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Journal articles on the topic 'Streptomyces cattleya'

Author: Grafiati

Published: 4 June 2021

Last updated: 1 February 2022

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1

Coyne, Vernon E., and Ralph Kirby. "VC11: an Actinophage Virulent to Streptomyces cattleya and Streptomyces olivaceus." Intervirology 25, no. 2 (1986): 61–68. http://dx.doi.org/10.1159/000149657.

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2

Hsiao, Nai-hua, and Ralph Kirby. "Comparative genomics of Streptomyces avermitilis, Streptomyces cattleya, Streptomyces maritimus and Kitasatospora aureofaciens using a Streptomyces coelicolor microarray system." Antonie van Leeuwenhoek 93, no. 1-2 (2007): 1–25. http://dx.doi.org/10.1007/s10482-007-9175-1.

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3

Reid, K. A., R. D. Bowden, L. Dasaradhi, M. R. Amin, and D. B. Harper. "Biosynthesis of fluorinated secondary metabolites by Streptomyces cattleya." Microbiology 141, no. 6 (1995): 1385–93. http://dx.doi.org/10.1099/13500872-141-6-1385.

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4

Deng, Hai, David O'Hagan, and Christoph Schaffrath. "Fluorometabolite biosynthesis and the fluorinase from Streptomyces cattleya." Natural Product Reports 21, no. 6 (2004): 773. http://dx.doi.org/10.1039/b415087m.

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5

O’Hagan, David. "Recent developments on the fluorinase from Streptomyces cattleya." Journal of Fluorine Chemistry 127, no. 11 (2006): 1479–83. http://dx.doi.org/10.1016/j.jfluchem.2006.09.006.

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6

Murphy, Cormac D., Steven J. Moss, and David O'Hagan. "Isolation of an Aldehyde Dehydrogenase Involved in the Oxidation of Fluoroacetaldehyde to Fluoroacetate inStreptomyces cattleya." Applied and Environmental Microbiology 67, no. 10 (2001): 4919–21. http://dx.doi.org/10.1128/aem.67.10.4919-4921.

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ABSTRACT Streptomyces cattleya is unusual in that it produces fluoroacetate and 4-fluorothreonine as secondary metabolites. We now report the isolation of an NAD+-dependent fluoroacetaldehyde dehydrogenase from S. cattleya that mediates the oxidation of fluoroacetaldehyde to fluoroacetate. This is the first enzyme to be identified that is directly involved in fluorometabolite biosynthesis. Production of the enzyme begins in late exponential growth and continues into the stationary phase. Measurement of kinetic parameters shows that the enzyme has a high affinity for fluoroacetaldehyde and glyc

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7

SANADA, MINORU, TETSUJI MIYANO, and SHUICHI IWADARE. ".BETA.-Ethynylserine, an antimetabolite of L-threonine, from Streptomyces cattleya." Journal of Antibiotics 39, no. 2 (1986): 304–5. http://dx.doi.org/10.7164/antibiotics.39.304.

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8

Williamson, J. M., E. Inamine, K. E. Wilson, A. W. Douglas, J. M. Liesch, and G. Albers-Schönberg. "Biosynthesis of the beta-lactam antibiotic, thienamycin, by Streptomyces cattleya." Journal of Biological Chemistry 260, no. 8 (1985): 4637–47. http://dx.doi.org/10.1016/s0021-9258(18)89118-9.

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9

PARESS, P. S., and S. L. STREICHER. "Glutamine Synthetase of Streptomyces cattleya: Purification and Regulation of Synthesis." Microbiology 131, no. 8 (1985): 1903–10. http://dx.doi.org/10.1099/00221287-131-8-1903.

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10

Houck, David R., and Edward Inamine. "Oxalic acid biosynthesis and oxalacetate acetylhydrolase activity in Streptomyces cattleya." Archives of Biochemistry and Biophysics 259, no. 1 (1987): 58–65. http://dx.doi.org/10.1016/0003-9861(87)90470-x.

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11

Foor, Forrest, Gary P. Roberts, Nancy Morin, et al. "Isolation and characterization of the Streptomyces cattleya temperate phage TG1." Gene 39, no. 1 (1985): 11–16. http://dx.doi.org/10.1016/0378-1119(85)90101-5.

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12

Rodríguez, Miriam, Carmen Méndez, José A. Salas, and Gloria Blanco. "Transcriptional organization of ThnI-regulated thienamycin biosynthetic genes in Streptomyces cattleya." Journal of Antibiotics 63, no. 3 (2010): 135–38. http://dx.doi.org/10.1038/ja.2009.133.

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13

Schaffrath, Christoph, Steven L. Cobb, and David O'Hagan. "Cell-Free Biosynthesis of Fluoroacetate and 4-Fluorothreonine in Streptomyces cattleya." Angewandte Chemie International Edition 41, no. 20 (2002): 3913–15. http://dx.doi.org/10.1002/1521-3773(20021018)41:20<3913::aid-anie3913>3.0.co;2-e.

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14

Schaffrath, Christoph, Steven L. Cobb, and David O'Hagan. "Cell-Free Biosynthesis of Fluoroacetate and 4-Fluorothreonine in Streptomyces cattleya." Angewandte Chemie 114, no. 20 (2002): 4069–71. http://dx.doi.org/10.1002/1521-3757(20021018)114:20<4069::aid-ange4069>3.0.co;2-w.

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15

Williamson, J. M., R. Meyer, and E. Inamine. "Reverse transsulfuration and its relationship to thienamycin biosynthesis in Streptomyces cattleya." Antimicrobial Agents and Chemotherapy 28, no. 4 (1985): 478–84. http://dx.doi.org/10.1128/aac.28.4.478.

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16

SANADA, MINORU, TETSUJI MIYANO, SHUICHI IWADARE, et al. "Biosynthesis of fluorothreonine and fluoroacetic acid by the thienamycin producer, Streptomyces cattleya." Journal of Antibiotics 39, no. 2 (1986): 259–65. http://dx.doi.org/10.7164/antibiotics.39.259.

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17

Tamura, T., M. Wada, N. Esaki, and K. Soda. "Synthesis of fluoroacetate from fluoride, glycerol, and beta-hydroxypyruvate by Streptomyces cattleya." Journal of bacteriology 177, no. 9 (1995): 2265–69. http://dx.doi.org/10.1128/jb.177.9.2265-2269.1995.

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18

Moss, Steven J., Cormac D. Murphy, David O’Hagan, et al. "Fluoroacetaldehyde: a precursor of both fluoroacetate and 4-fluorothreonine in Streptomyces cattleya." Chemical Communications, no. 22 (2000): 2281–82. http://dx.doi.org/10.1039/b007261n.

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19

Hamilton, John T. G., Cormac D. Murphy, Muhammad R. Amin, David O’Hagan, and David B. Harper. "Exploring the biosynthetic origin of fluoroacetate and 4-fluorothreonine in Streptomyces cattleya." Journal of the Chemical Society, Perkin Transactions 1, no. 4 (1998): 759–68. http://dx.doi.org/10.1039/a706554j.

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20

Braña, Alfredo F., Miriam Rodríguez, Pallab Pahari, Jurgen Rohr, Luis A. García, and Gloria Blanco. "Activation and silencing of secondary metabolites in Streptomyces albus and Streptomyces lividans after transformation with cosmids containing the thienamycin gene cluster from Streptomyces cattleya." Archives of Microbiology 196, no. 5 (2014): 345–55. http://dx.doi.org/10.1007/s00203-014-0977-z.

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21

Núñez, Luz Elena, Carmen Méndez, Alfredo F. Braña, Gloria Blanco та José A. Salas. "The Biosynthetic Gene Cluster for the β-Lactam Carbapenem Thienamycin in Streptomyces cattleya". Chemistry & Biology 10, № 4 (2003): 301–11. http://dx.doi.org/10.1016/s1074-5521(03)00069-3.

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22

Murphy, Cormac D., Christoph Schaffrath, and David O’Hagan. "Fluorinated natural products: the biosynthesis of fluoroacetate and 4-fluorothreonine in Streptomyces cattleya." Chemosphere 52, no. 2 (2003): 455–61. http://dx.doi.org/10.1016/s0045-6535(03)00191-7.

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23

Schaffrath, Christoph, Hai Deng, and David O'Hagan. "Isolation and characterisation of 5′-fluorodeoxyadenosine synthase, a fluorination enzyme from Streptomyces cattleya." FEBS Letters 547, no. 1-3 (2003): 111–14. http://dx.doi.org/10.1016/s0014-5793(03)00688-4.

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24

Weeks, Amy M., Ningkun Wang, Jeffrey G. Pelton, and Michelle C. Y. Chang. "Entropy drives selective fluorine recognition in the fluoroacetyl–CoA thioesterase from Streptomyces cattleya." Proceedings of the National Academy of Sciences 115, no. 10 (2018): E2193—E2201. http://dx.doi.org/10.1073/pnas.1717077115.

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Fluorinated small molecules play an important role in the design of bioactive compounds for a broad range of applications. As such, there is strong interest in developing a deeper understanding of how fluorine affects the interaction of these ligands with their targets. Given the small number of fluorinated metabolites identified to date, insights into fluorine recognition have been provided almost entirely by synthetic systems. The fluoroacetyl–CoA thioesterase (FlK) from Streptomyces cattleya thus provides a unique opportunity to study an enzyme–ligand pair that has been evolutionarily optim

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25

Kim, Hee-Jung, Seyoung Jang, Joonwon Kim, et al. "Biosynthesis of indigo in Escherichia coli expressing self-sufficient CYP102A from Streptomyces cattleya." Dyes and Pigments 140 (May 2017): 29–35. http://dx.doi.org/10.1016/j.dyepig.2017.01.029.

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26

Moss, Steven J., Cormac D. Murphy, John T. G. Hamilton, et al. "ChemInform Abstract: Fluoroacetaldehyde: A Precursor of Both Fluoroacetate and 4-Fluorothreonine in Streptomyces cattleya." ChemInform 32, no. 11 (2001): no. http://dx.doi.org/10.1002/chin.200111033.

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27

Barbe, V., M. Bouzon, S. Mangenot, et al. "Complete Genome Sequence of Streptomyces cattleya NRRL 8057, a Producer of Antibiotics and Fluorometabolites." Journal of Bacteriology 193, no. 18 (2011): 5055–56. http://dx.doi.org/10.1128/jb.05583-11.

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28

Cobb, Steven L., Hai Deng, Andrew R. McEwan, James H. Naismith, David O'Hagan, and David A. Robinson. "Substrate specificity in enzymatic fluorination. The fluorinase from Streptomyces cattleya accepts 2′-deoxyadenosine substrates." Organic & Biomolecular Chemistry 4, no. 8 (2006): 1458. http://dx.doi.org/10.1039/b600574h.

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29

Meade, Harry. "Cloning of argG from Streptomyces: Loss of Gene in Arg− Mutants of S. cattleya." Bio/Technology 3, no. 10 (1985): 917–18. http://dx.doi.org/10.1038/nbt1085-917.

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30

Hamilton, John T. G., Muhammad R. Amin, David B. Harper, and David O’Hagan. "Biosynthesis of fluoroacetate and 4-fluorothreonine by Streptomyces cattleya. Glycine and pyruvate as precursors." Chemical Communications, no. 8 (1997): 797–98. http://dx.doi.org/10.1039/a700495h.

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31

Nieschalk, Jens, John T. G. Hamilton, Cormac D. Murphy, David B. Harper, and David O’Hagan. "Biosynthesis of fluoroacetate and 4-fluorothreonine by Streptomyces cattleya. The stereochemical processing of glycerol." Chemical Communications, no. 8 (1997): 799–800. http://dx.doi.org/10.1039/a700498b.

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32

Zhao, Chunhua, Peng Li, Zixin Deng, Hong-Yu Ou, Ryan P. McGlinchey, and David O’Hagan. "Insights into fluorometabolite biosynthesis in Streptomyces cattleya DSM46488 through genome sequence and knockout mutants." Bioorganic Chemistry 44 (October 2012): 1–7. http://dx.doi.org/10.1016/j.bioorg.2012.06.002.

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33

Lilley, Gerald, Anne E. Clark, and Gordon C. Lawrence. "Control of the production of cephamycin C and thienamycin by Streptomyces cattleya NRRL 8057." Journal of Chemical Technology and Biotechnology 31, no. 1 (2007): 127–34. http://dx.doi.org/10.1002/jctb.503310118.

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34

Kim, Joonwon, Pyung-gang Lee, Eun-ok Jung, and Byung-Gee Kim. "In vitro characterization of CYP102G4 from Streptomyces cattleya: A self-sufficient P450 naturally producing indigo." Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics 1866, no. 1 (2018): 60–67. http://dx.doi.org/10.1016/j.bbapap.2017.08.002.

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35

Sugai, Shogo, Hisayuki Komaki, Hikaru Hemmi, and Shinya Kodani. "Isolation and structural determination of a new antibacterial compound demethyl-L-681,217 from Streptomyces cattleya." Journal of Antibiotics 69, no. 11 (2016): 839–42. http://dx.doi.org/10.1038/ja.2016.53.

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36

BUCHAN, TIM, CLAUDIA ROACH, CAROLYN RUBY, DEAN TAYLOR, CAROL PREISIG, and CHRISTOPHER REEVES. "Mutants of Streptomyces cattleya defective in the synthesis of a factor required for thienamycin production." Journal of Antibiotics 47, no. 9 (1994): 992–1000. http://dx.doi.org/10.7164/antibiotics.47.992.

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37

Wu, Linrui, Ming Him Tong, Kwaku Kyeremeh, and Hai Deng. "Identification of 5-Fluoro-5-Deoxy-Ribulose as a Shunt Fluorometabolite in Streptomyces sp. MA37." Biomolecules 10, no. 7 (2020): 1023. http://dx.doi.org/10.3390/biom10071023.

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A fluorometabolite, 5-fluoro-5-deoxy-D-ribulose (5-FDRul), from the culture broth of the soil bacterium Streptomyces sp. MA37, was identified through a combination of genetic manipulation, chemo-enzymatic synthesis and NMR comparison. Although 5-FDRul has been chemically synthesized before, it was not an intermediate or a shunt product in previous studies of fluorometalism in S. cattleya. Our study of MA37 demonstrates that 5-FDRul is a naturally occurring fluorometabolite, rendering it a new addition to this rare collection of natural products. The genetic inactivation of key biosynthetic gen

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38

Tamura, Takashi, Yukako Sawamoto, Takatoshi Kuriyama, Kouzo Oba, Hidehiko Tanaka, and Kenji Inagaki. "Cosynthesis of monofluoroacetate and 4-fluorothreonine by resting cells of blocked mutants of Streptomyces cattleya NRRL8057." Journal of Molecular Catalysis B: Enzymatic 23, no. 2-6 (2003): 257–63. http://dx.doi.org/10.1016/s1381-1177(03)00088-2.

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39

Hromic, Alma, and Ralph Kirby. "Isolation and study of two mutants of Streptomyces cattleya affected in DNA repair and genetic instability." FEMS Microbiology Letters 57, no. 2 (1989): 139–43. http://dx.doi.org/10.1111/j.1574-6968.1989.tb03288.x.

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40

Sugai, Shogo, Mayumi Ohnishi-Kameyama, and Shinya Kodani. "Isolation and identification of a new lasso peptide cattlecin from Streptomyces cattleya based on genome mining." Applied Biological Chemistry 60, no. 2 (2017): 163–67. http://dx.doi.org/10.1007/s13765-017-0268-x.

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41

de la FUENTE, Juan L., Angel RUMBERO, Juan F. MARTÍN та Paloma LIRAS. "Δ-1-Piperideine-6-carboxylate dehydrogenase, a new enzyme that forms α-aminoadipate in Streptomyces clavuligerus and other cephamycin C-producing actinomycetes". Biochemical Journal 327, № 1 (1997): 59–64. http://dx.doi.org/10.1042/bj3270059.

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Δ-1-Piperideine-6-carboxylate (P6C) dehydrogenase activity, which catalyses the conversion of P6C into α-aminoadipic acid, has been studied in the cephamycin C producer Streptomyces clavuligerus by both spectrophotometric and radiometric assays. The enzyme has been purified 124-fold to electrophoretic homogeneity with a 26% yield. The native protein is a monomer of 56.2 kDa that efficiently uses P6C (apparent Km 14 μM) and NAD+ (apparent Km 115 μM), but not NADP+ or other electron acceptors, as substrates. The enzyme activity was inhibited (by 66%) by its end product NADH at 0.1 mM concentrati

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42

Huang, Fanglu, Stephen F. Haydock, Dieter Spiteller, et al. "The Gene Cluster for Fluorometabolite Biosynthesis in Streptomyces cattleya: A Thioesterase Confers Resistance to Fluoroacetyl-Coenzyme A." Chemistry & Biology 13, no. 5 (2006): 475–84. http://dx.doi.org/10.1016/j.chembiol.2006.02.014.

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43

Cadicamo, Cosimo D., Jacques Courtieu, Hai Deng, Abdelkrim Meddour, and David O'Hagan. "Enzymatic Fluorination in Streptomyces cattleya Takes Place with an Inversion of Configuration Consistent with an SN2 Reaction Mechanism." ChemBioChem 5, no. 5 (2004): 685–90. http://dx.doi.org/10.1002/cbic.200300839.

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44

Cobb, Steven L., Hai Deng, John T. G. Hamilton, Ryan P. McGlinchey, David O’Hagan, and Christoph Schaffrath. "The identification of 5′-fluoro-5-deoxyinosine as a shunt product in cell free extracts of Streptomyces cattleya." Bioorganic Chemistry 33, no. 5 (2005): 393–401. http://dx.doi.org/10.1016/j.bioorg.2005.07.002.

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45

Cobb, Steven L., Hai Deng, John T. G. Hamilton, Ryan P. McGlinchey, and David O'Hagan. "Identification of 5-fluoro-5-deoxy-d-ribose-1-phosphate as an intermediate in fluorometabolite biosynthesis in Streptomyces cattleya." Chemical Communications, no. 5 (2004): 592. http://dx.doi.org/10.1039/b400754a.

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46

USDIN, KAREN, KAREN M. CHRISTIANS, C. ANDRE DE WET, TROY D. POTGIETER, CORRINE B. SHAW, and RALPH KIRBY. "The Loss of a Large DNA Fragment is Associated with an Aerial Mycelium Negative (Amy-) Phenotype of Streptomyces cattleya." Microbiology 131, no. 4 (1985): 979–81. http://dx.doi.org/10.1099/00221287-131-4-979.

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47

Foor, Forrest, and Nancy Morin. "Construction of a shuttle vector consisting of the Escherichia coli plasmid pACYC177 inserted into the Streptomyces cattleya phage TG1." Gene 94, no. 1 (1990): 109–13. http://dx.doi.org/10.1016/0378-1119(90)90475-7.

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48

Onadipe, Adekunle O., and Michael E. Bushell. "The use of multivariate analysis for the design of selective isolation conditions for mutants of Streptomyces cattleya with improved antibiotic titre." Journal of Chemical Technology & Biotechnology 39, no. 4 (2007): 237–49. http://dx.doi.org/10.1002/jctb.280390405.

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49

Onega, Mayca, Ryan P. McGlinchey, Hai Deng, John T. G. Hamilton, and David O’Hagan. "The identification of (3R,4S)-5-fluoro-5-deoxy-d-ribulose-1-phosphate as an intermediate in fluorometabolite biosynthesis in Streptomyces cattleya." Bioorganic Chemistry 35, no. 5 (2007): 375–85. http://dx.doi.org/10.1016/j.bioorg.2007.04.001.

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50

Cadicamo, Cosimo D., Jacques Courtieu, Hai Deng, Abdelkrim Meddour, and David O'Hagan. "Cover Picture: Enzymatic Fluorination in Streptomyces cattleya Takes Place with an Inversion of Configuration Consistent with an SN2 Reaction Mechanism (ChemBioChem 5/2004)." ChemBioChem 5, no. 5 (2004): 557. http://dx.doi.org/10.1002/cbic.200490021.

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