Chemistry: molecular biology and microbiology – Micro-organism – tissue cell culture or enzyme using process...
Reexamination Certificate
2011-01-04
2011-01-04
Swope, Sheridan (Department: 1652)
Chemistry: molecular biology and microbiology
Micro-organism, tissue cell culture or enzyme using process...
Reexamination Certificate
active
07863014
ABSTRACT:
The present invention provides a novel process for preparing nicotinamide adenine dinucleotide phosphate (NADP). The process of the present invention comprises performing phosphorylation using a polyphosphoric acid or a salt thereof and nicotinamide adenine dinucleotide (NAD+) as substrates in the presence of a polyphosphate-dependent NAD+kinase from aMycobacterium, wherein the reaction solution contains 0.1-15% by weight of the polyphosphoric acid or a salt thereof, and 5-150 mM of a divalent metal ion.
REFERENCES:
patent: 52-82792 (1977-07-01), None
Kawai et al., Biochem. Biophys. Res. Commun. 2000, vol. 276, No. 1, p. 57-63.
Ngo et al. in The Protein Folding Problem and Tertiary Structure Prediction, 1994, Merz et al. (ed.), Birkhauser, Boston, MA, pp. 433 and 492-495, Ref: U, Form-892.
Zerez et al, Negative modulation ofEscherichia coliNAD kinase by NADPH and NADH. J Bacteriol. Jan. 1987;169(1):184-8.
USPTO in house BLAST alignment of SEQ ID No. 1 with PIR database F70502 and UniProt database P0A5S6.
Labesse et al, Diacylglyceride kinases, sphingosine kinases and NAD kinases: distant relatives of 6-phosphofructokinases. Trends Biochem Sci. Jun. 2002;27(6):273-5. Review.
Kawai et al, “Establishment of Mass-Production System for NADP Using Bacterial Inorganic Polyphosphate/ATP-NAD Kinase”, J. Biosci. Bioeng., Dec. 2001, vol. 92, No. 5, pp. 447-452.
Kawai et al, “Inorganic Polyphosphate/ATP-NAD Kinase ofMicrococcus flavusandMycobacterium tuberculosisH37Rv”, Biochem. Biophys. Res. Commun. 2000, vol. 276, No. 1, pp. 57-63.
Beutler et al, “Coenzymes, metabolites, and other biochemical reagents”, pp. 328-393, In Bergmeyer, H. U. (ed.), Methods of enzymatic analysis, vol. 1, Verlag Chemie, Weinheim (1983).
Matsushita et al, “NADP production using thermostable NAD kinase ofCorynebacterium flaccumfaciensAHU-1622”, Can. J. Microbiol., vol. 32, 1986, pp, 585-590.
McGuinness et al, “NAD Kinase—A Review”, Int. J. Biochem., vol. 17, No. 1, pp. 1-11, 1985.
Murata et al, “Continuous Production of NADP by ImmobilizedBrevibacterium ammoniagenesCells”, Biotechnology and Bioengineering, vol. XXI, pp. 887-895 (1979).
Murata et al, “Metaphosphate: A New Phosphoryl Donor for NAD Phosphorylation”, Agric. Biol. Chem., 44(1), 61-68, 1980.
Wood et al, “Biological Aspects of Inorganic Polyphosphates”, Ann. Rev. Biochem. 1988, 57:235-260.
Kawai et al, “Inorganic Polyphosphate/ATP-NAD Kinase ofMicrococcus flavusandMycobacterium tuberculosisH37Rv”, Biochemical and Biophysical Research Communications, 276, 57-63 (2000).
Ausubel et al, “Current Protocols in Molecular Biology”, John Wiley & Sons, Inc., New York (1994).
Bradford et al, “A Rapid and Sensitive Method for the Quantitation of Microgram Quantities of Protein Utilizing the Principle of Protein-Dye Binding”, Analytical Biochemistry 72, 248-254 (1976).
Chibata et al, “Immobilized Aspartase-Containing Microbial Cells: Preparation and Enzymatic Properties”, Applied Microbiology, May 1974, vol. 27, No. 5, pp. 878-885.
Murata et al, “Continuous Production of Glucose-6-phosphate by ImmobilizedAchromobacter butyriCells”, European J. Appl. Microbiol. Biotechnol. 7, 45-51 (1979).
Fiske et al, “The Colorimetric Determination of Phosphorus”, The Journal of Biological Chemistry, vol. 66, No. 2, pp. 375-400 (1925).
Langer et al, “Enzymatic Regeneration of ATP”, AIChE Journal, Nov. 1976, vol. 22, No. 6, pp. 1079-1090.
Maruyama et al, “ATP Production from Adenine by a Self-coupling Enzymatic Process: High-level Accumulation under Ammonium-limited Conditions”, Biosci. Biotechnol. Biochem., 65(3), 644-650, 2001.
Fujio et al, Enzymatic Production of Pyrimidine Nucleotides UsingCorynebacterium ammoniagenesCells and RecombinantEscherichia coliCells: Enzymatic Production of CDP-Choline from Orotic Acid and Choline Chloride (Part I), Biosci. Biotech. Biochem., 61(6), 956-959, 1997.
Kawai et al, “Molecular characterization ofEscherichia coliNAD kinase”, Eur. J. Biochem. 268, 4359-4365 (2001).
Kawai et al, “Molecular cloning and identification ofUTR1of a yeastSaccharomyces cerevisiaeas a gene encoding an NAD kinase”, FEMS Microbiology Letters, vol. 200 No. 2, (2001), 181-184.
Waehneldt et al, “Phosphorylation of Nucleosides with Polyphosphoric Acid”, Biochem. Biophys. Acta, 134 (1967), 1-8.
Cole et al, “Deciphering the biology ofMycobacterium tuberculosisfrom the complete genome sequence”, Nature, vol. 393, Jun. 1998, 537-544.
“Enzyme Handbook”, 1983, Asakura Publishing, p. 339.
Schoner et al, “Enhanced Translational Efficiency with Two-Cistron Expression System”, Methods in Enzymology, vol. 185, 94-103 (1990).
Suzuki et al, “Organization of rRNA Genes inMycobacterium bovisBCG”, Journal of Bacteriology, Feb. 1987, vol. 169, No. 2, pp. 839-843.
Patent Abstracts of Japan, Publication No. 52-082792, published Nov. 7, 1977, Applicant Tanabe Seiyaku CO LTD, Inventor: Senhata Ichiro et al, Title: Preparation of Nicotinamide-Adenine Dinucleotide Phosphate (Abstract only).
Filippovich et al, “ATP- and Polyphosphate-dependent Bacterial NAD+Kinases”, Prikladnaya Biokhimiya i Mikrobiologiya, vol. 36, No. 2 (2000), p. 117-121 (with English abstract).
Zerez et al, Arch Microbiol. May 1986;144(4):313-6 “NAD kinase fromBacillus licheniformis: inhibition by NADP and other properties” (Abstract only).
Kawai et al, Eur J Biochem. Aug. 2001;268(15):4359-65 “Molecular characterization ofEscherichia coliNAD kinase.”
Garavaglia, S et al J. Bacteriol. 185, 4844-4850 (2003) “Allosteric regulation ofBacillus subtilisNAD kinase by quinolinic acid”.
Raffaelli, N et al, Biochemistry 43, 7610-7617 (2004) “Characterization ofMycobacterium tuberculosisNAD kinase: functional analysis of the full-length enzyme by site-directed mutagenesis” (Abstract only).
Ochiai, A et al Protein Expr. Purif. 36, 124-130 (2004) “Overexpression, purification, and characterization of ATP-NAD kinase ofSphingomonassp. A1” (Abstract only).
Kawai, S et al J. Biol. Chem. 280, 39200-39207 (2005) “MJ0917 in archaeonMethanococcus jannaschiiis a novel NADP phosphatase/NAD kinase” (Abstract only).
Lerner, F et al Biochem. Biophys. Res. Commun. 288, 69-74 (2001) “Structural and functional characterization of human NAD kinase” (Abstract only).
Stephan, C et al Int. J. Biochem. Cell Biol. 32, 855-863 (2000) “Evidence for the existence of two soluble NAD(+) kinase isoenzymes inEuglena gracilisZ”.
Delumeau, O. et al Plant Sci. 138, 43-52 (1998) “NAD+ kinase activity, calmodulin levels during the growth of isolated cells fromLycopersicon pimpinellifoliumand kinetic constants of the calmodulin-dependent NAD+ kinase” (as summarized from http://www.brenda-enzymes.info/literature/lit.php4?e=2.7.1.23&r=641199 retrieved Sep. 14, 2009).
Williams, M.BArch. Biochem. Biophys. 237, 80-87 (1985) “Calmodulin-dependent NAD kinase of human neutrophils” (Abstract only).
Ji, X. et al Ann. N.Y. Acad. Sci. 434, 264-266 (1984) “Immobilization of NAD kinase” (Abstract only).
Muto, S.; Z. Pflanzenphysiol. 109, 385-393 (1983) “Kinetic nature of calmodulin-dependent NAD kinase from pea seedlings” (as summarized from http://www.brenda-enzymes.info/literature/lit.php4?e=2.7.1.23&r=641200 retrieved Sep. 14, 2009).
Tseng, Y.M et al Biochim. Biophys. Acta 568, 205-214 (1979) “Isolation and characterization of yeast nicotinamide adenine dinucleotide kinase” (Abstract only).
Kawai S et al Biochem Biophys Res Commun. Sep. 16, 2000;276(1):57-63 “Inorganic Polyphosphate/ATP-NAD kinase ofMicrococcus flavusandMycobacterium tuberculosisH37Rv.” (Abstract only).
Chung, A.E.; J. Biol. Chem. 242, 1182-1186 (1967) “Nicotinamide
Ando Yoshio
Kawai Shigeyuki
Matsukawa Hirokazu
Matsuo Yuhsi
Murata Kousaku
Nixon & Vanderhye P.C.
Oriental Yeast Co. Ltd.
Swope Sheridan
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