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Volumn 175, Issue 6, 2015, Pages 2934-2949

Enhanced Production of Nargenicin A1 and Generation of Novel Glycosylated Derivatives

Author keywords

Glucopyranoside; Nargenicin A1; Nocardia sp. CS682; Novel nargenicin A1; One pot glycosylation

Indexed keywords

BACTERIOLOGY; DRUG PRODUCTS; ELECTROSPRAY IONIZATION; GLUCOSE; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; KETONES; MASS SPECTROMETRY; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; SOLUBILITY;

EID: 84924040451     PISSN: 02732289     EISSN: 15590291     Source Type: Journal    
DOI: 10.1007/s12010-014-1472-3     Document Type: Article
Times cited : (25)

References (43)
  • 3
    • 64249148822 scopus 로고    scopus 로고
    • Nargenicin enhances 1,25-dihydroxyvitamin D3- and all-trans retinoic acid-induced leukemia cell differentiation via PKCβI/MAPK pathways
    • COI: 1:CAS:528:DC%2BD1MXkvVSqtr0%3D
    • Kim, S. H., Yoo, J. C., & Kim, T. S. (2009). Nargenicin enhances 1,25-dihydroxyvitamin D3- and all-trans retinoic acid-induced leukemia cell differentiation via PKCβI/MAPK pathways. Biochemical Pharmacology, 77, 1694–1701.
    • (2009) Biochemical Pharmacology , vol.77 , pp. 1694-1701
    • Kim, S.H.1    Yoo, J.C.2    Kim, T.S.3
  • 4
    • 67749124149 scopus 로고    scopus 로고
    • Nargenicin attenuates lipopolysaccharide-induced inflammatory responses in BV-2 cells
    • COI: 1:CAS:528:DC%2BD1MXnslyru7o%3D
    • Yoo, J. C., Cho, H. S., Park, E., Park, J. A., Kim, S., Kim, D. K., Kim, C. S., & Chun, H. S. (2009). Nargenicin attenuates lipopolysaccharide-induced inflammatory responses in BV-2 cells. Neuroreport, 20, 1007–1012.
    • (2009) Neuroreport , vol.20 , pp. 1007-1012
    • Yoo, J.C.1    Cho, H.S.2    Park, E.3    Park, J.A.4    Kim, S.5    Kim, D.K.6    Kim, C.S.7    Chun, H.S.8
  • 7
    • 50249084003 scopus 로고    scopus 로고
    • Improving production of bioactive secondary metabolites in actinomycetes by metabolic engineering
    • COI: 1:CAS:528:DC%2BD1cXhtVKjtb3K
    • Olano, C., Lombó, F., Méndez, C., & Salas, J. A. (2008). Improving production of bioactive secondary metabolites in actinomycetes by metabolic engineering. Metabolic Engineering, 10, 281–292.
    • (2008) Metabolic Engineering , vol.10 , pp. 281-292
    • Olano, C.1    Lombó, F.2    Méndez, C.3    Salas, J.A.4
  • 8
    • 79951848091 scopus 로고    scopus 로고
    • Molecular insights on the biosynthesis of antitumour compounds by actinomycetes
    • COI: 1:CAS:528:DC%2BC3MXjt1Wquro%3D
    • Olano, C., Méndez, C., & Salas, J. A. (2011). Molecular insights on the biosynthesis of antitumour compounds by actinomycetes. Microbial Biotechnology, 4, 144–164.
    • (2011) Microbial Biotechnology , vol.4 , pp. 144-164
    • Olano, C.1    Méndez, C.2    Salas, J.A.3
  • 9
    • 0024571809 scopus 로고
    • Clinical pharmacokinetic properties of the macrolide antibiotics
    • COI: 1:CAS:528:DyaL1MXkslSju7c%3D
    • Periti, P., Mazzei, T., Mini, E., & Novelli, A. (1989). Clinical pharmacokinetic properties of the macrolide antibiotics. Clinical Pharmacokinetics, 16, 193–214.
    • (1989) Clinical Pharmacokinetics , vol.16 , pp. 193-214
    • Periti, P.1    Mazzei, T.2    Mini, E.3    Novelli, A.4
  • 11
    • 77956260624 scopus 로고    scopus 로고
    • Genetic engineering approach for the production of rhamnosyl and allosyl flavonoids from Escherichia coli
    • COI: 1:CAS:528:DC%2BC3cXptFGltbg%3D
    • Simkhada, D., Lee, H. C., & Sohng, J. K. (2010). Genetic engineering approach for the production of rhamnosyl and allosyl flavonoids from Escherichia coli. Biotechnology and Bioengineering, 107, 154–162.
    • (2010) Biotechnology and Bioengineering , vol.107 , pp. 154-162
    • Simkhada, D.1    Lee, H.C.2    Sohng, J.K.3
  • 12
    • 84871830186 scopus 로고    scopus 로고
    • The structural biology of enzymes involved in natural product glycosylation
    • COI: 1:CAS:528:DC%2BC38XhtlCjsbjF
    • Singh, S., Phillips, G. N., Jr., & Thorson, J. S. (2012). The structural biology of enzymes involved in natural product glycosylation. Natural Product Reports, 29, 1201–1237.
    • (2012) Natural Product Reports , vol.29 , pp. 1201-1237
    • Singh, S.1    Phillips, G.N.2    Thorson, J.S.3
  • 13
    • 0034872489 scopus 로고    scopus 로고
    • Glycosides in medicine: “the role of glycosidic residue in biological activity
    • COI: 1:CAS:528:DC%2BD3MXmt1ShtbY%3D
    • Kren, V., & Martínková, L. (2001). Glycosides in medicine: “the role of glycosidic residue in biological activity”. Current Medicinal Chemistry, 8, 1303–1328.
    • (2001) Current Medicinal Chemistry , vol.8 , pp. 1303-1328
    • Kren, V.1    Martínková, L.2
  • 14
    • 0031127564 scopus 로고    scopus 로고
    • The role of carbohydrates in biologically active natural products
    • COI: 1:CAS:528:DyaK2sXivVGrtro%3D
    • Weymouth-Wilson, A. C. (1997). The role of carbohydrates in biologically active natural products. Natural Product Reports, 14, 99–110.
    • (1997) Natural Product Reports , vol.14 , pp. 99-110
    • Weymouth-Wilson, A.C.1
  • 15
  • 17
    • 84880810277 scopus 로고    scopus 로고
    • Regiospecific modifications of naringenin for astragalin production in Escherichia coli
    • COI: 1:CAS:528:DC%2BC3sXmt1Omur8%3D
    • Malla, S., Pandey, R. P., Kim, B. G., & Sohng, J. K. (2013). Regiospecific modifications of naringenin for astragalin production in Escherichia coli. Biotechnology and Bioengineering, 110, 2525–2535.
    • (2013) Biotechnology and Bioengineering , vol.110 , pp. 2525-2535
    • Malla, S.1    Pandey, R.P.2    Kim, B.G.3    Sohng, J.K.4
  • 18
    • 4444253051 scopus 로고    scopus 로고
    • One-pot enzymatic synthesis of UDP-D-glucose from UMP and glucose-1-phosphate using an ATP regeneration system
    • Lee, H. C., Lee, S. D., Sohng, J. K., & Liou, K. (2004). One-pot enzymatic synthesis of UDP-D-glucose from UMP and glucose-1-phosphate using an ATP regeneration system. Journal of Biochemistry and Molecular Biology, 37, 503–506.
    • (2004) Journal of Biochemistry and Molecular Biology , vol.37 , pp. 503-506
    • Lee, H.C.1    Lee, S.D.2    Sohng, J.K.3    Liou, K.4
  • 20
    • 34248581665 scopus 로고    scopus 로고
    • An efficient chemoenzymatic production of small molecule glucosides with in situ UDP-glucose recycling
    • COI: 1:CAS:528:DC%2BD2sXlvFamtr4%3D
    • Masada, S., Kawase, Y., Nagatoshi, M., Oguchi, Y., Terasaka, K., & Mizukami, H. (2007). An efficient chemoenzymatic production of small molecule glucosides with in situ UDP-glucose recycling. FEBS Letters, 581, 2562–2566.
    • (2007) FEBS Letters , vol.581 , pp. 2562-2566
    • Masada, S.1    Kawase, Y.2    Nagatoshi, M.3    Oguchi, Y.4    Terasaka, K.5    Mizukami, H.6
  • 21
    • 84870499885 scopus 로고    scopus 로고
    • In situ UDP-glucose regeneration unravels diverse functions of plant secondary product glycosyltransferases
    • COI: 1:CAS:528:DC%2BC38XhsleisbjL
    • Terasaka, K., Mizutani, Y., Nagatsu, A., & Mizukami, H. (2012). In situ UDP-glucose regeneration unravels diverse functions of plant secondary product glycosyltransferases. FEBS Letters, 586, 4344–4350.
    • (2012) FEBS Letters , vol.586 , pp. 4344-4350
    • Terasaka, K.1    Mizutani, Y.2    Nagatsu, A.3    Mizukami, H.4
  • 22
    • 84920254307 scopus 로고    scopus 로고
    • Efficient enzymatic systems for synthesis of novel α-mangostin glycosides exhibiting antibacterial activity against Gram-positive bacteria
    • Tuoi, L. T., Pandey, R. P., Gurung, R. B., Dhakal, D., & Sohng, J. K. (2014). Efficient enzymatic systems for synthesis of novel α-mangostin glycosides exhibiting antibacterial activity against Gram-positive bacteria. Applied Microbiology and Biotechnology, 98, 8527–8538.
    • (2014) Applied Microbiology and Biotechnology , vol.98 , pp. 8527-8538
    • Tuoi, L.T.1    Pandey, R.P.2    Gurung, R.B.3    Dhakal, D.4    Sohng, J.K.5
  • 23
    • 84864005341 scopus 로고    scopus 로고
    • Effect of different biosynthetic precursors on the production of nargenicin A1 from metabolically engineered Nocardia sp. CS682
    • COI: 1:CAS:528:DC%2BC38XhsFWktbjE
    • Koju, D., Dhakal, D., & Sohng, J. K. (2012). Effect of different biosynthetic precursors on the production of nargenicin A1 from metabolically engineered Nocardia sp. CS682. Journal of Microbiology and Biotechnology, 22, 1127–1132.
    • (2012) Journal of Microbiology and Biotechnology , vol.22 , pp. 1127-1132
    • Koju, D.1    Dhakal, D.2    Sohng, J.K.3
  • 24
    • 33746608987 scopus 로고    scopus 로고
    • Biological formation of pyrroles: nature's logic and enzymatic machinery
    • COI: 1:CAS:528:DC%2BD28XovVWmu7o%3D
    • Walsh, C. T., Garneau-Tsodikova, S., & Howard-Jones, A. R. (2006). Biological formation of pyrroles: nature's logic and enzymatic machinery. Natural Product Reports, 23, 517–531.
    • (2006) Natural Product Reports , vol.23 , pp. 517-531
    • Walsh, C.T.1    Garneau-Tsodikova, S.2    Howard-Jones, A.R.3
  • 26
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • COI: 1:CAS:528:DyaE28XksVehtrY%3D
    • Bradford, M. M. (1976). A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Analytical Biochemistry, 72, 248–254.
    • (1976) Analytical Biochemistry , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 27
    • 84884874505 scopus 로고    scopus 로고
    • An insight into the “-omics” based engineering of streptomycetes for secondary metabolite overproduction
    • Chaudhary, A. K., Dhakal, D., &Sohng, J. K. (2013). An insight into the “-omics” based engineering of streptomycetes for secondary metabolite overproduction. BioMedResearch International, 2013, 968518.
    • (2013) BioMedResearch International , vol.2013
    • Chaudhary, A.K.1    Dhakal, D.2
  • 28
    • 58149190072 scopus 로고    scopus 로고
    • Metabolic engineering of microorganisms: general strategies and drug production
    • COI: 1:CAS:528:DC%2BD1MXktVShtg%3D%3D
    • Lee, S. Y., Kim, H. U., Park, J. H., Park, J. M., & Kim, T. Y. (2009). Metabolic engineering of microorganisms: general strategies and drug production. Drug Discovery Today, 14, 78–88.
    • (2009) Drug Discovery Today , vol.14 , pp. 78-88
    • Lee, S.Y.1    Kim, H.U.2    Park, J.H.3    Park, J.M.4    Kim, T.Y.5
  • 29
    • 84858703813 scopus 로고    scopus 로고
    • Metabolic engineering of Nocardia sp. CS682 for enhanced production of nargenicin A1
    • COI: 1:CAS:528:DC%2BC38Xhslynu7o%3D
    • Maharjan, S., Koju, D., Lee, H. C., Yoo, J. C., & Sohng, J. K. (2012). Metabolic engineering of Nocardia sp. CS682 for enhanced production of nargenicin A1. Applied Biochemistry and Biotechnology, 166, 805–817.
    • (2012) Applied Biochemistry and Biotechnology , vol.166 , pp. 805-817
    • Maharjan, S.1    Koju, D.2    Lee, H.C.3    Yoo, J.C.4    Sohng, J.K.5
  • 30
    • 84891861698 scopus 로고    scopus 로고
    • Enhancement of ansamitocin P-3 production in Actinosynnemapretiosum by a synergistic effect of glycerol and glucose
    • COI: 1:CAS:528:DC%2BC3sXhslWhtbfF
    • Gao, Y., Fan, Y., Nambou, K., Wei, L., Liu, Z., Imanaka, T., & Hua, Q. (2014). Enhancement of ansamitocin P-3 production in Actinosynnemapretiosum by a synergistic effect of glycerol and glucose. Journal of Industrial Microbiology & Biotechnology, 41, 143–152.
    • (2014) Journal of Industrial Microbiology & Biotechnology , vol.41 , pp. 143-152
    • Gao, Y.1    Fan, Y.2    Nambou, K.3    Wei, L.4    Liu, Z.5    Imanaka, T.6    Hua, Q.7
  • 31
    • 82855178853 scopus 로고    scopus 로고
    • Enhancement of pradimicin production in Actinomadurahibisca P157-2 by metabolic engineering
    • Paudel, S., Lee, H. C., Kim, B. S., & Sohng, J. K. (2011). Enhancement of pradimicin production in Actinomadurahibisca P157-2 by metabolic engineering. Microbiological Research, 167, 32–39.
    • (2011) Microbiological Research , vol.167 , pp. 32-39
    • Paudel, S.1    Lee, H.C.2    Kim, B.S.3    Sohng, J.K.4
  • 32
    • 49749112862 scopus 로고    scopus 로고
    • Heterologous expression of metK1-sp and afsR-sp in Streptomyces venezuelae for the production of pikromycin
    • COI: 1:CAS:528:DC%2BD1cXpvVKlsro%3D
    • Maharjan, S., Oh, T. J., Lee, H. C., & Sohng, J. K. (2008). Heterologous expression of metK1-sp and afsR-sp in Streptomyces venezuelae for the production of pikromycin. Biotechnology Letters, 30, 1621–1626.
    • (2008) Biotechnology Letters , vol.30 , pp. 1621-1626
    • Maharjan, S.1    Oh, T.J.2    Lee, H.C.3    Sohng, J.K.4
  • 33
    • 84893103701 scopus 로고    scopus 로고
    • Enhancement of herboxidiene production in Streptomyces chromofuscus ATCC 49982
    • COI: 1:CAS:528:DC%2BC2cXlvFSqu7Y%3D
    • Jha, A. K., Lamichhane, J., & Sohng, J. K. (2014). Enhancement of herboxidiene production in Streptomyces chromofuscus ATCC 49982. Journal of Microbiology and Biotechnology, 24, 52–58.
    • (2014) Journal of Microbiology and Biotechnology , vol.24 , pp. 52-58
    • Jha, A.K.1    Lamichhane, J.2    Sohng, J.K.3
  • 34
    • 64049107094 scopus 로고    scopus 로고
    • Enzymatic synthesis of TDP-deoxysugars
    • COI: 1:CAS:528:DC%2BD1MXpsFaqu74%3D
    • White-Phillip, J., Thibodeaux, C. J., & Liu, H. W. (2009). Enzymatic synthesis of TDP-deoxysugars. Methods in Enzymology, 459, 521–544.
    • (2009) Methods in Enzymology , vol.459 , pp. 521-544
    • White-Phillip, J.1    Thibodeaux, C.J.2    Liu, H.W.3
  • 35
    • 80055000805 scopus 로고    scopus 로고
    • Enzymatic methods for glyco (diversification/randomization) of drugs and small molecules
    • COI: 1:CAS:528:DC%2BC3MXhtlaku73N
    • Gantt, R. W., Peltier-Pain, P., & Thorson, J. S. (2011). Enzymatic methods for glyco (diversification/randomization) of drugs and small molecules. Natural Product Reports, 28, 1811–1853.
    • (2011) Natural Product Reports , vol.28 , pp. 1811-1853
    • Gantt, R.W.1    Peltier-Pain, P.2    Thorson, J.S.3
  • 36
    • 0025980420 scopus 로고
    • Enzymic synthesis of valienamine glucosides and their antibiotic activity
    • COI: 1:CAS:528:DyaK3MXktV2iu7c%3D
    • Furumoto, T., Yoshika, T., Kamata, K., Kameda, Y., & MatsuiI, K. (1991). Enzymic synthesis of valienamine glucosides and their antibiotic activity. Journal of Antibiotics, 44, 371–373.
    • (1991) Journal of Antibiotics , vol.44 , pp. 371-373
    • Furumoto, T.1    Yoshika, T.2    Kamata, K.3    Kameda, Y.4    MatsuiI, K.5
  • 37
    • 84924030576 scopus 로고    scopus 로고
    • Glycosylated aminocoumarins and methods of preparing and uses of same. Available from. Accessed 30 Jul 2014
    • Glycosylated aminocoumarins and methods of preparing and uses of same. Available from http://www.google.com/patents/EP2627661A1?cl=en. Accessed 30 Jul 2014
  • 38
    • 0029832833 scopus 로고    scopus 로고
    • Dietary quercetin glycosides: antioxidant activity and induction of the anticarcinogenic phase II marker enzyme quinone reductase in Hepalclc7 cells
    • COI: 1:CAS:528:DyaK28XnsVOqurs%3D
    • Williamson, G., Plumb, G. W., Uda, Y., Price, K. R., & Rhodes, M. J. (1996). Dietary quercetin glycosides: antioxidant activity and induction of the anticarcinogenic phase II marker enzyme quinone reductase in Hepalclc7 cells. Carcinogenesis, 17, 2385–2387.
    • (1996) Carcinogenesis , vol.17 , pp. 2385-2387
    • Williamson, G.1    Plumb, G.W.2    Uda, Y.3    Price, K.R.4    Rhodes, M.J.5
  • 40
    • 84901950139 scopus 로고    scopus 로고
    • Assessing acceptor substrate promiscuity of YjiC-mediated glycosylation toward flavonoids
    • COI: 1:CAS:528:DC%2BC2cXhtVWgs7zM
    • Pandey, R. P., Gurung, R. B., Parajuli, P., Koirala, N., Tuoi, L. T., & Sohng, J. K. (2014). Assessing acceptor substrate promiscuity of YjiC-mediated glycosylation toward flavonoids. Carbohydrate Research, 393, 26–31.
    • (2014) Carbohydrate Research , vol.393 , pp. 26-31
    • Pandey, R.P.1    Gurung, R.B.2    Parajuli, P.3    Koirala, N.4    Tuoi, L.T.5    Sohng, J.K.6
  • 41
    • 84888400278 scopus 로고    scopus 로고
    • Enzymatic synthesis of apigenin glucosides by glucosyltransferase (YjiC) from Bacillus licheniformis DSM 13
    • COI: 1:CAS:528:DC%2BC3sXhs1yqsrrL
    • Gurung, R. B., Kim, E. H., Oh, T. J., & Sohng, J. K. (2013). Enzymatic synthesis of apigenin glucosides by glucosyltransferase (YjiC) from Bacillus licheniformis DSM 13. Molecules and Cells, 36, 355–361.
    • (2013) Molecules and Cells , vol.36 , pp. 355-361
    • Gurung, R.B.1    Kim, E.H.2    Oh, T.J.3    Sohng, J.K.4
  • 42
    • 84868628568 scopus 로고    scopus 로고
    • Enzymatic glycosylation of nonbenzoquinone geldanamycin analogs via Bacillus UDP-glycosyltransferase
    • COI: 1:CAS:528:DC%2BC38XhsFyis7rM
    • Wu, C. Z., Jang, J. H., Woo, M., Ahn, J. S., Kim, J. S., & Hong, Y. S. (2012). Enzymatic glycosylation of nonbenzoquinone geldanamycin analogs via Bacillus UDP-glycosyltransferase. Applied and Environmental Microbiology, 78, 7680–7686.
    • (2012) Applied and Environmental Microbiology , vol.78 , pp. 7680-7686
    • Wu, C.Z.1    Jang, J.H.2    Woo, M.3    Ahn, J.S.4    Kim, J.S.5    Hong, Y.S.6


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