β-galactoside-α2,3-sialyltransferase, a gene...

Chemistry: molecular biology and microbiology – Enzyme – proenzyme; compositions thereof; process for... – Transferase other than ribonuclease

Reexamination Certificate

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C435S183000, C435S069100, C435S091100, C435S320100, C435S252100, C435S252300, C435S074000, C536S023200, C536S023100, C536S023700

Reexamination Certificate

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08030043

ABSTRACT:
The present invention provides a novel β-galactoside-α2,3-sialyltransferase and a nucleic acid encoding the sialyltransferase. The present invention also provides a microorganism producing the sialyltransferase, as well as a method for producing the sialyltransferase using such a microorganism. The present invention further provides a vector carrying a nucleic acid encoding the sialyltransferase, and a host cell transformed with the vector, as well as a method for producing a recombinant β-galactoside-α2,3-sialyltransferase. The present invention further provides a method for preparing a sialylsugar chain, which uses the sialyltransferase of the present invention.

REFERENCES:
patent: 0915153 (1999-05-01), None
patent: 0915163 (1999-05-01), None
patent: 0 906 432 (2004-06-01), None
patent: 10-234373 (1998-09-01), None
patent: 2001-503961 (2001-03-01), None
patent: WO-97/47749 (1997-12-01), None
patent: WO-99/49051 (1999-09-01), None
patent: WO-01/77314 (2001-10-01), None
patent: WO-03/027297 (2003-04-01), None
Broun et al., Catalytic plasticity of fatty acid modification enzymes underlying chemical diversity of plant lipids. Science, 1998, vol. 282: 1315-1317.
Chica et al., Semi-rational approaches to engineering enzyme activity: combining the benefits of directed evolution and rational design. Curr. Opi. Biotechnol., 2005, vol. 16: 378-384.
Devos et al., Practical limits of function prediction. Proteins: Structure, Function, and Genetics. 2000, vol. 41: 98-107.
Guo et al., Protein tolerance to random amino acid change. PNAS., 2004, vol. 101 (25): 9205-9210.
Seffernick et al., Melamine deaminase and Atrazine chlorohydrolase: 98 percent identical but functionally different. J. Bacteriol.,2001, vol. 183 (8): 2405-2410.
Sen et al., Developments in directed evolution for improving enzyme functions. Appl. Biochem. Biotechnol., 2007, vol. 143: 212-223.
Wishart et al., A single mutation converts a novel phosphotyrosine binding domain into a dual-specificity phosphatase. J. Biol. Chem., 1995, vol. 270(45): 26782-26785.
Whisstock et al., Prediction of protein function from protein sequence. Q. Rev. Biophysics., 2003, vol. 36 (3): 307-340.
Witkowski et al., Conversion of b-ketoacyl synthase to a Malonyl Decarboxylase by replacement of the active cysteine with glutamine. Biochemistry, 1999, vol. 38: 11643-11650.
Cameron ER., Recent advances in transgenic technology. 1997, vol. 7: 253-265.
Kappel et al., Regulating gene expression in transgenic animals. Current Opinion in Biotechnology 1992, vol. 3: 548-553.
Mullins et al., Transgenesis in nonmurine species. Hypertension, 1993, vol. 22 (4): 630-633.
Mullins et al., Transgenesis in the rat and larger mammals. J. Clin. Invest., 1996, vol. 97 (7): 1557-1560.
Wigley et al., Site-specific transgene insertion: an approach. Reprod. Fert. Dev., 1994, vol. 6: 585-588.
Tsukamoto et al., Purification, cloning, and expression of an a/b-Galactoside a-2,3-sialyltransferase from a luminous marine bacterium,Photobacterium phosphoreum. J. Biol. Chem., 2007, vol. 282 (41): 29794-29802.
Takakura Y et al., “Molecular Cloning and Production of a Beta-Galactoside Alpha 2,3-Sialyltransferase of Vibrio sp. JT-FAJ-16”, Glycobiology, vol. 15, No. 11, p. 1206, 2005, Oxford University Press. XP008109319.
Tsukamoto Hiroshi et al., “Purification, cloning, and expression of an alpha/beta-galactoside alpha-2,3-sialyltransferase from a luminous bacterium,Photobacterium phosphoreum” Journal of Biological Chemistry, vol. 282, No. 41, pp. 29794-29802, 2007. XP002540676.
Takakura Yoshimitsu et al., “Molecular Cloning, Expression and Properties of an alpha/beta-galactoside alpha 2, 3-sialyltransferase from Vibrio sp. JT-FAJ-16” Journal of Biochemistry, vol. 142, No. 3, pp. 403-412, 2007. XP002540661.
Tsukamoto Hiroshi et al., “Photobacteriumsp JT-ISH-224 produces two sialyltransferase, alpha-/beta-galactoside alpha 2,3-sialyltransferase”, Journal of Biochemistry, vol. 143, No. 2, pp. 187-197, 2008. XP002540660.
Harduin-Lepers et al., Biochem. J., vol. 352, pp. 37-48 (2000).
Lee et al., The Journal of Biological Chemistry, vol. 274, No. 17, pp. 11958-11967 (1999).
Lee et al., Eur. J. Biochem., vol. 216, pp. 377-385 (1993).
Chang et al., Glycobiology, vol. 5, No. 3, pp. 319-325 (1995).
Gillespie et al., J. Biol. Chem., vol. 267, No. 29, pp. 21004-21010 (1992).

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