Aeromonas hydrophila strains as biocatalysts for transglycosylation

Microbial transglycosylation is useful as a green alternative in the preparation of purine nucleosides and analogues, especially for those that display pharmacological activities. In a search for new transglycosylation biocatalysts, two Aeromonas hydrophila strains were selected. The substrate speci...

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Autor principal: Nbile, M.
Otros Autores: Terreni, M., Lewkowicz, E., Iribarren, A.M
Formato: Capítulo de libro
Lenguaje:Inglés
Publicado: 2010
Acceso en línea:Registro en Scopus
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LEADER 08528caa a22009857a 4500
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024 7 |2 scopus  |a 2-s2.0-78650598107 
024 7 |2 cas  |a didanosine, 69655-05-6; ribavirin, 36791-04-5 
040 |a Scopus  |b spa  |c AR-BaUEN  |d AR-BaUEN 
030 |a BOBOE 
100 1 |a Nbile, M. 
245 1 0 |a Aeromonas hydrophila strains as biocatalysts for transglycosylation 
260 |c 2010 
270 1 0 |m Lewkowicz, E.; Biotransformation Laboratory, Universidad Nacional de Quilmes, R. S. Pea 352, (1876) Bernal, Buenos Aires, Argentina; email: elewko@unq.edu.ar 
506 |2 openaire  |e Política editorial 
504 |a Agarwal, S., Gopal, K., Upadhyaya, T., Dixit, A., Biochemical and functional characterization of UDP-galactose 4-epimerase from Aeromonas hydrophila (2007) Biochim Biophys Acta, 1774, pp. 828-837 
504 |a Bentancor, L., Trelles, J., Nobile, M., Lewkowicz, E.S., Iribarren, A.I., Benzimidazole as deazapurine analogue for microbial transglycosylation (2004) J Mol Catal B: Enzym, 29, pp. 3-7 
504 |a De Clercq, E., New developments in anti-HIV chemotherapy (2002) Biochim Biophys Acta, 1587, pp. 258-275 
504 |a De Clercq, E., Antiviral drug discovery and development: Where chemistry meets with biomedicine (2005) Antivir Res, 67, pp. 56-75 
504 |a Gish, R.G., Treating HCV with ribavirin analogues and ribavirin-like molecules (2006) J Antimicrob Chemoth, 57, pp. 8-13 
504 |a Iaskovich, G.A., Iakovleva, E.P., Microbiological synthesis of virazole by immobilized cells (1999) Prikl Biokhim Mikrobiol, 35, pp. 146-149 
504 |a Imada, A., Igarasi, S., Ribosyl and deoxyribosyl transfer by bacterial enzyme systems (1967) J Bacteriol, 94, pp. 1551-1559 
504 |a Kitos, T.E., Tyrrell, D.L.J., Intracellular metabolism of 2 ',3 '-dideoxynucleosides in duck hepatocyte primary cultures (1995) Biochem Pharmacol, 49, pp. 1291-1302 
504 |a Konstantinova, I.D., Esipov, R.S., Muraveva, T.I., Taran, S.A., Verevkina, K.N., Gurevich, A.I., Feofanov, S.A., Miroshnikov, A.I., (2004) Method for Preparing 1-/?-D-ribofuranosyl-1,2,4-triazole-3-carboxamide (Ribavirin)., , Patent number RU2230118 
504 |a Lewkowicz, E.S., Iribarren, A.M., Nucleoside phosphorylases (2006) Curr Org Chem, 10, pp. 1197-1215 
504 |a Li, N., Smith, T.J., Zong, M.-H., Biocatalytic transformation of nucleoside derivatives (2010) Biotechnol Adv, 28, pp. 348-366 
504 |a Medici, R., Lewkowicz, E., Iribarren, A.M., Microbial synthesis of 2,6-diaminopurine nucleosides (2006) J Mol Catal B: Enzym, 39, pp. 40-44 
504 |a Medici, R., Lewkowicz, E., Iribarren, A.M., Arthrobacter oxydans as biocatalyst for purine deamination (2008) FEMS Microbiol Lett, 289, pp. 20-26 
504 |a Murakami, K., Shirasaka, T., Yoshioka, H., Kojima, E., Aoki, S., Ford, H., Driscoll, J.S., Mitsuya, H., Escherichia coli mediated biosynthesis and in vitro anti-HIV activity of lipophilic 6-halo-2 ',3 '-dideoxypurine nucleosides (1991) J Med Chem, 34, pp. 1606-1612 
504 |a Prasad, A.K., Trikha, S., Parmar, V.S., Nucleoside synthesis mediated by glycosyl transferring enzymes (1999) Bioorg Chem, 27, pp. 135-154 
504 |a Sashiwa, H., Fujishima, S., Yaman, N., Kawasaki, N., Nakayama, A., Muraki, E., Hiraga, K., Aiba, S., Production of N-acetyl-D-glucosamine from α-chitin by crude enzymes from Aeromonas hydrophila H-2330 (2002) Carbohydr Res, 337, pp. 761-763 
504 |a Shirae, H., Yokozeki, K., Purifications and properties of orotidine-phosphorolyzing enzyme and purine nucleoside phosphorylase from Erwinia carotovora AJ 2992 (1991) Agric Biol Chem, 55, pp. 1849-1857 
504 |a Shirae, H., Yokozeki, K., Purification and properties of purine nucleoside phosphorylase from Brevibacterium acetyli-cum ATCC954 (1991) Agric Biol Chem, 55, pp. 493-499 
504 |a Shiragami, H., Irie, Y., Yasuda, N., (2001) Process for Produc Ing and Purifying 2 ',3 '-dideoxynucleosides, and Process for Producing 2 ',3 '-dideoxy-2 ',3 '-didehydronucleosides, , US Patent 6306647 
504 |a Trelles, J.A., Bentancor, L., Schoijet, A., Porro, S., Lewkowicz, E.S., Sinisterra, J.V., Iribarren, A.M., Immobilised Escherichia coli BL21 as a catalyst for the synthesis of adenine and hypoxan-thine nucleosides (2004) Chem Biodiversity, 1, pp. 380-388 
504 |a Utagawa, T., Enzymatic preparation of nucleoside antibiot-ics (1999) J Mol Catal B: Enzym, 6, pp. 215-222 
504 |a Witkowski, J., Robins, R., Sidwell, R., Simon, L., Design, synthesis, and broad spectrum antiviral activity of 1-ß-D-ribofuranosyl-1,2,4-triazole-3-carboxamide and related nucleo-sides (1972) J Med Chem, 15, pp. 1150-1154 
504 |a Wu, J.Z., Larson, G., Walker, H., Shim, J.H., Hong, Z., Phospho-rylation of ribavirin and viramidine by adenosine kinase and cytosolic 5 '-nucleotidase II: Implications for ribavirin meta-bolism in erythrocytes (2005) Antimicrob Agents Chemother, 49, pp. 2164-2171 
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520 3 |a Microbial transglycosylation is useful as a green alternative in the preparation of purine nucleosides and analogues, especially for those that display pharmacological activities. In a search for new transglycosylation biocatalysts, two Aeromonas hydrophila strains were selected. The substrate specificity of both micro-organisms was studied and, as a result, several nucleoside analogues have been prepared. Among them, ribavirin, a broad spectrum antiviral, and the well-known anti HIV didanosine, were prepared, in 77 and 62% yield using A. hydrophila CECT 4226 and A. hydrophila CECT 4221, respectively. In order to scale-up the processes, the reaction conditions, product purification and biocatalyst preparation were analyzed and optimized. © 2010 Informa UK, Ltd.  |l eng 
536 |a Detalles de la financiación: Universidad Nacional de Quilmes 
536 |a Detalles de la financiación: Declaration of interest: This work was supported by Universidad Nacional de Quilmes and Secretar í a de Ciencia y T é cnica de la Naci ó n, Argentina The authors report no conflicts of interest. The authors alone are responsible for the content and writing of the paper. 
593 |a Biotransformation Laboratory, Universidad Nacional de Quilmes, R. S. Pea 352, (1876) Bernal, Buenos Aires, Argentina 
593 |a Italian Biocatalysis Center, PBL Dipartimento di Chimica Farmaceutica, Universit Degli Studi, via Taramelli 12, I-27100, Pavia, Italy 
593 |a INGEBI, CONICET, Vuelta de Obligado 2490, (1428) Buenos Aires, Argentina 
690 1 0 |a AEROMONAS HYDROPHILA 
690 1 0 |a DIDANOSINE 
690 1 0 |a MICROBIAL TRANSGLYCOSYLATION 
690 1 0 |a RIBAVIRIN 
690 1 0 |a WHOLE CELL BIOCATALYSTS 
690 1 0 |a AEROMONAS HYDROPHILA 
690 1 0 |a DIDANOSINE 
690 1 0 |a MICROBIAL TRANSGLYCOSYLATION 
690 1 0 |a RIBAVIRIN 
690 1 0 |a WHOLE CELL BIOCATALYSTS 
690 1 0 |a AMIDES 
690 1 0 |a BIOMOLECULES 
690 1 0 |a ENZYMES 
690 1 0 |a DIDANOSINE 
690 1 0 |a RIBAVIRIN 
690 1 0 |a AEROMONAS HYDROPHILA 
690 1 0 |a ARTICLE 
690 1 0 |a BIOTRANSFORMATION 
690 1 0 |a DRUG ISOLATION 
690 1 0 |a DRUG PURIFICATION 
690 1 0 |a DRUG STRUCTURE 
690 1 0 |a DRUG SYNTHESIS 
690 1 0 |a GLYCOSYLATION 
690 1 0 |a HIGH PERFORMANCE LIQUID CHROMATOGRAPHY 
690 1 0 |a NONHUMAN 
690 1 0 |a AEROMONAS HYDROPHILA 
700 1 |a Terreni, M. 
700 1 |a Lewkowicz, E. 
700 1 |a Iribarren, A.M. 
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