Chemistry: molecular biology and microbiology – Enzyme – proenzyme; compositions thereof; process for... – Oxidoreductase
Reexamination Certificate
2011-03-29
2011-03-29
Raghu, Ganapathirama (Department: 1652)
Chemistry: molecular biology and microbiology
Enzyme , proenzyme; compositions thereof; process for...
Oxidoreductase
C435S008000, C435S025000, C435S006120, C536S023200
Reexamination Certificate
active
07915021
ABSTRACT:
This invention relates to: the development of a mutant firefly luciferase in order to use dATP as a DNA polymerase substrate upon pyrosequencing, such luciferase being subjected to substrate specificity modification in a manner such that the dATP-induced activity alone is decreased while the ATP-induced activity is maintained; and a mutant firefly luciferase for which the proportion of activity induced by dATP to activity induced by ATP (dATP/ATP) is lower than that for the wild-type firefly luciferase, in which an amino acid identified based on homology analysis as corresponding with the 421stamino acid (glycine) of the amino acid sequence of the wild-type North American firefly (Photinus pyralis) luciferase has been substituted with a polar amino acid.
REFERENCES:
patent: 2666561 (1997-06-01), None
patent: 09-510610 (1997-10-01), None
patent: 10-512750 (1998-12-01), None
patent: 11-239493 (1999-09-01), None
patent: 3048466 (2000-03-01), None
patent: 2000-197484 (2000-07-01), None
patent: 2000-197487 (2000-07-01), None
patent: 2001-501092 (2001-01-01), None
patent: 2001-518799 (2001-10-01), None
patent: 2003-512071 (2003-04-01), None
patent: 2003-518912 (2003-06-01), None
patent: 2007-094577 (2007-04-01), None
patent: WO 99/02697 (1999-01-01), None
patent: WO 2009/140662 (2009-11-01), 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.
Kisselev L., Polypeptide release factors in prokaryotes and eukaryotes: same function, different structure. Structure, 2002, vol. 10: 8-9.
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.
Cont et al., “Crystal Structure of Firefly Luciferase Throws Light on a Superfamily of Adenylate-forming Enzymes”, Structure 1996, vol. 4, 287-298.
Nakatsu, et al, “Structural Basis for the Spectral Differenc in Luciferase Bioluminescence”, Nature 2006, vol. 440, 372-376.
Cohen et al., “Nonchromosomal Antibiotic Resistance in Bacteria: Genetic Transformation ofEscherichia”, Cohen, S. N. et al.: Proc. Natl. Acad. Sci., USA, 69: 2110-2114 (1972).
Becker, D. M. et al., “High-Efficiency Transformation of Yeast by Electroporation”, Methods. Enzymol., 194: 182-187 (1991).
Hinmen, A. et al., “Transformation of Yeast”, Proc. Natl. Acad. Sci., USA, 75: 1929-1933 (1978).
Itoh, H., “Transformation of Intact Yeast Cells Treated with Alkali Cations”, J. Bacteriol., 153: 163-168 (1983).
Kambara Hideki
Tsunoda Hiroyuki
Antonelli, Terry Stout & Kraus, LLP.
Hitachi , Ltd.
Raghu Ganapathirama
LandOfFree
Mutant firefly luciferase does not yet have a rating. At this time, there are no reviews or comments for this patent.
If you have personal experience with Mutant firefly luciferase, we encourage you to share that experience with our LandOfFree.com community. Your opinion is very important and Mutant firefly luciferase will most certainly appreciate the feedback.
Profile ID: LFUS-PAI-O-2699033