towards the heterologous expression of complex bacterial natural product biosynthetic pathways. Curr. Opin. Biotechnol. 16 (2005) 594-606
    • (2005) Curr. Opin. Biotechnol. , vol.16 , pp. 594-606
    • Wenzel, S.C.1    Müller, R.2
  • 48
    • 36348982083 scopus 로고    scopus 로고
    • Myxobacterial natural product assembly lines: fascinating examples of curious biochemistry
    • Wenzel S.C., and Müller R. Myxobacterial natural product assembly lines: fascinating examples of curious biochemistry. Nat. Prod. Rep. 24 (2007) 1211-1224
    • (2007) Nat. Prod. Rep. , vol.24 , pp. 1211-1224
    • Wenzel, S.C.1    Müller, R.2
  • 49
    • 11844260210 scopus 로고    scopus 로고
    • A mild palladium catalyzed N-allylation of amino acids and peptides
    • Zumpe F.L., and Kazmaier U. A mild palladium catalyzed N-allylation of amino acids and peptides. Synlett (1998) 1199-1200
    • (1998) Synlett , pp. 1199-1200
    • Zumpe, F.L.1    Kazmaier, U.2
  • 50
    • 0032855073 scopus 로고    scopus 로고
    • Application of the palladium catalyzed N-allylation to the modification of amino acids and peptides
    • Zumpe F.L., and Kazmaier U. Application of the palladium catalyzed N-allylation to the modification of amino acids and peptides. Synthesis (1999) 1785-1791
    • (1999) Synthesis , pp. 1785-1791
    • Zumpe, F.L.1    Kazmaier, U.2


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