Rationally designed polysaccharide lyases derived from...

Drug – bio-affecting and body treating compositions – Enzyme or coenzyme containing – Transferases

Reexamination Certificate

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C435S232000, C435S252300, C435S320100, C536S023200

Reexamination Certificate

active

06962699

ABSTRACT:
The invention relates to rationally designed polysaccharide lyases and uses thereof. In particular, the invention relates to modified chondroitinase B. The modified chondroitinase B enzymes of the invention are useful for a variety of purposes, including cleaving and sequencing polysaccharides such as glycosaminoglycans (GAGs) as well as removing polysaccharides from a solution. The invention also includes methods of inhibiting anticoagulant activity, inhibiting angiogenesis, treating cancer, and inhibiting maternal malarial infection.

REFERENCES:
patent: 5198355 (1993-03-01), Kikuchi et al.
patent: 5498536 (1996-03-01), Khandke
patent: 5525500 (1996-06-01), Khandke et al.
patent: 5668274 (1997-09-01), Petitou et al.
patent: 5716617 (1998-02-01), Khandke et al.
patent: 5741692 (1998-04-01), Khandke et al.
patent: 5801162 (1998-09-01), Takada et al.
patent: 5817645 (1998-10-01), Zamboni et al.
patent: 5997863 (1999-12-01), Zimmermann et al.
patent: 6007810 (1999-12-01), Ishikawa et al.
patent: 6054569 (2000-04-01), Bennett et al.
patent: 6093563 (2000-07-01), Bennett et al.
patent: 6217863 (2001-04-01), Godavarti et al.
patent: 6597996 (2003-07-01), Venkataraman et al.
patent: 2002/0122793 (2002-09-01), Liu et al.
patent: 2002/0128225 (2002-09-01), Liu et al.
patent: 2002/0169143 (2002-11-01), Sasisekharan et al.
patent: 2003/0008820 (2003-01-01), Kwan et al.
patent: 2003/0099628 (2003-05-01), Liu et al.
patent: 2003/0191587 (2003-10-01), Venkataraman et al.
patent: 2004/0092037 (2004-05-01), Sasisekharan et al.
patent: 2004/0197933 (2004-10-01), Venkataraman et al.
patent: 2004/0204869 (2004-10-01), Venkataraman et al.
patent: 2005/0037376 (2005-02-01), Sasisekharan et al.
patent: 0355831 (1990-02-01), None
patent: 54107586 (1979-08-01), None
patent: 2000044601 (2000-02-01), None
patent: WO 96/01648 (1996-01-01), None
patent: WO 01/35977 (2001-05-01), None
patent: WO 01/38399 (2001-05-01), None
patent: WO 200139795 (2001-06-01), None
patent: WO 2004/110360 (2004-12-01), None
Achur et al., “Characterization of Proteoglycans of Human Placenta and Identification of Unique Chondroitin Sulfate Proteoglycans of the Intervillous Spaces that Mediate the Adherence ofPlasmodium falciparum-infected Erythrocytes to the Placenta,”The Journal of Biological Chemistry, vol. 275(51), Dec. 22, 2000, pp. 40344-40356.
Alkhalil et al., “Structural Requirements for the Adherence ofPlasmodium falciparum-infected Erythrocytes to Chondroitin Sulfate Proteoglycans of Human Placenta,”The Journal of Biological Chemistry, vol. 275(51), Dec. 22, 2000, pp. 40357-40364.
Baker, J. R. et al., “Action Pattern and Substrate Specificity of the Hyaluronan Lyase from Group B Streptococci”,Biochem. J., vol. 348, 2000, pp. 465-471.
Catlow et al., “Hepatocyte Growth Factor/scatter Factor and its Interaction With Heparan Sulphate and Dermatan Sulphate”,Biochemical Society Transactions, 2003, vol. 31(Part 2), pp. 352-353.
Daidouji et al., “Neoplastic Changes in Saccharide Sequence of Dermatan Sulfate Chains Derived from Human Colon Cancer,”Digestive Diseases and Sciences, vol. 47(2) Feb. 2002, pp. 331-337.
Denholm et al., “Anti-Tumor Activities of Chondroitinase AC and Chondroitinase B: Inhibition of Angiogenesis, Proliferation and Invasion,”European Journal of Pharmacology, vol. 416, 2001, pp. 213-221.
Denholm et al., “Inhibition of Human Dermal Fibroblast Proliferation by Removal of Dermatan Sulfate,”European Journal of Pharmacology, vol. 400, 2000, pp. 145-153.
Dierks et al., “Posttranslational Formation of Formylglycine in Prokaryotic Sulfatases by Modification of Either Cysteine or Serine”,The Journal of Biological Chemistry, vol. 273(40), Oct. 2, 1998, pp. 25560-25564.
Ernst, S. et al., “Enzymatic Degradation of Glycosaminoglycans”Critical Reviews in Biochemistry and Molecular Biology, vol. 30(5), 1995, pp. 387-444.
Ernst, S. et al., “Direct Evidence for a Predominantly Exolytic Processive Mechanism for Depolymerization of Heparin-like Glycosaminoglycans by Heparinase I”,Proceedings of the National Academy of Sciences of the United States of America, vol. 95, Apr. 1998, pp. 4182-4187.
Gacesa et al., “Enzymic Degradation of Alginates”,International Journal of Biochemistry, vol. 24(4), 1992, pp. 545-552.
Gandra et al., “Anticoagulant Sulfated Glycosaminoglycans in the Tissues of the Primitive ChordateStyela Plicata(Tunicata)”,Glycobiology, vol. 10(12), 2000, pp. 1333-1340.
Gerlt et al., “Understanding the Rates of Certain Enzyme-Catalyzed Reactions: Proton Abstraction from Carbon Acids, Acyl-Transfer Reactions and Displacement Reactions of Phosphodiesters”,Biochemistry. vol. 32(45), Nov. 16, 2003, pp. 11943-11952.
Gu, K. et al., “Purification, Characterization and Specificity of Chondroitin Lyases and Glycuronidase fromFlavobacterium heparinum” Biochemistry Journal, vol. 312, 1995, pp. 569-577.
Habuchi, O., “Diversity and Functions of Glycosaminoglycan Sulfotransferases ”,Biochimica Et Biophysica Acta, vol. 1474, 2000, pp. 115-127.
Homans, S. W., “A Molecular Mechanical Force Field for the Conformational Analysis of Oligosaccharides: Comparison of Theoretical and Crystal Structures of Manα1-3Manβ1-4GlcNAc”,Biochemistry, vol. 29, 1990, pp. 9110-9118.
Huang et al., “Crystal Structure of Chondroitinase B fromFlavobacterium heparinumand Its Complex with a Disaccharide Product at 1.7 Å Resolution,”The Journal of Molecular Biology, vol. 294, 1999, pp. 1257-1269.
Huang, W. et al., “Active Site of Chondroitin AC Lyase Revealed by the Structure of Enzyme-Oligosaccharide Complexes and Mutagenesis”,Biochemistry, vol. 40, 2001, pp. 2359-2372.
Huige, C. J. M. et al., “Force Field Parameters for Sulfates and Sulfamates Based on Ab Initio Calculations: Extensions of AMBER and CHARMm Fields”,Journal of Computational Chemistry, vol. 16(1), 1995, pp. 56-79.
Jandik, K. A., et al., “Action Pattern of Polysaccharide Lyases on Glycosaminoglycans”,Glycobiology, vol. 4(3), 1994, pp. 289-296.
Jenkins et al., “The Architecture of Parallel β-Helices and Related Folds”,Progress in Biophysics&Molecular Biology, vol. 77, 2001, pp. 111-175.
Karamanos et al., “Identity of Dermatan and Chondroitin Sequences in Dermatan Sulfate Chains Determined by Using Fragmentation with Chondroitinases and Ion-Pair High-Performance Liquid Chromatography,”Analytical Biochemistry, vol. 225, 1995, pp. 220-230.
Lin, B. et al., “Identification of a Histidine Residue Essential for Enzymatic Activity of Group B Streptococcal Hyaluronate Lyase”,Biochemical and Biophysical Research Communications, vol. 231, 1997, pp. 379-382.
Liu, D. et al., “Tumor Cell Surface Heparan Sulfate as Cryptic Promoters or Inhibitors of Tumor Growth and Metastasis”,Proceedings of the National Academy of Sciences of the United States of America, vol. 99(2), Jan. 22, 2002, pp. 568-573.
Lyon et al., “Hepatocyte Growth Factor/Scatter Factor Binds with High Affinity to Dermatan Sulfate,”The Journal of Biological Chemistry, vol. 273(1), Jan. 2, 1998, pp. 271-278.
Lyon et al., “The Mode of Action of Heparan and Dermatan Sulfates in the Regulation of Hepatocyte Growth Factor/Scatter Factor,”The Journal of Biological Chemistry, vol. 277(2), Jan. 11, 2002, pp. 1040-1046.
Maimone, M. M. et al., “Structure of a Dermatan Sulfate Hexasaccharide that Binds to Heparin Cofactor II with High Affinity”,The Journal of Biological Chemistry, vol. 265, 1990, p. 14830.
Mascellani, G. et al., “Structure and Contribution to the Heparin Cofactor II-mediated Inhibition of Thrombin of Naturally Oversulphated Sequences of Dermatan Sulphate”,Biochemical Journal, vol. 296, 1993, pp. 639-648.
Michel et al., “The Structure of Chondroitin B Lyase Complexed with Glycosaminoglycan Oligosaccharides Unravels a

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