Bottromycins - biosynthesis, synthesis and activity
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This review summarizes bottromycin research from the 1950s to 2020, including structure elucidation, activity, mechanism of action, total synthesis, biosynthetic gene cluster and biosynthesis, biosynthetic enzymes and heterologous expression.
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Nissle 1917 contains two microcins (M and H47), one colicin, and one bottromycin, with the colicin and bottromycin not phenotypically expressed.
“the strain Nissle 1917, besides the already described two microcins, known as M and H47 [31, 32], demonstrates the presence of one colicin and one bottromycin [116], both not phenotypically expressed.”
From Selection, Comparative Genomics, and Potential Probiotic Features of Escherichia coli 5C, a pks-Negative Strain Isolated from Healthy Infant Donor Feces (2026) · cites this paper as [116]
The Introduction and Section 2 discuss bottromycin’s structure and discovery, but do not identify it in Nissle 1917. Searches for Nissle 1917, colicin, microcins, and phenotypic expression found no passage addressing the attributed claim; page numbers were unavailable in our copy. (LLM, conf=0.76)
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Wang, M., Carver, J. J., Phelan, V. V., Sanchez, L. M., Garg, N., Peng, Y., Nguyen, D. D., Watrous, J., Kapono, C. A., Luzzatto-Knaan, T., et al. (2016) · Nature Biotechnology · doi:10.1038/nbt.3597 · Cited by 4,629 · see citing works
Arnison, P. G., Bibb, M. J., Bierbaum, G., Bowers, A. A., Bugni, T. S., Bulaj, G. W., Camarero, J. A., Campopiano, D. J., Challis, G. L., Clardy, J., et al. (2012) · Natural Product Reports · doi:10.1039/c2np20085f · Cited by 2,065 · see citing works
Self-citationGust, B., Challis, G. L., Fowler, K., Kieser, T., & Chater, K. F. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0337542100 · Cited by 1,416 · see citing works
Plasmid cloning vectors for the conjugal transfer of DNA from Escherichia coli to Streptomyces spp.
Bierman, M. A., Logan, R. M., O'Brien, K. A., Seno, E. T., Rao, R. N., & Schoner, B. E. (1992) · Gene · doi:10.1016/0378-1119(92)90627-2 · Cited by 1,403 · see citing works
Brodersen, D. E., Clemons, W. M., Carter, A. P., Morgan-Warren, R. J., Wimberly, B. T., & Ramakrishnan, V. (2000) · Cell · doi:10.1016/s0092-8674(00)00216-6 · Cited by 950 · see citing works
New developments in RiPP discovery, enzymology and engineering
Montalbán‐López, M., Scott, T. A., Ramesh, S., Rahman, I. R., van Heel, A. J., Viel, J. H., Bandarian, V., Dittmann, E., Genilloud, O., Goto, Y., et al. (2020) · Natural Product Reports · doi:10.1039/d0np00027b · Cited by 775 · see citing works
Self-citationSchmidt, E. W., Nelson, J. T., Rasko, D. A., Sudek, S., Eisen, J. A., Haygood, M. G., & Ravel, J. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0501424102 · Cited by 567 · see citing works
Gomez‐Escribano, J. P., & Bibb, M. J. (2010) · Microbial Biotechnology · doi:10.1111/j.1751-7915.2010.00219.x · Cited by 556 · see citing works
Compilation and analysis of DNA sequences associated with apparent streptomycete promoters
Strohl, W. R. (1992) · Nucleic Acids Research · doi:10.1093/nar/20.5.961 · Cited by 481 · see citing works
Yamanaka, K., Reynolds, K. A., Kersten, R. D., Ryan, K. S., Gonzalez, D. J., Nizet, V., Dorrestein, P. C., & Moore, B. S. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1319584111 · Cited by 475 · see citing works
Understanding transport by the major facilitator superfamily (MFS): structures pave the way
Quistgaard, E. M., Löw, C., Guettou, F., & Nordlund, P. (2016) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2015.25 · Cited by 451 · see citing works
Lin, J., Zhou, D., Steitz, T. A., Polikanov, Y. S., & Gagnon, M. G. (2018) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-062917-011942 · Cited by 414 · see citing works
Follow the leader: the use of leader peptides to guide natural product biosynthesis
Oman, T. J., & van der Donk, W. A. (2009) · Nature Chemical Biology · doi:10.1038/nchembio.286 · Cited by 405 · see citing works
The Proteomics of N-terminal Methionine Cleavage
Frottin, F., Martinez, A., Peynot, P., Mitra, S., Holz, R. C., Giglione, C., & Meinnel, T. (2006) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m600225-mcp200 · Cited by 385 · see citing works
Leucine aminopeptidases: diversity in structure and function
Matsui, M., Fowler, J. H., & Walling, L. L. (2006) · Biological Chemistry · doi:10.1515/bc.2006.191 · Cited by 374 · see citing works
Rauwerdink, A. M., & Kazlauskas, R. J. (2015) · ACS Catalysis · doi:10.1021/acscatal.5b01539 · Cited by 354 · see citing works
Metagenome Mining Reveals Polytheonamides as Posttranslationally Modified Ribosomal Peptides
Freeman, M. F., Gurgui, C., Helf, M. J., Morinaka, B. I., Uria, A. R., Oldham, N. J., Sahl, H., Matsunaga, S., & Piel, J. (2012) · Science · doi:10.1126/science.1226121 · Cited by 351 · see citing works
RiPP antibiotics: biosynthesis and engineering potential
Hudson, G. A., & Mitchell, D. A. (2018) · Current Opinion in Microbiology · doi:10.1016/j.mib.2018.02.010 · Cited by 218 · see citing works
Siegl, T., Tokovenko, B. T., Myronovskyi, M., & Luzhetskyy, A. N. (2013) · Metabolic Engineering · doi:10.1016/j.ymben.2013.07.006 · Cited by 210 · see citing works
Discovery of a widely distributed toxin biosynthetic gene cluster
Lee, S. W., Mitchell, D. A., Markley, A. L., Hensler, M. E., Gonzalez, D. J., Wohlrab, A. M., Dorrestein, P. C., Nizet, V., & Dixon, J. E. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0801338105 · Cited by 206 · see citing works
Thirteen posttranslational modifications convert a 14-residue peptide into the antibiotic thiocillin
Brown, L. C. W., Acker, M. G., Clardy, J., Walsh, C. T., & Fischbach, M. A. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0900008106 · Cited by 187 · see citing works
Unveiling the functional diversity of the alpha/beta hydrolase superfamily in the plant kingdom
Mindrebo, J. T., Nartey, C. M., Seto, Y., Burkart, M. D., & Noel, J. P. (2016) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2016.08.005 · Cited by 181 · see citing works
Tang, T. P., & Ellman, J. A. (1998) · The Journal of Organic Chemistry · doi:10.1021/jo9820824 · Cited by 176 · see citing works
In Vitro Biosynthesis of the Core Scaffold of the Thiopeptide Thiomuracin
Hudson, G. A., Zhang, Z., Tietz, J. I., et al. (2015) · Journal of the American Chemical Society · doi:10.1021/jacs.5b10194 · Cited by 162 · see citing works
Hu, H., Zhang, Q., & Ochi, K. (2002) · Journal of Bacteriology · doi:10.1128/jb.184.14.3984-3991.2002 · Cited by 138 · see citing works
Morinaka, B. I., Vagstad, A. L., Helf, M. J., et al. (2014) · Angewandte Chemie International Edition · doi:10.1002/anie.201400478 · Cited by 128 · see citing works
Synthetic Biotechnology to Study and Engineer Ribosomal Bottromycin Biosynthesis
Huo, L., Rachid, S., Stadler, M., et al. (2012) · Chemistry & Biology · doi:10.1016/j.chembiol.2012.08.013 · Cited by 127 · see citing works
The Mechanisms of Action of Ribosome-Targeting Peptide Antibiotics
Polikanov, Y. S., Aleksashin, N. A., Beckert, B., & Wilson, D. N. (2018) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2018.00048 · Cited by 124 · see citing works
Hu, H., & Ochi, K. (2001) · Applied and Environmental Microbiology · doi:10.1128/aem.67.4.1885-1892.2001 · Cited by 118 · see citing works
Benjdia, A., Guillot, A., Ruffié, P., Leprince, J., & Berteau, O. (2017) · Nature Chemistry · doi:10.1038/nchem.2714 · Cited by 113 · see citing works
Huo, L., & van der Donk, W. A. (2016) · Journal of the American Chemical Society · doi:10.1021/jacs.6b02513 · Cited by 102 · see citing works
Davis, F. A., Reddy, R. E., & Szewczyk, J. M. (1995) · The Journal of Organic Chemistry · doi:10.1021/jo00126a070 · Cited by 91 · see citing works
Biosynthetic Timing and Substrate Specificity for the Thiopeptide Thiomuracin
Zhang, Z., Hudson, G. A., Mahanta, N., et al. (2016) · Journal of the American Chemical Society · doi:10.1021/jacs.6b08987 · Cited by 88 · see citing works
New Pathways in Plastics Recycling
Kaminsky, W., & Hartmann, F. (2000) · Angewandte Chemie International Edition · doi:10.1002/(sici)1521-3773(20000117)39:2 · Cited by 86 · see citing works
Structure and Biosynthesis of the Antibiotic Bottromycin D
Hou, Y., Tianero, M. D. B., Kwan, J. C., et al. (2012) · Organic Letters · doi:10.1021/ol3022758 · Cited by 85 · see citing works
Hug, J. J., Dastbaz, J., Adam, S., et al. (2020) · ACS Chemical Biology · doi:10.1021/acschembio.0c00430 · Cited by 85 · see citing works
Mahlert, C., Kopp, F. B., Thirlway, J., et al. (2007) · Journal of the American Chemical Society · doi:10.1021/ja074427i · Cited by 82 · see citing works
Synthetic riboswitches for the conditional control of gene expression in Streptomyces coelicolor
Rudolph, M. M., Vockenhuber, M.-P., & Suess, B. (2013) · Microbiology · doi:10.1099/mic.0.067322-0 · Cited by 81 · see citing works
Oppolzer, W., & Moretti, R. (1988) · Tetrahedron · doi:10.1016/s0040-4020(01)86059-2 · Cited by 81 · see citing works
New strategy for the synthesis of 3-substituted prolines
Karoyan, P., & Chassaing, G. (1997) · Tetrahedron Letters · doi:10.1016/s0040-4039(96)02221-6 · Cited by 77 · see citing works
DHARANIPRAGADA, R., VanHulle, K., Bannister, A., et al. (1992) · Tetrahedron · doi:10.1016/s0040-4020(01)81570-2 · Cited by 76 · see citing works
Studies on the Formation of Transfer Ribonucleic Acid-Ribosome Complexes
Pestka, S., & Brot, N. (1971) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)45834-1 · Cited by 75 · see citing works
Dissecting Bottromycin Biosynthesis Using Comparative Untargeted Metabolomics
Crone, W. J. K., Vior, N. M., Santos‐Aberturas, J., et al. (2016) · Angewandte Chemie International Edition · doi:10.1002/anie.201604304 · Cited by 75 · see citing works
DHARANIPRAGADA, R., Nicolás, E., Tóth, G., et al. (1989) · Tetrahedron Letters · doi:10.1016/s0040-4039(01)93366-0 · Cited by 72 · see citing works
Bott, T. M., Vanecko, J. A., & West, F. G. (2009) · The Journal of Organic Chemistry · doi:10.1021/jo9001323 · Cited by 71 · see citing works
Sharma, R. L., & Lubell, W. D. (1996) · The Journal of Organic Chemistry · doi:10.1021/jo9514984 · Cited by 71 · see citing works
Young, T. S., & Walsh, C. T. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1110435108 · Cited by 70 · see citing works
Crone, W. J. K., Leeper, F. J., & Truman, A. W. (2012) · Chemical Science · doi:10.1039/c2sc21190d · Cited by 70 · see citing works
Self-citationPeptide Syntheses via Ugi Reactionswith Ammonia
Kazmaier, U., & Hebach, C. (2003) · Synlett · doi:10.1055/s-2003-40987 · Cited by 70 · see citing works
Self-citationZheng, Q., Wang, Q., Wang, S., et al. (2015) · Chemistry & Biology · doi:10.1016/j.chembiol.2015.06.019 · Cited by 69 · see citing works
Gomez‐Escribano, J. P., Song, L., Bibb, M. J., & Challis, G. L. (2012) · Chemical Science · doi:10.1039/c2sc21183a · Cited by 69 · see citing works
Shimamura, H., Gouda, H., Nagai, K., et al. (2008) · Angewandte Chemie International Edition · doi:10.1002/anie.200804138 · Cited by 67 · see citing works
Secondary metabolites overproduction through transcriptional gene cluster refactoring
Horbal, L., Marques, F., Nadmid, S., et al. (2018) · Metabolic Engineering · doi:10.1016/j.ymben.2018.09.010 · Cited by 65 · see citing works
A straightforward approach towards thiazoles and endothiopeptides via Ugi reaction
Kazmaier, U., & Ackermann, S. (2005) · Organic & Biomolecular Chemistry · doi:10.1039/b507028g · Cited by 64 · see citing works
Self-citationBottromycin. I. A New Sulfur-containing Antibiotic
Waisvisz, J. M., van der Hoeven, M. G., Peppen, J. F. V., et al. (1957) · Journal of the American Chemical Society · doi:10.1021/ja01573a072 · Cited by 63 · see citing works
Noskov, V. N. (2002) · Nucleic Acids Research · doi:10.1093/nar/30.2.e8 · Cited by 61 · see citing works
Kobayashi, Y., Ichioka, M., Hirose, T., et al. (2010) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2010.08.037 · Cited by 59 · see citing works
Kataoka, Y., Seto, Y., Yamamoto, M., et al. (1976) · Bulletin of the Chemical Society of Japan · doi:10.1246/bcsj.49.1081 · Cited by 57 · see citing works
Negamycin interferes with decoding and translocation by simultaneous interaction with rRNA and tRNA
Polikanov, Y. S., Szal, T., Jiang, F., Gupta, P., Matsuda, R., Shiozuka, M., Steitz, T. A., Vázquez-Laslop, N., & Mankin, A. S. (2014) · Molecular Cell · doi:10.1016/j.molcel.2014.09.021 · Cited by 57 · see citing works
Yang, X., & van der Donk, W. A. (2015) · Journal of the American Chemical Society · doi:10.1021/jacs.5b05207 · Cited by 52 · see citing works
Houge‐Frydrych, C. S. V., Gilpin, M. L., Skett, P. W., et al. (2000) · The Journal of Antibiotics · doi:10.7164/antibiotics.53.364 · Cited by 52 · see citing works
The Structure of the Sulfur-containing Moiety of Bottromycin
Waisvisz, J. M., van der Hoeven, M. G., & Nijenhuis, B. T. (1957) · Journal of the American Chemical Society · doi:10.1021/ja01573a074 · Cited by 51 · see citing works
Olivier, N. B., Altman, R. B., Noeske, J., Basarab, G. S., Code, E., Ferguson, A. D., Gao, N., Huang, J., Juette, M. F., Livchak, S., et al. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1414401111 · Cited by 48 · see citing works
O'Donnell, M. J., Cooper, J. T., & Mader, M. M. (2003) · Journal of the American Chemical Society · doi:10.1021/ja0298794 · Cited by 47 · see citing works
Synthesis of homochiral 3-substituted glutamic acids and prolines from pyroglutamic acid
Herdeis, C., Hubmann, H. P., & Lotter, H. L. (1994) · Tetrahedron Asymmetry · doi:10.1016/s0957-4166(00)86204-7 · Cited by 46 · see citing works
Nogle, L. M., Mann, C. W., Watts, W. L., et al. (2005) · Journal of Pharmaceutical and Biomedical Analysis · doi:10.1016/j.jpba.2005.08.034 · Cited by 45 · see citing works
The revised structure of bottromycin A2.
Schipper, D. (1983) · The Journal of Antibiotics · doi:10.7164/antibiotics.36.1076 · Cited by 44 · see citing works
Flamant‐Robin, C., Wang, Q., Chiaroni, A., et al. (2002) · Tetrahedron · doi:10.1016/s0040-4020(02)01405-9 · Cited by 43 · see citing works
Mode of action of bottromycin A2. Release of aminoacyl- or peptidyl-tRNA from ribosomes.
Otaka, T., & Kaji, A. (1976) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)33586-x · Cited by 41 · see citing works
Dorus, S., Wilkin, E. C., & Karr, T. L. (2011) · BMC Genomics · doi:10.1186/1471-2164-12-177 · Cited by 40 · see citing works
Enright, A., Alexandre, F.-R., Roff, G. J., et al. (2003) · Chemical Communications · doi:10.1039/b309787k · Cited by 40 · see citing works
Ooi, T., Kato, D., Inamura, K., et al. (2007) · Organic Letters · doi:10.1021/ol701558e · Cited by 39 · see citing works
Synthesis and Evaluation of Antibacterial Activity of Bottromycins
Yamada, T., Yagita, M., Kobayashi, Y., et al. (2018) · The Journal of Organic Chemistry · doi:10.1021/acs.joc.8b00045 · Cited by 38 · see citing works
Grobuschek, N., Schmid, M. G., Tuscher, C., et al. (2002) · Journal of Pharmaceutical and Biomedical Analysis · doi:10.1016/s0731-7085(01)00616-1 · Cited by 37 · see citing works
Nouvelles synthèses de l-amino-acids—I
Titouani, S. L., Lavergne, J., Viallefont, P., et al. (1980) · Tetrahedron · doi:10.1016/0040-4020(80)88020-3 · Cited by 35 · see citing works
Schwalen, C. J., Hudson, G. A., Kosol, S., Mahanta, N., Challis, G. L., & Mitchell, D. A. (2017) · Journal of the American Chemical Society · doi:10.1021/jacs.7b09899 · Cited by 35 · see citing works
Eyles, T. H., Vior, N. M., & Truman, A. W. (2018) · ACS Synthetic Biology · doi:10.1021/acssynbio.8b00038 · Cited by 35 · see citing works
Self-citationMode of action of bottromycin A2: Effect of bottromycin A2 on polysomes
Otaka, T., & Kaji, A. (1983) · FEBS Letters · doi:10.1016/0014-5793(83)80118-5 · Cited by 32 · see citing works
Alı́as, M., López, P., & Cativiela, C. (2003) · Tetrahedron · doi:10.1016/j.tet.2003.11.044 · Cited by 32 · see citing works
Total Synthesis and Stereochemistry Revision of Mannopeptimycin Aglycone
Fuse, S., Koinuma, H., Kimbara, A., et al. (2014) · Journal of the American Chemical Society · doi:10.1021/ja505105t · Cited by 32 · see citing works
Macroamidine Formation in Bottromycins Is Catalyzed by a Divergent YcaO Enzyme
Franz, L. P., Adam, S., Santos‐Aberturas, J., Truman, A. W., & Koehnke, J. (2017) · Journal of the American Chemical Society · doi:10.1021/jacs.7b09898 · Cited by 32 · see citing works
Self-citationAn Enzymatic Route to Selenazolines
Koehnke, J., Morawitz, F., Bent, A. F., Houssen, W. E., Shirran, S. L., Fuszard, M. A., Smellie, I. A., Botting, C. H., Smith, M. C. M., Jaspars, M., et al. (2013) · ChemBioChem · doi:10.1002/cbic.201300037 · Cited by 29 · see citing works
Self-citationTörök, G., Péter, A., Armstrong, D. W., Tourwé, D., Tóth, G., & Sápi, J. (2001) · Chirality · doi:10.1002/chir.10004 · Cited by 28 · see citing works
Enantioselective approach to 3-substituted prolines
Kamenecka, T. M., Park, Y., Lin, L. S., et al. (2001) · Tetrahedron Letters · doi:10.1016/s0040-4039(01)01869-x · Cited by 28 · see citing works
Separation of enantiomeric β-methyl amino acids and of β-methyl amino acid containing peptides
Péter, A., Tóth, G., Török, G., et al. (1996) · Journal of Chromatography A · doi:10.1016/0021-9673(95)01022-x · Cited by 28 · see citing works
Mode of action of bottromycin A2: effect on peptide bond formation
Otaka, T., & Kaji, A. (1981) · FEBS Letters · doi:10.1016/0014-5793(81)80280-3 · Cited by 27 · see citing works
The revised structure of Bottromycin A2.
Takahashi, Y., NAGANAWA, H., TAKITA, T., et al. (1976) · The Journal of Antibiotics · doi:10.7164/antibiotics.29.1120 · Cited by 27 · see citing works
Isolation and characterization of bottromycins A2, B2, C2.
Nakamura, S., Yajima, T., Lin, Y., et al. (1967) · PubMed · Cited by 26 · see citing works
Seto, Y., Torii, K., Bori, K. O., et al. (1974) · Bulletin of the Chemical Society of Japan · doi:10.1246/bcsj.47.151 · Cited by 26 · see citing works
Medina, E., Moyano, A., Pericàs, M. À., et al. (1998) · The Journal of Organic Chemistry · doi:10.1021/jo981140i · Cited by 25 · see citing works
Kaneda, M. (1992) · The Journal of Antibiotics · doi:10.7164/antibiotics.45.792 · Cited by 24 · see citing works
Isolation, Characterization and Structural Elucidation of New Amino Acids from Bottromycin A
NAKAMURA, S., Chikaike, T., Yonehara, H., et al. (1965) · Chemical and Pharmaceutical Bulletin · doi:10.1248/cpb.13.599 · Cited by 23 · see citing works
The bottromycin epimerase BotH defines a group of atypical α/β-hydrolase-fold enzymes
Sikandar, A., Franz, L. P., Adam, S., et al. (2020) · Nature Chemical Biology · doi:10.1038/s41589-020-0569-y · Cited by 23 · see citing works
Self-citationVékes, E., Török, G., Péter, A., et al. (2002) · Journal of Chromatography A · doi:10.1016/s0021-9673(01)01455-8 · Cited by 21 · see citing works
Thiazoline-Specific Amidohydrolase PurAH Is the Gatekeeper of Bottromycin Biosynthesis
Sikandar, A., Franz, L. P., Melse, O., et al. (2019) · Journal of the American Chemical Society · doi:10.1021/jacs.8b12231 · Cited by 21 · see citing works
Self-citationSynthetic studies towards bottromycin
Ackermann, S., Lerchen, H., Häbich, D., et al. (2012) · Beilstein Journal of Organic Chemistry · doi:10.3762/bjoc.8.189 · Cited by 20 · see citing works
Gouda, H., Kobayashi, Y., Yamada, T., et al. (2012) · Chemical and Pharmaceutical Bulletin · doi:10.1248/cpb.60.169 · Cited by 20 · see citing works
Bai, X., Guo, H., Chen, D., et al. (2020) · Organic Chemistry Frontiers · doi:10.1039/c9qo01328h · Cited by 20 · see citing works
Synthesis of (S,S)-2-Amino-3-phenylbutyric Acid
Tsuchihashi, G.-I., Mitamura, S., & Ogura, K. (1979) · Bulletin of the Chemical Society of Japan · doi:10.1246/bcsj.52.2167 · Cited by 19 · see citing works
A straightforward approach towards 5-substituted thiazolylpeptides via the thio-Ugi-reaction
Kazmaier, U., & Persch, A. (2010) · Organic & Biomolecular Chemistry · doi:10.1039/c0ob00453g · Cited by 19 · see citing works
Self-citationPark, S. B. (2011) · Journal of Microbiology and Biotechnology · doi:10.4014/jmb.1106.06047 · Cited by 19 · see citing works
Yamada, T., Suegane, K., Kuwata, S., et al. (1977) · Bulletin of the Chemical Society of Japan · doi:10.1246/bcsj.50.1088 · Cited by 19 · see citing works
Bottromycin. II. Preliminary Degradation Studies
Waisvisz, J. M., van der Hoeven, M. G., Jf, H., et al. (1957) · Journal of the American Chemical Society · doi:10.1021/ja01573a073 · Cited by 19 · see citing works
Inhibition of Protein Synthesis by Bottromycin A2 and Its Hydrazide
Tanaka, N., Sashikata, K., Yamaguchi, H., et al. (1966) · The Journal of Biochemistry · doi:10.1093/oxfordjournals.jbchem.a128451 · Cited by 18 · see citing works
MECHANISM OF PROTEIN SYNTHESIS INHIBITION BY BOTTROMYCIN A2 : STUDIES WITH PUROMYCIN
LIN, Y.-C., Kinoshita, T., & Tanaka, N. (1968) · The Journal of Antibiotics · doi:10.7164/antibiotics.21.471 · Cited by 18 · see citing works
Bottromycin A1, A2 and their structures.
Nakamura, S., Tanaka, N., & Umezawa, H. (1966) · PubMed · Cited by 18 · see citing works
Mechanism of Action of Bottromycin in Polypeptide Biosynthesis
LIN, Y.-C., & Tanaka, N. (1968) · The Journal of Biochemistry · doi:10.1093/oxfordjournals.jbchem.a128735 · Cited by 17 · see citing works
Studies on translocation of F-met-tRNA and peptidyl-tRNA with antibiotics
Tanaka, N., LIN, Y.-C., & Okuyama, A. (1971) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(71)90626-7 · Cited by 17 · see citing works
In Vitro Biosynthesis of Peptides Containing Exotic Azoline Analogues
Goto, Y., & Suga, H. (2019) · ChemBioChem · doi:10.1002/cbic.201900521 · Cited by 17 · see citing works
The Structure of Bottromycin A2, a New Component of Bottromycins
NAKAMURA, S., & UMEZAWA, H. (1966) · Chemical and Pharmaceutical Bulletin · doi:10.1248/cpb.14.981 · Cited by 15 · see citing works
ISOLATION AND CHARACTERIZATION OF BOTTROMYCINS A AND B.
NAKAMURA, S., Chikaike, T., KARASAWA, K., et al. (1965) · PubMed · Cited by 15 · see citing works
Structure and Substrate Recognition of the Bottromycin Maturation Enzyme BotP
Mann, G., Huo, L., Adam, S., et al. (2016) · ChemBioChem · doi:10.1002/cbic.201600406 · Cited by 15 · see citing works
Ammonia in Ugi Reactions - Four-Component versus Six-Component Couplings
Kazmaier, U., Pick, R., Bauer, M., et al. (2005) · Synlett · doi:10.1055/s-2005-863722 · Cited by 15 · see citing works
Self-citationVior, N. M., Cea-Torrescassana, E., Eyles, T. H., Chandra, G., & Truman, A. W. (2020) · Frontiers in Microbiology · doi:10.3389/fmicb.2020.00495 · Cited by 15 · see citing works
Self-citationON THE SITE OF ACTION OF BOTTROMYGIN A2
Kinoshita, T., & Tanaka, N. (1970) · The Journal of Antibiotics · doi:10.7164/antibiotics.23.311 · Cited by 14 · see citing works
Enantiomeric Separation of Synthetic Amino Acids Using Capillary Zone Electrophoresis
Jiang, C., Armstrong, D. W., Lantz, A. W., et al. (2007) · Journal of Liquid Chromatography & Related Technologies · doi:10.1080/10826070701277018 · Cited by 13 · see citing works
ACTIVITY OF BOTTROMYGIN AGAINST MYCOPLASMA GALLISEPTICUM
Tanaka, N., Nishimura, T., NAKAMURA, S., et al. (1968) · The Journal of Antibiotics · doi:10.7164/antibiotics.21.75 · Cited by 13 · see citing works
Adam, S., Franz, L. P., Milhim, M., et al. (2020) · Journal of the American Chemical Society · doi:10.1021/jacs.0c10361 · Cited by 13 · see citing works
Self-citationIlisz, I., FODOR, G., Iványi, R., et al. (2008) · Journal of Chromatography B · doi:10.1016/j.jchromb.2008.05.020 · Cited by 12 · see citing works
The Chemistry and Partial Structure of Bottromycin. IV.
Waisvisz, J. M., & van der Hoeven, M. G. (1958) · Journal of the American Chemical Society · doi:10.1021/ja01535a034 · Cited by 12 · see citing works
Miller, W., Chaiet, L., Rasmussen, G., et al. (1968) · Journal of Medicinal Chemistry · doi:10.1021/jm00310a603 · Cited by 11 · see citing works
Török, R., Berkecz, R., & Péter, A. (2006) · Journal of Separation Science · doi:10.1002/jssc.200600100 · Cited by 9 · see citing works
Hydroxyalkyl Thiazolines, a New Class of Highly Efficient Ligands for Carbonyl Additions
Bauer, M., Maurer, F., Hoffmann, S., et al. (2008) · Synlett · doi:10.1055/s-0028-1087366 · Cited by 9 · see citing works
Ogawa, J., Ryono, A., Xie, S., et al. (2001) · Journal of Molecular Catalysis B Enzymatic · doi:10.1016/s1381-1177(00)00205-8 · Cited by 8 · see citing works
Medina, J. R., Blackledge, C. W., Erhard, K. F., et al. (2008) · The Journal of Organic Chemistry · doi:10.1021/jo7027163 · Cited by 7 · see citing works
Yamada, T., Miyazawa, T., Kuwata, S., et al. (1977) · Bulletin of the Chemical Society of Japan · doi:10.1246/bcsj.50.1827 · Cited by 7 · see citing works
The Long, Long Way to Bottromycin
Kazmaier, U. (2020) · Israel Journal of Chemistry · doi:10.1002/ijch.202000068 · Cited by 7 · see citing works
Self-citationBiological studies on bottromycin A and its hydrazide.
Tanaka, N., Nishimura, T., NAKAMURA, S., et al. (1966) · PubMed · Cited by 6 · see citing works
STRUCTURES OF BOTTROMYCINS A AND B.
Nakamura, S., Chikaike, T., Yonehara, H., et al. (1965) · PubMed · Cited by 5 · see citing works
Flagged first, then by citations
Research works printed but not linked: 6
- S. L. Titouani, J. P. Lavergne, P. Viallefont and R. Jacquier, New syntheses of L-amino acids. I. Stereospecic synthesis of L-proline, and of the cis-and trans-3-and 4-methyl L- prolines, Tetrahedron, 1980, 36(20-21), 2961-2965.
- Y. Seto, K. Torii, K. Bori, K. Inabata, S. Kuwata and H. Watanabe, Studies of Unusual Amino Acids and Their Peptides. VI. The Syntheses and the Optical Resolutions of b-Methylphenylalanine and Its Dipeptide Present in Bottromycin, Bull. Chem. Soc. Jpn., 1974, 47(1), 151-155.
- S. Nakamura, T. Chikaike, H. Yonehara and H. Umezawa, Structures of Bottromycins A and B, J. Antibiot., 1965, 18, 60-61.
- J. Kellenberger, On the Stereochemical Course of the C- methylation Steps in Bottromycin Biosynthesis, PhD thesis, ETH Switzerland, 1997.
- H. Mosimann and B. Kräutler, Methylcorrinoids Methylate Radicals-Their Second Biological Mode of Action?, Angew. Chem., Int. Ed. Engl., 2000, 39(2), 393-395.
- W. J. K. Crone, Investigations into the biosynthesis of bottromycin, University of Cambridge Cambridge, 2015.
Cited by
Sorted by citations
Di Pierro, F., Sagheddu, V., Galletti, S., Casaroli, A., Labrini, E., Soldi, S., Cazzaniga, M., Bertuccioli, A., Matera, M., Cavecchia, I., et al. (2026) · Probiotics and Antimicrobial Proteins · doi:10.1007/s12602-025-10522-5 · Cited by 5 · see citing works
“As regards to bacteriocin genes, the strain Nissle 1917, besides the already described two microcins, known as M and H47 [31, 32], demonstrates the presence of one colicin and one bottromycin [116], both not pheno-typically expressed.”
- Authors
- Franz, L., Kazmaier, U., Truman, A. W., & Koehnke, J.
- Affiliations
- Helmholtz Centre for Infection Research (DE)
- Saarland University (DE)
- John Innes Centre (GB)
- Corresponding author
- Koehnke, Jesko
- Venue
- Natural Product Reports
- Publisher
- Royal Society of Chemistry (RSC)
- Published
- 2021
- Volume
- 38
- Issue
- 9
- Pages
- 1659-1683
- ISSN
- 0265-0568 (ISSN-L)
- 1460-4752
- OpenAlex
- W3133121664
- Cited by
- 62
- References
- 129
- Citations by year
- 2026: 6 · 2025: 13 · 2024: 16 · 2023: 15 · 2022: 11 · 2021: 1
- FWCI
- 1.46
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Locations
- Natural Product Reports (publishedVersion, cc-by)
- PubMed (publishedVersion)
- ENLIGHTEN (Jurnal Bimbingan dan Konseling Islam) (acceptedVersion, cc-by-sa)
- HZI (Helmholtz Centre for Infection Research) (submittedVersion, cc-by)
- Funders
- Deutsche Forschungsgemeinschaft (KO 4116/3-2)
- Topics
- Health Sciences › Medicine › Pharmacology › Microbial Natural Products and Biosynthesis
- Physical Sciences › Chemistry › Organic Chemistry › Organic Chemistry Synthesis Methods
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Chemical Synthesis and Analysis
- Keywords
- biosynthesis, total synthesis, C-methylation, D-amino acids, macrolide antibiotics, natural product synthesis
- MeSH terms
- Anti-Bacterial Agents, Biological Products, Microbial Sensitivity Tests, Peptides, Cyclic, Protein Processing, Post-Translational, Molecular Structure
About these checks
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