Organic compounds -- part of the class 532-570 series – Organic compounds – Carbohydrates or derivatives
Reexamination Certificate
2000-06-19
2002-10-15
Peselev, Elli (Department: 1623)
Organic compounds -- part of the class 532-570 series
Organic compounds
Carbohydrates or derivatives
C536S017200, C536S017500, C536S017600, C536S018100, C549S385000, C549S387000, C549S388000, C549S510000, C549S511000
Reexamination Certificate
active
06465625
ABSTRACT:
BACKGROUND OF THE INVENTION
1. Field of the Invention
This invention is in the field of biologically active compounds.
2. Discussion of the Background
The prior art is replete with examples of chemically, microbially, or enzymatically synthesizing compounds with biological activity. The goal of these efforts is the discovery of new and improved pharmaceutical compounds.
The discovery of new pharmaceutical compounds is for the most part a trial and error process. So many diverse factors constitute an effective pharmaceutical compound that it is extremely difficult to reduce the discovery process to a systematic approach. Typically, thousands of organic compounds must be isolated from biological sources or chemically synthesized and tested before a pharmaceutical compound is found.
Synthesizing and testing new compounds for biological activity, which is the first step in identifying a new synthetic drug, is a time consuming and expensive undertaking. Typically, compounds must by synthesized, purified, tested and quantitatively compared to other compounds in order to identify active compounds or identify compounds with optimal activity. The synthesis of new compounds is accomplished for the most part using standard chemical methods. Such methods provide for the synthesis of virtually any type of organic compound; however, because chemical reactions are non-specific, these syntheses require numerous steps and multiple purifications before a final compound is produced and ready for testing.
New biological and chemical approaches have recently been developed which provide for the synthesis and screening of large libraries of small peptides and oligonucleotides. These methods provide for the synthesis of a broad range of chemical compounds and provide the means to potentially identify biologically active compounds. The chemistries for synthesizing such large numbers of these natural and non-naturally occurring polymeric compounds is complicated, but manageable because each compound is synthesized with the same set of chemical protocols, the difference being the random order in which amino acids or nucleotides are introduced into the reaction sequence.
The prior art Is replete with examples showing enzymatic conversion of non-physiological substances under many conditions.
REFERENCES DEMONSTRATING THAT ENZYME SPECIFICITY CAN BE CHANGED/TAILORED
1. Zaks, A. and Klibanov, A. M. Substrate specificity of enzymes in organic solvents vs. water is reversed. Journal of the American Chemical Society 108 2767-2768, 1986.
2. Ferjancic, A., Puigserver, A. and Gaertner, H. Unusual specificity of PEG-modified thermolysin in peptide synthesis catalyzed in organic solvents. Biotechnology Letters 10 (2) 101-106, 1988.
3. Nasri, M. and Thomas, D. Increase of the potentialities of restriction endonucleases by specificity relaxation in the presence of organic solvents. Ann. N.Y. Acad. Sci. 542 255-265, 1988.
4. Stahl, M., Mansson, M. O. and Mosbach, K. The synthesis of a D-amino acid ester in an organic media with chymotrypsin modified by a bio-imprinting procedure. Biotechnology Letters 12 (3) 161-166, 1990.
5. Stahl, M., Jeppsson-Wistrand, U., Mansson, M. O. and Mosbach, K. Induced stereoselectivity and substrate selectivity of bio-imprinted a-chymotrypsin in anhydrous organic media. Journal of the American Chemical Society 113 (24) 9366-9368, 1991.
6. Gololobov, M. Y., Voyushina, T. L., Stepanov, V. M. and Adlercreutz, P. Organic solvent changes the chymotrypsin specificity with respect to nucleophiles. FEBS Letters 307 (3) 309-312, 1992.
7. Hertmanni, P., Pourplanche, C. and Larreta-Garde, V. Orientation of enzyme catalysis and specificity by water-soluble additives. Ann. New York Acad. Sci. (Enzyme Eng. XI, D. S. Clark, D. A. Estell, eds) 672 329-335, 1992.
8. Cabezas, M. J., del Campo, C., Llama, E., Sinisterra, J. V. and Gaertner, H. Organic reactions catalyzed by modified enzymes. 1. Alteration of the substrate specificity of a-chymotrypsin by the modification process. Journal of Molecular Catalysis 71 (2) 261-278, 1992.
9. Nagashima, T., Watanabe, A. and Kise, H. Peptide synthesis by proteases in organic solvents: medium effect on substrate specificity. Enzyme and Microbial Technology 14 (10) 842-847, 1992.
10. Parida, S. and Dordick, J. S. Tailoring lipase specificity by solvent and substrate chemistries, J. Org. Chem. 58 (12) 3238-3244, 1993.
11. Tawaki, S. and Klibanov, A. M. Chemoselectivity of enzymes in anhydrous media is strongly solvent dependent. Biocatalysis 8 (1) 3-19, 1993.
12. Wescott, C. F. and Klibanov, A. M. Solvent variation inverts substrate specificity of an enzyme. JACS 115 (5) 1629-1631, 1993.
REFERENCES DEMONSTRATING THAT ENZYME ENANTIOSELECTIVITY CAN BE CHANGED/TAILORED
1. Sakurai, T., Margolin, A. L., Russell, A. J. and Klibanov, A. M. Control of enzyme enantioselectivity by the reaction medium. Journal of the American Chemical Society 110 (21) 7236-7237, 1988.
2. Fitzpatrick, P. A. and Klibanov, A. M. How can the solvent affect enzyme enantioselectivity? Journal of the American Chemical Society 113 (8) 3166-3171, 1991.
3. Hult, K. and Norin, T. Enantioselectivity of some lipases—control and prediction. Pure and Applied Chemistry 64 (8) 1129-1134, 1992.
4. Miyazawa, T., Kurita, S., Ueji, S., Yamada, T. and Kuwata, S. Resolution of racemic carboxylic acids via the lipase-catalyzed irreversible transesterification using vinyl esters—effects of alcohols as nucleophiles and organic solvents on enantioselectivity. Biotechnology Letters 14 (10) 941-946, 1992.
5. Tawaki, S. and Klibanov, A. M. Inversion of enzyme enantioselectivity mediated by the solvent. Journal of the American Chemical Society 114 (5) 1882-1884, 1992.
6. Ueji, S., Fujino, R., Okubo, N., Miyazawa, T., Kurita, S., Kitadani, M. and Muromatsu, A. Solvent-induced inversion of enantioselectivity in lipase-catalyzed esterification of 2-phenoxypropionic acids. Biotechnology Letters 14 (3) 163-168, 1992.
7. Terradas, F., Testonhenry, M., Fitzpatrick, P. A. and Klibanov, A. M. Marked dependence of enzyme prochiral selectivity on the solvent. Journal of the American Chemical Society 115 (2) 390-396, 1993.
8. Herradon, B. Biocatalytic synthesis of chiral polyoxygenated compounds: effect of the solvent on the enantioselectivity of lipase catalyzed transesterifications in organic solvents. Synlett 2 108-110, 1993.
REFERENCES DEMONSTRATING THE ABILITY OF ENZYMES TO CONVERT UNNATURAL SUBSTRATES
1. Bianchi, D., Cesti, P., Golini, P., Spezia, S., Garavaglia, C. and Mirenna, L. Enzymatic preparation of optically active fungicide intermediates in aqueous and in organic media. Pure and Applied Chemistry 64 (8) 1073-1078, 1992.
2. Natoli, M., Nicolosi, G. and Piattelli, M. Regioselective alcoholysis of flavonoid acetates with lipase in an organic solvent. Journal of Organic Chemistry 57 (21) 5776-5778, 1992.
3. Izumi, T., Tamura, F. and Sasaki, K. Enzymatic kinetic resolution of <4> (1,2)ferrocenophane derivatives. Bulletin of the Chemical Society of Japan 65 (10) 2784-2788, 1992.
4. Miyazawa, T., Mio, M., Watanabe, Y., Yamada, T. and Kuwata, S. Lipase-catalyzed transesterification procedure for the resolution of non-protein amino acids. Biotechnology Letters 14 (9) 789-794, 1992.
5. Murata, M., Uchida, H. and Achiwa, K. Lipase-catalyzed enantioselective synthesis of optically active mephobarbital, hexobarbital and febarbamate. Chemical-Pharmaceutical Bulletin 40 (10) 2605-2609, 1992.
6. Johnson, C. R., Golebiowski, A. and Steensma, D. H. Enzymatic asymmetrization in organic media—synthesis of unnatural glucose from cycloheptatriene. Journal of the American Chemical Society 114 (24) 9414-9418, 1992.
7. Cruces, M. A., Otero, C., Bernabe, M., Martinlomas, M. and Ballesteros, A. Enzymatic preparation of acylated sucroses. Ann. New York Acad. Sci. (Enzyme Eng. XI, D. S. Clark, D. A. Estell, eds) 672 436-443, 1992.
8. Tanaka, A., Fukui, T., Uejima, A., Zong, M. H. and Kawamoto, T. Bioconversion of nonnatural organic compounds—esterification and dehydrogenation of organosilicon compounds. Ann. New York Acad. Sci (Enzyme Eng
Clark Douglas S.
Dordick Jonathan S.
Khmelnitsky Yuri L.
Michels Peter C.
Albany Molecular Research, Inc.
Nixon & Peabody LLP
Peselev Elli
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