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Volumn 10, Issue , 2011, Pages

Synthesis of an antiviral drug precursor from chitin using a saprophyte as a whole-cell catalyst

Author keywords

[No Author keywords available]

Indexed keywords

ANTIVIRUS AGENT; CHITIN; GLUTATHIONE TRANSFERASE; HYBRID PROTEIN; N ACETYLGLUCOSAMINE; N ACETYLNEURAMINIC ACID; RECOMBINANT ENZYME; BACTERIAL PROTEIN; CARRIER PROTEIN; EPIMERASE; HEXOSAMINE; LYASE; N ACETYLMANNOSAMINE; N ACETYLNEURAMINATE SYNTHASE; N ACYL D GLUCOSAMINE 2 EPIMERASE; N-ACETYLMANNOSAMINE; N-ACETYLNEURAMINATE SYNTHASE; N-ACYL-D-GLUCOSAMINE 2-EPIMERASE;

EID: 82655183779     PISSN: None     EISSN: 14752859     Source Type: Journal    
DOI: 10.1186/1475-2859-10-102     Document Type: Article
Times cited : (12)

References (35)
  • 2
    • 0030993576 scopus 로고    scopus 로고
    • Sialic acids as ligands in recognition phenomena
    • Varki A. Sialic acids as ligands in recognition phenomena. Faseb J 1997, 11(4):248-255.
    • (1997) Faseb J , vol.11 , Issue.4 , pp. 248-255
    • Varki, A.1
  • 3
    • 0002044965 scopus 로고
    • Sialic acid as receptor determinant of ortho-and paramyxoviruses
    • NY and London: Plenum Press, Rosenberg A
    • Herrler G, Hausmann J, Klenk HD. Sialic acid as receptor determinant of ortho-and paramyxoviruses. Biology of the Sialic Acids 1995, 315-331. NY and London: Plenum Press, Rosenberg A.
    • (1995) Biology of the Sialic Acids , pp. 315-331
    • Herrler, G.1    Hausmann, J.2    Klenk, H.D.3
  • 4
    • 33646030306 scopus 로고    scopus 로고
    • The other drug for avian flu
    • 3228980, 22148109
    • Tremblay JF. The other drug for avian flu. C&EN 2006, 84(15):33-36. 3228980, 22148109.
    • (2006) C&EN , vol.84 , Issue.15 , pp. 33-36
    • Tremblay, J.F.1
  • 5
    • 0026556267 scopus 로고
    • Preparation of N-acetylneuraminic acid from delipidated egg yolk
    • 10.1007/BF00731701, 1344710
    • Koketsu M, Juneja LR, Kawanami H, Kim M, Yamamoto T. Preparation of N-acetylneuraminic acid from delipidated egg yolk. Glycoconj J 1992, 9(2):70-74. 10.1007/BF00731701, 1344710.
    • (1992) Glycoconj J , vol.9 , Issue.2 , pp. 70-74
    • Koketsu, M.1    Juneja, L.R.2    Kawanami, H.3    Kim, M.4    Yamamoto, T.5
  • 6
    • 0036105953 scopus 로고    scopus 로고
    • Why is sialic acid attracting interest now? Complete enzymatic synthesis of sialic acid with N-acylglucosamine 2-epimerase
    • 10.1263/jbb.93.258, 16233198
    • Maru I, Ohnishi J, Ohta Y, Tsukada Y. Why is sialic acid attracting interest now? Complete enzymatic synthesis of sialic acid with N-acylglucosamine 2-epimerase. J Biosci Bioeng 2002, 93(3):258-265. 10.1263/jbb.93.258, 16233198.
    • (2002) J Biosci Bioeng , vol.93 , Issue.3 , pp. 258-265
    • Maru, I.1    Ohnishi, J.2    Ohta, Y.3    Tsukada, Y.4
  • 7
    • 0025745022 scopus 로고
    • The synthesis and glycosidation of N-acetyl-D-neuraminic acid
    • de Ninno M. The synthesis and glycosidation of N-acetyl-D-neuraminic acid. Synthesis 1991, 8:583-593.
    • (1991) Synthesis , vol.8 , pp. 583-593
    • de Ninno, M.1
  • 8
    • 0032586151 scopus 로고    scopus 로고
    • Alkaline biocatalysis for the direct synthesis of N-acetyl-D-neuraminic acid (Neu5Ac) from N-acetyl-D-glucosamine (GlcNAc)
    • 10.1002/(SICI)1097-0290(1999)66:2<131::AID-BIT6>3.0.CO;2-X, 10567071
    • Blayer S, Woodley JM, Dawson MJ, Lilly MD. Alkaline biocatalysis for the direct synthesis of N-acetyl-D-neuraminic acid (Neu5Ac) from N-acetyl-D-glucosamine (GlcNAc). Biotechnol Bioeng 1999, 66(2):131-136. 10.1002/(SICI)1097-0290(1999)66:2<131::AID-BIT6>3.0.CO;2-X, 10567071.
    • (1999) Biotechnol Bioeng , vol.66 , Issue.2 , pp. 131-136
    • Blayer, S.1    Woodley, J.M.2    Dawson, M.J.3    Lilly, M.D.4
  • 10
    • 0025850357 scopus 로고
    • Enzymatic two step synthesis of N-acetylneuraminic acid in the enzyme membrane reactor
    • Kragl U, Gygax D, Ghisalba O, Wandrey C. Enzymatic two step synthesis of N-acetylneuraminic acid in the enzyme membrane reactor. Angew Chem Int Ed Eng 1991, 30:827-828.
    • (1991) Angew Chem Int Ed Eng , vol.30 , pp. 827-828
    • Kragl, U.1    Gygax, D.2    Ghisalba, O.3    Wandrey, C.4
  • 11
    • 0031874166 scopus 로고    scopus 로고
    • Simple and large-scale production of N-acetylneuraminic acid from N-acetyl-D-glucosamine and pyruvate using N-acyl-D-glucosamine 2-epimerase and N-acetylneuraminate lyase
    • 10.1016/S0008-6215(97)10106-9, 9679278
    • Maru I, Ohnishi J, Ohta Y, Tsukada Y. Simple and large-scale production of N-acetylneuraminic acid from N-acetyl-D-glucosamine and pyruvate using N-acyl-D-glucosamine 2-epimerase and N-acetylneuraminate lyase. Carbohydr Res 1998, 306(4):575-578. 10.1016/S0008-6215(97)10106-9, 9679278.
    • (1998) Carbohydr Res , vol.306 , Issue.4 , pp. 575-578
    • Maru, I.1    Ohnishi, J.2    Ohta, Y.3    Tsukada, Y.4
  • 12
    • 0037070491 scopus 로고    scopus 로고
    • Production of N-acetyl-D-neuraminic acid by coupling bacteria expressing N-acetyl-D-glucosamine 2-epimerase and N-acetyl-D-neuraminic acid synthetase
    • Tabata K, Koizumi S, Endo T, Ozaki A. Production of N-acetyl-D-neuraminic acid by coupling bacteria expressing N-acetyl-D-glucosamine 2-epimerase and N-acetyl-D-neuraminic acid synthetase. Enzyme Microb Techn 2002, 30:327-333.
    • (2002) Enzyme Microb Techn , vol.30 , pp. 327-333
    • Tabata, K.1    Koizumi, S.2    Endo, T.3    Ozaki, A.4
  • 13
    • 34147123274 scopus 로고    scopus 로고
    • Production of N-acetyl-D-neuraminic acid by recombinant whole cells expressing Anabaena sp. CH1 N-acetyl-D-glucosamine 2-epimerase and Escherichia coli N-acetyl-D-neuraminic acid lyase
    • 10.1016/j.jbiotec.2007.01.027, 17349707
    • Lee YC, Chien HC, Hsu WH. Production of N-acetyl-D-neuraminic acid by recombinant whole cells expressing Anabaena sp. CH1 N-acetyl-D-glucosamine 2-epimerase and Escherichia coli N-acetyl-D-neuraminic acid lyase. J Biotechnol 2007, 129(3):453-460. 10.1016/j.jbiotec.2007.01.027, 17349707.
    • (2007) J Biotechnol , vol.129 , Issue.3 , pp. 453-460
    • Lee, Y.C.1    Chien, H.C.2    Hsu, W.H.3
  • 15
    • 0345743697 scopus 로고    scopus 로고
    • The chitinolytic cascade in Vibrios is regulated by chitin oligosaccharides and a two-component chitin catabolic sensor/kinase
    • 10.1073/pnas.0307645100, 327198, 14699052
    • Li X, Roseman S. The chitinolytic cascade in Vibrios is regulated by chitin oligosaccharides and a two-component chitin catabolic sensor/kinase. Proc Natl Acad Sci USA 2004, 101(2):627-631. 10.1073/pnas.0307645100, 327198, 14699052.
    • (2004) Proc Natl Acad Sci USA , vol.101 , Issue.2 , pp. 627-631
    • Li, X.1    Roseman, S.2
  • 16
    • 77955288971 scopus 로고    scopus 로고
    • Chitin research revisited
    • 10.3390/md8071988, 2920538, 20714419
    • Khoushab F, Yamabhai M. Chitin research revisited. Mar Drugs 2010, 8(7):1988-2012. 10.3390/md8071988, 2920538, 20714419.
    • (2010) Mar Drugs , vol.8 , Issue.7 , pp. 1988-2012
    • Khoushab, F.1    Yamabhai, M.2
  • 17
    • 0030200163 scopus 로고    scopus 로고
    • Acid hydrolysis of shrimp-shell wastes and the production of single cell protein from the hydrolysate
    • Ferrer J, Paez G, Marmol Z, Ramones E, Garcia H, Forster C. Acid hydrolysis of shrimp-shell wastes and the production of single cell protein from the hydrolysate. Bioresour Technol 1996, 57:55-60.
    • (1996) Bioresour Technol , vol.57 , pp. 55-60
    • Ferrer, J.1    Paez, G.2    Marmol, Z.3    Ramones, E.4    Garcia, H.5    Forster, C.6
  • 18
    • 0003126088 scopus 로고    scopus 로고
    • Chitinolytic enzymes and theire genes
    • London, UK: Taylor & Francis, Harman GE, Kubicek CP
    • Lorito M. Chitinolytic enzymes and theire genes. Trichoderma & Gliocladium 1998, 2:73-92. London, UK: Taylor & Francis, Harman GE, Kubicek CP.
    • (1998) Trichoderma & Gliocladium , vol.2 , pp. 73-92
    • Lorito, M.1
  • 19
    • 28044450149 scopus 로고    scopus 로고
    • A complete survey of Trichoderma chitinases reveals three distinct subgroups of family 18 chitinases
    • 10.1111/j.1742-4658.2005.04994.x, 16279955
    • Seidl V, Huemer B, Seiboth B, Kubicek CP. A complete survey of Trichoderma chitinases reveals three distinct subgroups of family 18 chitinases. FEBS J 2005, 272(22):5923-5939. 10.1111/j.1742-4658.2005.04994.x, 16279955.
    • (2005) FEBS J , vol.272 , Issue.22 , pp. 5923-5939
    • Seidl, V.1    Huemer, B.2    Seiboth, B.3    Kubicek, C.P.4
  • 22
    • 0142090514 scopus 로고    scopus 로고
    • Enhanced enzymatic hydrolysis of langostino shell chitin with mixtures of enzymes from bacterial and fungal sources
    • 10.1016/S0008-6215(03)00269-6, 12932365
    • Donzelli BG, Ostroff G, Harman GE. Enhanced enzymatic hydrolysis of langostino shell chitin with mixtures of enzymes from bacterial and fungal sources. Carbohydr Res 2003, 338(18):1823-1833. 10.1016/S0008-6215(03)00269-6, 12932365.
    • (2003) Carbohydr Res , vol.338 , Issue.18 , pp. 1823-1833
    • Donzelli, B.G.1    Ostroff, G.2    Harman, G.E.3
  • 23
    • 6344233434 scopus 로고    scopus 로고
    • Characterization of N-acetylneuraminic acid synthase isoenzyme 1 from Campylobacter jejuni
    • 1134046, 15200387
    • Sundaram AK, Pitts L, Muhammad K, Wu J, Betenbaugh M, Woodard RW, Vann WF. Characterization of N-acetylneuraminic acid synthase isoenzyme 1 from Campylobacter jejuni. Biochem J 2004, 383(Pt 1):83-89. 1134046, 15200387.
    • (2004) Biochem J , vol.383 , Issue.PART 1 , pp. 83-89
    • Sundaram, A.K.1    Pitts, L.2    Muhammad, K.3    Wu, J.4    Betenbaugh, M.5    Woodard, R.W.6    Vann, W.F.7
  • 24
    • 33845760011 scopus 로고    scopus 로고
    • Engineering of a sialic acid synthesis pathway in transgenic plants by expression of bacterial Neu5Ac-synthesizing enzymes
    • 10.1111/j.1467-7652.2006.00211.x, 17207253
    • Paccalet T, Bardor M, Rihouey C, Delmas F, Chevalier C, D'Aoust MA, Faye L, Vezina L, Gomord V, Lerouge P. Engineering of a sialic acid synthesis pathway in transgenic plants by expression of bacterial Neu5Ac-synthesizing enzymes. Plant Biotechnol J 2007, 5(1):16-25. 10.1111/j.1467-7652.2006.00211.x, 17207253.
    • (2007) Plant Biotechnol J , vol.5 , Issue.1 , pp. 16-25
    • Paccalet, T.1    Bardor, M.2    Rihouey, C.3    Delmas, F.4    Chevalier, C.5    D'Aoust, M.A.6    Faye, L.7    Vezina, L.8    Gomord, V.9    Lerouge, P.10
  • 25
    • 71349086576 scopus 로고    scopus 로고
    • An accurate normalization strategy for RT-qPCR in Hypocrea jecorina (Trichoderma reesei)
    • 10.1016/j.jbiotec.2009.10.012, 19861137
    • Steiger MG, Mach RL, Mach-Aigner AR. An accurate normalization strategy for RT-qPCR in Hypocrea jecorina (Trichoderma reesei). J Biotechnol 2010, 145(1):30-37. 10.1016/j.jbiotec.2009.10.012, 19861137.
    • (2010) J Biotechnol , vol.145 , Issue.1 , pp. 30-37
    • Steiger, M.G.1    Mach, R.L.2    Mach-Aigner, A.R.3
  • 26
    • 0029839467 scopus 로고    scopus 로고
    • Molecular evidence that the asexual industrial fungus Trichoderma reesei is a clonal derivative of the ascomycete Hypocrea jecorina
    • 10.1073/pnas.93.15.7755, 38820, 8755548
    • Kuhls K, Lieckfeldt E, Samuels GJ, Kovacs W, Meyer W, Petrini O, Gams W, Borner T, Kubicek CP. Molecular evidence that the asexual industrial fungus Trichoderma reesei is a clonal derivative of the ascomycete Hypocrea jecorina. Proc Natl Acad Sci U S A 1996, 93(15):7755-7760. 10.1073/pnas.93.15.7755, 38820, 8755548.
    • (1996) Proc Natl Acad Sci U S A , vol.93 , Issue.15 , pp. 7755-7760
    • Kuhls, K.1    Lieckfeldt, E.2    Samuels, G.J.3    Kovacs, W.4    Meyer, W.5    Petrini, O.6    Gams, W.7    Borner, T.8    Kubicek, C.P.9
  • 27
    • 39749127156 scopus 로고    scopus 로고
    • Role of Ace2 (Activator of Cellulases 2) within the xyn2 transcriptosome of Hypocrea jecorina
    • 10.1016/j.fgb.2007.08.005, 17920314
    • Stricker AR, Trefflinger P, Aro N, Penttilä M, Mach RL. Role of Ace2 (Activator of Cellulases 2) within the xyn2 transcriptosome of Hypocrea jecorina. Fungal Genet Biol 2008, 45(4):436-445. 10.1016/j.fgb.2007.08.005, 17920314.
    • (2008) Fungal Genet Biol , vol.45 , Issue.4 , pp. 436-445
    • Stricker, A.R.1    Trefflinger, P.2    Aro, N.3    Penttilä, M.4    Mach, R.L.5
  • 28
    • 0022054102 scopus 로고
    • Applications of cellulases
    • Mandels M. Applications of cellulases. Biochem Soc Trans 1985, 13(2):414-416.
    • (1985) Biochem Soc Trans , vol.13 , Issue.2 , pp. 414-416
    • Mandels, M.1
  • 29
    • 0001194009 scopus 로고
    • Plant and Bacterial Chitinases Differ in Antifungal Activity
    • Roberts WK, Selitrennikoff CP. Plant and Bacterial Chitinases Differ in Antifungal Activity. J Gen Microbiol 1988, 134:169-176.
    • (1988) J Gen Microbiol , vol.134 , pp. 169-176
    • Roberts, W.K.1    Selitrennikoff, C.P.2
  • 30
    • 0027947285 scopus 로고
    • Transformation of Trichoderma reesei based on hygromycin B resistance using homologous expression signals
    • 10.1007/BF00351679, 8082210
    • Mach RL, Schindler M, Kubicek CP. Transformation of Trichoderma reesei based on hygromycin B resistance using homologous expression signals. Curr Genet 1994, 25(6):567-570. 10.1007/BF00351679, 8082210.
    • (1994) Curr Genet , vol.25 , Issue.6 , pp. 567-570
    • Mach, R.L.1    Schindler, M.2    Kubicek, C.P.3
  • 31
    • 0025321953 scopus 로고
    • The development of a heterologous transformation system for the cellulolytic fungus Trichoderma reesei based on a pyrG-negative mutant strain
    • 10.1007/BF00321118, 2245476
    • Gruber F, Visser J, Kubicek CP, de Graaff LH. The development of a heterologous transformation system for the cellulolytic fungus Trichoderma reesei based on a pyrG-negative mutant strain. Curr Genet 1990, 18(1):71-76. 10.1007/BF00321118, 2245476.
    • (1990) Curr Genet , vol.18 , Issue.1 , pp. 71-76
    • Gruber, F.1    Visser, J.2    Kubicek, C.P.3    de Graaff, L.H.4
  • 32
    • 79251636256 scopus 로고    scopus 로고
    • Transformation system for Hypocrea jecorina (Trichoderma reesei) that favors homologous integration and employs reusable bidirectionally selectable markers
    • 10.1128/AEM.02100-10, 3019734, 21075888
    • Steiger MG, Vitikainen M, Uskonen P, Brunner K, Adam G, Pakula T, Penttilä M, Saloheimo M, Mach RL, Mach-Aigner AR. Transformation system for Hypocrea jecorina (Trichoderma reesei) that favors homologous integration and employs reusable bidirectionally selectable markers. Appl Environ Microbiol 2011, 77(1):114-121. 10.1128/AEM.02100-10, 3019734, 21075888.
    • (2011) Appl Environ Microbiol , vol.77 , Issue.1 , pp. 114-121
    • Steiger, M.G.1    Vitikainen, M.2    Uskonen, P.3    Brunner, K.4    Adam, G.5    Pakula, T.6    Penttilä, M.7    Saloheimo, M.8    Mach, R.L.9    Mach-Aigner, A.R.10
  • 33
    • 0030750194 scopus 로고    scopus 로고
    • Purification and characterization of the Escherichia coli K1 neuB gene product N-acetylneuraminic acid synthetase
    • 10.1093/glycob/7.5.697, 9254051
    • Vann WF, Tavarez JJ, Crowley J, Vimr E, Silver RP. Purification and characterization of the Escherichia coli K1 neuB gene product N-acetylneuraminic acid synthetase. Glycobiology 1997, 7(5):697-701. 10.1093/glycob/7.5.697, 9254051.
    • (1997) Glycobiology , vol.7 , Issue.5 , pp. 697-701
    • Vann, W.F.1    Tavarez, J.J.2    Crowley, J.3    Vimr, E.4    Silver, R.P.5
  • 34
    • 85008137144 scopus 로고
    • 1,2-Diamino-4,5-methylenedioxybenzene as a Highly Sensitive Fluorogenic Reagent for a-Keto Acids
    • Nakamura M, Hara S, Yamaguchi M, Takemori Y, Ohkura Y. 1,2-Diamino-4,5-methylenedioxybenzene as a Highly Sensitive Fluorogenic Reagent for a-Keto Acids. Chem Pharm Bull (Tokyo) 1987, 35(2):687-692.
    • (1987) Chem Pharm Bull (Tokyo) , vol.35 , Issue.2 , pp. 687-692
    • Nakamura, M.1    Hara, S.2    Yamaguchi, M.3    Takemori, Y.4    Ohkura, Y.5
  • 35
    • 77953340995 scopus 로고    scopus 로고
    • Basic rules for the interpretation of atmospheric pressure ionization mass spectra of small molecules
    • 10.1016/j.chroma.2010.02.049, 20303090
    • Holcapek M, Jirasko R, Lisa M. Basic rules for the interpretation of atmospheric pressure ionization mass spectra of small molecules. J Chromatogr A 2010, 1217(25):3908-3921. 10.1016/j.chroma.2010.02.049, 20303090.
    • (2010) J Chromatogr A , vol.1217 , Issue.25 , pp. 3908-3921
    • Holcapek, M.1    Jirasko, R.2    Lisa, M.3


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