Forms of soluble pyrroloquinoline quinone-dependent glucose...

Chemistry: molecular biology and microbiology – Enzyme – proenzyme; compositions thereof; process for... – Oxidoreductase

Reexamination Certificate

Rate now

  [ 0.00 ] – not rated yet Voters 0   Comments 0

Details

C536S023200

Reexamination Certificate

active

07547535

ABSTRACT:
The present invention relates to improved variants of soluble pyrroloquinoline quinone (PQQ)-dependent glucose dehydrogenases (s-GDH), to genes encoding mutated s-GDH, to mutant proteins of s-GDH with improved substrate specificity for glucose, and to different applications of these s-GDH variants, particularly for determining concentrations of sugar, especially of glucose in a sample.

REFERENCES:
patent: 5484708 (1996-01-01), Hoenes et al.
patent: 5997817 (1999-12-01), Crismore et al.
patent: 6057120 (2000-05-01), Heindl et al.
patent: 6103509 (2000-08-01), Sode
patent: 6190906 (2001-02-01), Schumacher et al.
patent: 7132270 (2006-11-01), Kratzsch et al.
patent: 2004/0265828 (2004-12-01), Sode
patent: 0620283 (1994-10-01), None
patent: 1 167 519 (2002-01-01), None
patent: 1 176 202 (2002-01-01), None
patent: 88/09373 (1988-12-01), None
patent: 92/07953 (1992-05-01), None
patent: 99/30152 (1999-06-01), None
patent: 00/61730 (2000-10-01), None
patent: 0066744 (2000-11-01), None
Branden et al. Introduction to protein structure, Gerald Publishing Inc., New York, p. 247, 1991.
Witkowski et al. Conversion of a beta-ketoacyl synthase to a malonyl decarboxylase by replacement of the active-site cysteine with glutamine, Biochemistry. Sep. 7, 1999;38(36):11643-50.
Seffernick et al. Melamine deaminase and atrazine chlorohydrolase: 98 percent identical but functionally different, J Bacteriol. Apr. 2001;183(8):2405-10.
Database WPI, Section Ch, Week 200064, Derwent Publications Ltd., London, GB, AN 2000-665126, XP0061730.
Japanese Abstract, JP11243949, Takeshima Seiji et al. (1999).
Cleton-Jansen, A-M, et al., (1991) Mol. Gen. Genet. 229, 206-212.
Murphy, L. et al. (1999) Acc. No. T36261.
Kaneko, T. et al. (1997) Acc. No. P72725.
Granger, B.L. et al. (1997) Acc. No. O00812.
NiceZyme View of Enzyme: EC 1.1.5.2, from ExPASy internet site.
Anthony, C. et al., “The pyrroloquinoline quinone (PQQ)-containing quinoprotein dehydrogenases,” The Diversity of Bacterial Redox Proteins, 1998, vol. 26 (5 pgs).
Anthony, Christopher et al., “Quinoprotein-catalysed reactions,”Biochem. J. (1996) 320, 697-711.
Anthony, Christopher et al., “The structure and function of PQQ-containing quinoproteins,” Current Science, vol. 72, No. 1, May 25, 1997, pp. 716-727.
Anthony Christopher et al., “The structure and function of PQQ-containing quinoprotein dehydrogenases,” Progress in Biophysics & Molecular Biology 69 (1998) 1-21.
Cleton-Janson, Anne-Marie et al., “Cloning, characterization and DNA sequencing of the gene encoding the Mr 50,000 quinoprotein glucose dehydrogenase fromAcinetobacter calcoaceticus,” Mol. Gen. Genet (1989) 217:430-436.
Cleton-Janson, Anne-Marie et al., “Cloning of the Genes Encoding the two Different Glucose Dehydrogenases fromAcinetobacter calcoaceticus,” Antonie van Leeuwenhock 56:73-79 (1989).
Cleton-Janson, Anne-Marie et al., “Cloning of the Gene Encoding Quinoprotein Glucose Dehydrogenase fromAcinetobacter calcoaceticus: Evidence for the Presence of a Second Enzyme,” Journal of Bacteriology, May 1988, p. 2121-2125.
D'Costa, E.J. et al., “Quinoprotein Glucose Dehydrogenase and its Application in an Amperometric Glucose Sensor,” Biosensors 2(1986) 71-87.
Dokter, Paul et al., “Cytochome b-562 fromAcinetobacter calcoacetiusL.M.D. 79.41,” Biochem. J. (1988) 254, 131-138.
Dokter, P. et al., “The in vivo and in vitro substrate specificity of quinoprotein glucose dehydrogenase ofAcinetobacter calcoaceticusL.M.D. 79.41,” FEMS Microbiology Letters 43 (1987) 195-200.
Dokter, P. et al., “Purification and characterization of quinoprotein glucose dehydrogenase fromAcinetobacter calcoaceticusL.M.D. 79.41,” Biochem. J. (1986) 239, 163-167.
Duine, J.A. et al., “Different Forms of Quinoprotein Aldose-(Glucose-)Dehydrogenase inAcinetobacter calcoaceticus,” Arch. Microbiol. (1982) 131:27-31.
Duine, J.A. et al., “Energy Generation and the Glucose Dehydrogenase Pathway inAcinetobacter,” The biology ofAcinetobacter, pp. 295-312,1991.
Duine, J.A. et al., “The importance of natural diversity in redox proteins for achieving cofactor-electrode-directed electron transfer,” Biosensors & Bioelectronics 10 (1995) 17-23.
Duine, Johannis A. et al., “Quinoproteins: enzymes containing the quinonoid cofactor pyrroloquinoline quinone, topaquinone or tryptophan-tryptophan quinone,” Eur. J. Biochem. 200, 271-284 (1991).
Goodwin, Pat M. et al., “The Biochemistry, Physiology and Genetics of PQQ and PQQ-Containing Enzymes,” Advances in Microbiol. Physiology, vol. 40, pp. 1-80, (1998).
Hill, David E. et al., “Mutagenesis with Degenerate Oligonucleotides: An Efficient Method for Saturating a Defined DNA Region with Base Pair Substitutions,” Mutagenesis with Degenerate Oligonucleotides, pp. 558-568, (1999).
Igarashi, Satoshi et al., “Construction and Characterization of Mutant Water-Soluble PQQ Glucose Dehydrogenases with Altered Km Values-Site-Directed Mutagenesis Studies on the Putative Active Site,” Biochemical and Biophysical Research Communications 264, 820-824 (1999).
Kaufmann, Norbert et al., “Development and evaluation of a new system for determining glucose from fresh capillary blood and heparinised venous blood,” Glucotrend (18 pgs.) (1997).
Laurinavicius, Valdas et al., “A Novel Application of Heterocyclic Compounds for Biosensors Based on NAD, FAD, and PQQ Dependent Oxidoreductases,” Monatshefte fur Chemie 130, 1269-1281 (1999).
Laurinavicius, V. et al., “Oxygen Insensitive Glucose Biosensor Based on PQQ-Dependent Glucose Dehydrogenase,” Analytical Letters, 32(2), 299-316 (1999).
Leung, David W. et al., “A Method for Random Mutagenesis of a Defined DNA Segment Using a Modified Polymerase Chain Reaction,” Technique-A Journal of Methods in Cell and Molecular Biology, vol. 1, No. 1 Aug. 1989: pp. 11-15.
Matsushita, K., Adachi, O. “Bacterial Quinoproteins Glucose Dehydrogenase and Alcohol Dehydrogenase,” in Principles and Applications of Quinoproteins, 1993, 47-63, Davidson, V.L., Ed., Marcel Dekker, New York.
Matsushita, Kazunobu et al., “Quinoprotein D-glucose dehydrogenases inAcinetobacter calcoaceticusLMD 79:41: Purification and characterization of the membrane-bound enzyme distinct from the soluble enzyme,” Antonie van Leeuwenhoek 5: 63-72 (1989).
Matsushita, Kazunobu et al., “Quinoprotein D-Glucose Dehydrogenase of theAcinetobacter calcoaceticusRespiratory Chain: Membrane-Bound and Soluble Forms are Different Molecular Species,” Biochemistry, 1989, 28, 6276-6280.
Matsushita, Kazunobu et al., “Soluble and Membrane-Bound Quinoprotein D-Glucose Dehydrogenases of theAcinetobacter calcoaceticus: The Binding process of PQQ to the Apoenzymes,” Biosci. Biotech. Biochem., 59 (8), 1548-1555, 1995.
Oliphant, Arnold R. et al., “Cloning of Random-Sequence Oligodeoxynucleotides,” Gene, 44 (1986), 177-183.
Olsthoorn, Arjen J.J. et al., “On the Mechanism and Specificity of Soluble, Quinoprotein Glucose Dehydrogenase in the Oxidation of Aldose Sugars,” Biochemistry, 1998, 37, 13854-13861.
Olsthoorn, Arjen J.J. et al., “Production, Characterization, and Reconstitution of Recombinant Quinoprotein Glucose Dehydrogenase (Soluble Type; EC 1.1.99.17) Apoenzyme ofAcinetobacter calcoaceticus,” Archives of Biochemistry and Biophysics, vol. 336, No. 1, Dec. 1, pp. 42-48, 1996.
Oubrie, Arthur et al., “Active-site structure of the soluble quinoprotein glucose dehydrogenase complexed with methylhydrazine: A covalent cofactor-inhibitor complex,” PNAS Oct. 12, 1991, vol. 96, No. 21, 11787-11791.
Oubrie, Arthur et al., “Structure and mechanism of soluble quinoprotein glucose dehydrogenase,” The EMBO Journal, vol. 18, No. 19, pp. 5187-5194, 1999.
Oubrie, Arthur et al., “Structural requirements of pyrroloquin

LandOfFree

Say what you really think

Search LandOfFree.com for the USA inventors and patents. Rate them and share your experience with other people.

Rating

Forms of soluble pyrroloquinoline quinone-dependent glucose... does not yet have a rating. At this time, there are no reviews or comments for this patent.

If you have personal experience with Forms of soluble pyrroloquinoline quinone-dependent glucose..., we encourage you to share that experience with our LandOfFree.com community. Your opinion is very important and Forms of soluble pyrroloquinoline quinone-dependent glucose... will most certainly appreciate the feedback.

Rate now

     

Profile ID: LFUS-PAI-O-4080559

  Search
All data on this website is collected from public sources. Our data reflects the most accurate information available at the time of publication.