Chemistry: molecular biology and microbiology – Measuring or testing process involving enzymes or... – Involving transferase
Reexamination Certificate
2005-10-04
2005-10-04
Gitomer, Ralph (Department: 1651)
Chemistry: molecular biology and microbiology
Measuring or testing process involving enzymes or...
Involving transferase
C435S004000
Reexamination Certificate
active
06951729
ABSTRACT:
Provided is a screening method for compounds affecting fatty acid biosynthesis, the method comprising: providing a reaction mixture comprising: an acyl carrier moiety or enzymes and precursors sufficient to generate the acyl carrier moiety; a bacterial enzymatic pathway comprising at least two consecutively acting enzymes selected from the group consisting of: malonyl-CoA:ACP transacylase, beta-ketoacyl-ACP synthase III, NADPH dependent beta-ketoacyl-ACP reductase, beta-hydroxylacyl-ACP dehydrase and enoyl-ACP reductase; and substrates and cofactors required for the operation of the enzymes; contacting the reaction mixture with a prospective bioactive agent; conducting a high throughput measurement of the activity of the enzymatic pathway; and determining if the contacting altered the activity of the enzymatic pathway.
REFERENCES:
patent: 5539132 (1996-07-01), Royer et al.
patent: 5614551 (1997-03-01), Dick et al.
patent: 5759837 (1998-06-01), Kuhajda et al.
patent: 5965402 (1999-10-01), Black et al.
patent: 6228619 (2001-05-01), Foster et al.
patent: 6274376 (2001-08-01), Black et al.
patent: 6294357 (2001-09-01), Kallender et al.
patent: 6380370 (2002-04-01), Doucette-Stamm et al.
patent: 6403337 (2002-06-01), Bailey et al.
patent: 6432670 (2002-08-01), Payne et al.
patent: 6475751 (2002-11-01), Reynolds et al.
patent: 6593114 (2003-07-01), Kunsch et al.
patent: 6613553 (2003-09-01), Rock et al.
patent: 2002/0076766 (2002-06-01), Black et al.
patent: 26 20 777 (1977-12-01), None
patent: 0 78 6519 (1997-07-01), None
patent: 0 826 774 (1998-04-01), None
patent: 10-174590 (1998-06-01), None
patent: WO 97/30070 (1997-08-01), None
patent: WO 97/30149 (1997-08-01), None
patent: WO 98/06734 (1998-02-01), None
patent: WO 98/18931 (1998-05-01), None
patent: WO 98/24475 (1998-06-01), None
patent: WO 98/26072 (1998-06-01), None
patent: WO 99/37800 (1999-07-01), None
patent: WO 00/70017 (2000-11-01), None
patent: WO 01/48248 (2000-12-01), None
patent: WO 01/30988 (2001-05-01), None
patent: WO 01/49721 (2001-07-01), None
patent: WO 01/70995 (2001-09-01), None
patent: WO 02/31128 (2002-04-01), None
Ward W. Kinetic and Structural Characteristics of the Inhibition of Enoyl (Acyl Carrier Protein) Reductase by Triclosan. Biochemistry 38(38)12514-12525, 1999.
Rock, et al., “Preparative Enzymatic Synthesis and Hydrophobic Chromatography of Acyl-Acyl Carrier Protein”,The Journal of Biological Chemistry, 254(15): 7123-7128 (1979).
Broadwater, et al., “Spinach Holo-Acyl Carrier Protein: Overproduction and Phosphopantetheinylation inEscherichia coliBL21 (DE3), in Vitro Acylation, and Enzymatic Desaturation of Histidine-Tagged Isoform I”, Protein Expression and Purification, 15: 314-326 (1999).
Edwards, et al., “Cloning of the fabF gene in an expression vector and in vitro characterization of recombinant fabF and fabB encoded enzymes fromEscherichia coli”, FEBS Letters, 402: 62-66 (1997).
Rock, et al., “Acyl Carrier Protein fromEscherichia coli”, Methods in Enzymology, 71: 341-351 (1981).
Lambalot, et al., “Cloning, Overproduction, and Characterization of theEscherichia coliHolo-acyl Carrier Protein Synthase”,The Journal of Biological Chemistry, 270(42): 24658-24661 (1995).
Bhargava et al., “Triclosan: Applications and Safety,” American Journal of Infection Control, 24:209-218 (1998).
Rock et al., “Lipid Metabolism in Prokaryotes,” Biochemistry of Lipids, Lipoproteins and Membranes, Elsevier Publishing Company Amsterdam, 35-74 (1996).
Rock et al., “Escherichia colias a model for the regulation of dissociable (type II) fatty acid biosynthesis,” Biochimica et Biophysica Acta, 1302:1-16 (1996).
Heath et al., “Mechanism of Triclosan Inhibition of Bacterial Fatty Acid Synthesis,” The Journal of Biological Chemistry, 274(16):11110-11114 (1999).
Gadda et al., “Substrate Specificity of a Nitroalkane-Oxidizing Enzyme,” Archives of Biochemistry and Biophysics, 363(2):309-313 (1999).
McMurray et al., “Triclosan targets lipid synthesis,” Nature, 394:531-532 (1998).
Ross et al., “Molecular Cloning and Analysis of the Gene Encoding the NADH Oxidase fromStreptococcus faecalis10C1,” Journal of Molecular Biology 227:658-671 (1992).
Bradford, Marion, “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).
Tchorzewski et al., “Unique primary structure of 2-nitropropane dioxygenase fromHansenula mrakii,” European Journal of Biochemistry, 226:841-846 (1994).
Komuniecki et al., “Electron-transfer flavoprotein from anaerobicAscaris suummitochondria and its role in NADH-dependent 2-methyl branched-chain enoyl-CoA reduction,” Biochimica et Biophysica Acta, 975:127-131 (1989).
Baker et al., “Enoyl-acyl-carrier-proteon reductase andMycobacterium tuberculosisInhA do not conserve the Tyr-Xaa-Xaa-Xaa-Lys motif in mammalian 11β- and 17β-hydroxysteriod dehydrogenases and Drosophila alcohol dehydrogenase,” Biochemical Journal, 309:1029-1030 (1995).
Gibson et al., “Contribution of NADH Oxidase to Aerobic Metabolism ofStreptococcus pyogenes,” Journal of Bacteriology, 182(2):448-455 (2000).
Boynton et al., “Cloning, Sequencing, and Expression of Clustered Genes Encoding β-Hydroxybutyryl-Coenzyme A (CoA) Dehydrogenase, Crotonase, and Butyrl-CoA Dehydrogenase fromClostridium acetobutylicumATCC 824,” Journal of Bacteriology, 178(11):3015-3024 (1996).
Heasley et al., “Kinetic Mechanism and Substrate Specificity of Nitroalkane Oxidase,” Biochemical and Biophysical Research Communication, 225:6-10 (1996).
Havarstein et al., “An unmodified heptadecapeptide pheromone induces competence for genetic transformation inStreptococcus pneumoniae,” Proceedings of the National Academy of Science USA, 92:11140-11144 (1995).
Deiz-Gonzalez et al., “NAD-Independent Lactate and Butyryl-CoA Dehydrogenases of Clostridium acetobutylicum P262,” Current Microbiology, 34:162-166 (1997).
Slater-Radosti et al., “Biochemical and genetic characterization of the action of triclosan onStaphylococcus aureus,” Journal of antimicrobial Chemotherapy, 48:1-6 (2001).
Heath et al., “A triclosan-resistant bacterial enzyme,” Nature, 406:145-146 (2000).
Heath et al., “Broad Spectrum Antimicrobial Biocides Target the FabI Component of Fatty Acid Synthesis,” The Journal of Biological Chemistry, 273(46):30316-30320 (1998).
Saito et al., “Genetic Evidence that Phosphatidylserine Synthase II Catalyzes the Conversion of Phosphatidylethanolamine to Phosphatidylserine in Chinese Hamster Ovary Cells,” The Journal of Biological Chemistry, 273(27):17199-17205 (1998).
Bergler et al., “Protein EnvM is the NADH-dependent Enoyl-ACP Reductase (FabI) ofEscherichia coli,” The Journal of Biological Chemistry, 269(8):5493-5496 (1994).
Duran et al., “Characterization of cDNA Clones for the 2-Methyl Branched-chain Enoyl-CoA Reductase,” The Journal of Biological Chemistry, 268(30):22391-22396 (1993).
Volkman et al., “Biosynthesis of D-Alanyl-Lipoteichoic Acid: The Teritary Structure of apo-D-Alanyl Carrier Protein,” Biochemistry, 40:7964-7972 (2001).
Parkh et al., “Roles of Tyrosine 158 and Lysine 165 in the Catalytic Mechanism of InhA, the Enoyl-ACP Reductase fromMycobacterium tuberculosis.” Biochemistry, 38:13623-13634 (1999).
Roujeinikova et al., “Crystallographic Analysis of Triclosan Bound to Enoyl Reductase,” Journal of Molecular Biology, 294:527-535 (1999).
Heath et al., “Inhibition ofStaphylococcus aureusNADPH-dependent Enoyl-Acyl Carrier Protein Reductase by Triclosan and Hexachlorophene,” The Journal of Biological Chemistry, 275(7):4654-4659 (2000).
Heath et al., “Inhibition of β-Ketoacyl-Acyl Carrier Protein Syn
Dewolf, Jr. Walter E
Kallender Howard
Lonsdale John T
Affinium Pharmaceuticals, Inc.
Foley & Hoag LLP
Gitomer Ralph
LandOfFree
High throughput screening method for biological agents... does not yet have a rating. At this time, there are no reviews or comments for this patent.
If you have personal experience with High throughput screening method for biological agents..., we encourage you to share that experience with our LandOfFree.com community. Your opinion is very important and High throughput screening method for biological agents... will most certainly appreciate the feedback.
Profile ID: LFUS-PAI-O-3464617