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Abstract:

The anomers methyl 2,3,5-tri-O-acetyl-α-d-ribofuranoside and methyl 2,3,5-tri-O-acetyl-β-d-ribofuranoside showed a different behaviour in the Candida antarctica B lipase-catalysed alcoholysis. While the enzymatic deprotection of the former proceeded regioselectively affording methyl 2,3-di-O-acetyl-α-d-ribofuranoside in 81% yield in 3 h at 45°C showing no further transformation, the alcoholysis of the β-diasteromer was less selective. For this anomer, mixtures of partially acetylated products were formed, but contrasting to the α epimer, full deacetylated methyl β-d-ribofuranoside was quantitatively formed at long reaction times (5 days). © 2005 Elsevier B.V. All rights reserved.

Registro:

Documento: Artículo
Título:Deprotection of peracetylated methyl D-ribosides through enzymatic alcoholysis: Different recognition of the anomers
Autor:Iñigo, S.; Porro, M.T.; Montserrat, J.M.; Iglesias, L.E.; Iribarren, A.M.
Filiación:Centro de Estudios e Investigaciones, Universidad Nacional de Quilmes, Roque Sáenz Peña 180, Provincia de Buenos Aires, Argentina
INGEBI (CONICET), Vuelta de Obligado 2490, 1428 Buenos Aires, Argentina
Instituto de Ciencias, Universidad Nacional de General Sarmiento, J.M. Gutiérrez 1150, Provincia de Buenos Aires, Argentina
Palabras clave:Deacetylation; Enzymatic alcoholysis; Lipases; Regioselectivity; Ribosides; Acetylation; Alcohols; Catalysis; Enzymes; Stereochemistry; Anomers; Deacetylation; Enzymatic alcoholysis; Regioselectivity; Isomers; furan derivative; lipase B; methyl 2,3 di o acetyl alpha dextro ribofuranoside; methyl 2,3,5 tri o acetyl beta dextro ribofuranoside; methyl 2.3.5 tri o acetyl alpha dextro ribofuranoside; methyl dextro riboside; unclassified drug; alcoholysis; article; biocatalyst; Candida antarctica; catalysis; deprotection reaction; diastereoisomer; enzyme mechanism; stereochemistry; temperature sensitivity; Candida antarctica
Año:2005
Volumen:35
Número:1-3
Página de inicio:70
Página de fin:73
DOI: http://dx.doi.org/10.1016/j.molcatb.2005.05.010
Título revista:Journal of Molecular Catalysis B: Enzymatic
Título revista abreviado:J. Mol. Catal. B Enzym.
ISSN:13811177
CODEN:JMCEF
Registro:https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_13811177_v35_n1-3_p70_Inigo

Referencias:

  • Davies, B.G., (2002) Chem. Rev., 102, p. 579
  • Gruner, S.A.W., Locardi, E., Lohof, E., Kessler, H., (2002) Chem. Rev., 102, p. 491
  • Park, O.J., Kim, D.Y., Dordick, J.S., (2000) Biotechnol. Bioeng., 70, p. 208
  • Bornsheuer, U., Kazlauskas, R., (1999) Hydrolases in Organic Chemistry, , Wiley/VCH Weinheim
  • Kadereit, D., Waldmann, H., (2001) Chem. Rev., 101, p. 3367
  • La Ferla, B., (2002) Monatsh. Chem., 133, p. 351
  • Prasad, A.K., Roy, S., Kumar, R., Kalra, N., Wengel, J., Olsen, C.E., Cholli, A.L., Parmar, V.S., (2003) Tetrahedron, 59, p. 1333
  • Mastihubova, M., Szemesova, J., Biely, P., (2003) Tetrahedron Lett., 44, p. 1671
  • Hennen, W.J., Sweers, H.M., Wang, Y.F., Wong, C.H., (1988) J. Org. Chem., 53, p. 4939
  • Fernandez-Lorente, G., Palomo, J.M., Cocca, J., Mateo, J.C., Moro, P., Terreni, M., Fernandez-Lafuente, R., Guisan, J.M., (2003) Tetrahedron, 59, p. 5705
  • Chien, T.C., Chern, J.W., (2004) Carbohydr. Res., 339, p. 1215
  • Iglesias, L.E., Zinni, M.A., Gallo, M., Iribarren, A.M., (2000) Biotechnol. Lett., 22, p. 361
  • Roncaglia, D.I., Schmidt, A.M., Iglesias, L.E., Iribarren, A.M., (2001) Biotechnol. Lett., 23, p. 1439
  • Zinni, M.A., Iglesias, L.E., Iribarren, A.M., (2002) Biotechnol. Lett., 24, p. 979
  • Zinni, M.A., Rodríguez, S.D., Pontiggia, R.M., Montserrat, J.M., Iglesias, L.E., Iribarren, A.M., (2004) J. Mol. Catal. B: Enzymatic, 29, p. 129
  • Nicolosi, G., Spatafora, C., Tringali, C., (1999) Tetrahedron: Asymmetry, 10, p. 2891
  • Shi, Z.D., Yang, B.H., Wu, Y.L., (2002) Tetrahedron, 58, p. 3287
  • Pulido, R., Gotor, V., (1993) J. Chem. Soc., Perkin Trans., 1, p. 589
  • Prasad, A.K., Soerensen, M.D., Parmar, V.S., Wengel, J., (1995) Tetrahedron Lett., 36, p. 6163

Citas:

---------- APA ----------
Iñigo, S., Porro, M.T., Montserrat, J.M., Iglesias, L.E. & Iribarren, A.M. (2005) . Deprotection of peracetylated methyl D-ribosides through enzymatic alcoholysis: Different recognition of the anomers. Journal of Molecular Catalysis B: Enzymatic, 35(1-3), 70-73.
http://dx.doi.org/10.1016/j.molcatb.2005.05.010
---------- CHICAGO ----------
Iñigo, S., Porro, M.T., Montserrat, J.M., Iglesias, L.E., Iribarren, A.M. "Deprotection of peracetylated methyl D-ribosides through enzymatic alcoholysis: Different recognition of the anomers" . Journal of Molecular Catalysis B: Enzymatic 35, no. 1-3 (2005) : 70-73.
http://dx.doi.org/10.1016/j.molcatb.2005.05.010
---------- MLA ----------
Iñigo, S., Porro, M.T., Montserrat, J.M., Iglesias, L.E., Iribarren, A.M. "Deprotection of peracetylated methyl D-ribosides through enzymatic alcoholysis: Different recognition of the anomers" . Journal of Molecular Catalysis B: Enzymatic, vol. 35, no. 1-3, 2005, pp. 70-73.
http://dx.doi.org/10.1016/j.molcatb.2005.05.010
---------- VANCOUVER ----------
Iñigo, S., Porro, M.T., Montserrat, J.M., Iglesias, L.E., Iribarren, A.M. Deprotection of peracetylated methyl D-ribosides through enzymatic alcoholysis: Different recognition of the anomers. J. Mol. Catal. B Enzym. 2005;35(1-3):70-73.
http://dx.doi.org/10.1016/j.molcatb.2005.05.010