Enterobacteriaceae strains over-expressing the yfiD gene for...

Chemistry: molecular biology and microbiology – Micro-organism – tissue cell culture or enzyme using process... – Preparing alpha or beta amino acid or substituted amino acid...

Reexamination Certificate

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C435S115000, C435S069100, C435S116000, C435S252300, C435S488000, C435S113000, C435S252330, C435S006120, C536S023100

Reexamination Certificate

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10817431

ABSTRACT:
The present invention relates to a process for the production of L-amino acids by fermentation of recombinant microorganisms of the Enterobacteriaceae family, whereina) the yfiD ORF and/or the pflB gene or nucleotide sequences coding for the gene products are overexpressed in the microorganisms producing the desired L-amino acid, and the microorganisms are cultured in a medium under conditions in which the desired L-amino acid is enriched in the medium or in the cells; andb) the desired L-amino acid is isolated, in a manner such that constituents of the fermentation broth and/or the biomass in its entirety or in portions (>0 to 100%) either remain in the isolated product or are completely removed.

REFERENCES:
patent: 4278765 (1981-07-01), Debabov et al.
patent: 101 32 946 (2001-07-01), None
patent: 101 35 053 (2001-07-01), None
patent: 0 271 838 (1988-06-01), None
patent: 0 994 190 (2000-04-01), None
patent: 1 013 765 (2000-06-01), None
patent: 1 149 911 (2001-10-01), None
patent: WO 99/18228 (1999-04-01), None
patent: WO 99/53035 (1999-10-01), None
patent: WO 01/05939 (2001-01-01), None
patent: WO 01/92545 (2001-12-01), None
patent: WO 02/06459 (2002-01-01), None
patent: WO 02/29080 (2002-04-01), None
patent: WO 02/36797 (2002-05-01), None
patent: WO 02/064808 (2002-08-01), None
patent: WO 02/077183 (2002-10-01), None
patent: WO 02/081698 (2002-10-01), None
patent: WO 02/081721 (2002-10-01), None
patent: WO 02/081722 (2002-10-01), None
patent: WO 03/004598 (2003-01-01), None
patent: WO 03/004663 (2003-01-01), None
patent: WO 03/004664 (2003-01-01), None
patent: WO 03/004665 (2003-01-01), None
patent: WO 03/004669 (2003-01-01), None
patent: WO 03/004670 (2003-01-01), None
patent: WO 03/004671 (2003-01-01), None
patent: WO 03/004674 (2003-01-01), None
patent: WO 03/006666 (2003-01-01), None
patent: WO 03/008603 (2003-01-01), None
patent: WO 03/008604 (2003-01-01), None
patent: WO 03/008605 (2003-01-01), None
patent: WO 03/008606 (2003-01-01), None
patent: WO 03/008607 (2003-01-01), None
patent: WO 03/008608 (2003-01-01), None
patent: WO 03/008609 (2003-01-01), None
patent: WO 03/008610 (2003-01-01), None
patent: WO 03/008612 (2003-01-01), None
patent: WO 03/008613 (2003-01-01), None
patent: WO 03/008614 (2003-01-01), None
patent: WO 03/008615 (2003-01-01), None
patent: WO 03/038106 (2003-05-01), None
patent: WO 03/076635 (2003-09-01), None
patent: WO 03/076637 (2003-09-01), None
Andrews, et al., “Cloning, Sequencing, and Mapping of the Bacterioferritin Gene (bfr) ofEscherichia coliK-12,”J. Bacteriol. 171:3940-3947 (1989).
Blankenhorn, et al., “Acid- and Base-Induced Proteins during Aerobic and Anaerobic Growth ofEscherichia coliRevealed by Two-Dimensional Gel Electrophoresis,”J. Bacteriol. 181:2209-2216 (1999).
Blattner, et al., “The Complete Genome Sequence ofEscherichia coliK-12,”Science 277:1453-1462 (1997).
Boos, et al., “Maltose/Maltodextrin System ofEscherichia coli: Transport, Metabolism, and Regulation,”Microbiol. Mol. Biol. Rev. 62:204-229 (1998).
Brune, et al., “Cloning and Sequencing of the Adenylate Kinase Gene (adk) ofEscherichia coli,” Nucleic Acids Res. 13:7139-7151 (1985).
Carrier, et al., “Library of Synthetic 5′ Secondary Structures to Manipulate mRNA Stability inEscherichia coli,” Biotechnol. Prog. 15:58-64 (1999).
Clarke, et al., “Nucleotide Sequence of thepntAandpntBGenes Encoding the Pyridine Nucleotide Transhydrogenase ofEscherichia coli,” Eur. J. Biochem. 158:647-653 (1986).
Cole, et al., “The Nucleotide Sequence of themalTGene Encoding the Positive Regulator ofEscherichia coliMaltose Regulon,”Gene 42:201-208 (1986).
Danot, “A Complex Signaling Module Governs the Activity of MalT, the Prototype of an Emerging Transactivator Family,”Proc. Natl. Acad. Sci. USA 98:435-440 (2001).
DiRusso, “Nucleotide Sequence of thefadRGene, a Multifunctional Regulator of Fatty Acid Metabolism inEscherichia coli,” Nucleic Acids Res. 16:7995-8009 (1988).
Enos-Berlage, et al., “Complex Metabolic Phenotypes Caused by a Mutation inyigF, Encoding a Member of the Highly Conserved YER057c/YjgF Family of Proteins,”J. Bacteriol. 180:6519-6528 (1998).
Fountoulakis, et al., “Enrichment of Low Abundance Proteins ofEscherichia coliby Hydroxyapatite Chromatography,”Electrophoresis 20:2181-2195 (1999).
Franch, et al., “U-Turns and Regulatory RNAs,”Curr. Opin. Microbiol. 3:159-164 (2000).
Garrido-Pertierra, “Isolation and Properties ofSalmonella typhimuriumMutants Defective in Enolase,”Revista Española de Fisiologia 36:33-40 (1980).
Gulick, et al., “Evolution of Enzymatic Activities in the Enolase Superfamily: Crystal Structures of the L-Ala-D/L-Glu Epimerases fromEscherichia coliandBacillus subtilis,” Biochemistry 40:15716-15724 (2001).
Heim, et al., “Cloning anEscherichia coliGene Encoding a Protein Remarkably Similar to Mammalian Aldehyde Dehydrogenases,”Gene 99:15-23 (1991).
Hofnung, Divergent Operons and the Genetic Structure of the Maltose B Region inEscherichia coliK12,Genetics 76:169-184 (1974).
Hogg, et al., “Nucleotide Sequence and Analysis of themglOperon ofEscherichia coliK12,”Mol. Gen. Genet. 229:453-459 (1991).
Jensen, et al., “Artificial Promoters for Metabolic Optimization,”Biotechnol. Bioeng. 58:191-195 (1998).
Kaga, et al., “Rnase G-Dependent Degradation of theenomRNA Encoding a Clycolysis Enzyme Enolase inEscherichia coli,” Biosci. Biotechnol. Biochem. 66:2216-2220 (2002).
Kirkpatrick, et al., “Acetate and Formate Stress: Opposite Responses in the Proteome ofEscherichia coli,” J. Bacteriol. 183:6466-6477 (2001).
Klein, et al., “Cloning, Nucleotide Sequence, and Functional Expression of theEscherichia coliEnolase (eno) Gene in a Temperature-SensitiveenoMutant Strain,”J. Seq. Mapping 6:351-355 (1996).
Knappe, et al., “A Radical-Chemical Route to Acetyl-CoA: The Anaerobically Induced Pyruvate Formate-Lyase System ofEscherichia coli,” FEMS Microbiol. Rev. 75:383-398 (1990).
Komatsubara, et al., “Transductional Construction of a Threonine-Producing Strain ofSerratia marcescens,” Appl. Environ. Microbiol. 38:1045-1051 (1979).
Landgraf, et al., “The Role of H-NS is One Carbon Metabolism,”Biochimie 76:1063-1070 (1994).
Lee, et al., “Global Analysis of Transcriptomes and Proteomes of a Parent Strain and an L-Threonine-Overproducing Mutant Strain,”J. Bacteriol. 185:5442-5451 (2003).
Macpherson, et al., “Identification of the GalP Galactose Transport Protein ofEscherichia coli,” J. Biol. Chem. 258:4390-4396 (1983).
Martin, et al., “Forskolin Specifically Inhibits the Bacterial Galactose-H+Transport Protein, GalP,”J. Biol. Chem. 268:24870-24877 (1994).
Masuda, et al., “Improvement of Nitrogen Supply for L-Threonine Production by a Recombinant Strain ofSerratia marcescens,” Appl. Biochem. Biotechnol. 37:255-265 (1992).
McPherson, et al., “Complete Nucleotide Sequence of theEscherichia coli gdhAGene,”Nucleic Acids Res. 11:5257-5267 (1983).
Meyer, et al., Molecular Characterization of Glucokinase fromEscherichia coliK-12,J. Bacteriol. 179:1298-1306 (1997).
Missiakas, et al., “Modulation of theEscherichia colioE(RpoE) Heat-Shock Transcription-Factor Activity by the RseA, RseB and RseC Proteins,”Mol. Microbiol. 24:355-371 (1997).
Nagelkerke, et al., “2-Deoxygalactose, a Specific Substrate of theSalmonella typhimuriumGalactose Permease: Its Use for the Isolation ofgalPMutants,”J. Bacteriol. 133:607-613 (1978).
Niersbach, et al., “Cloning and Nucleotide Sequence of theEscherichia coliK-12ppsAGene, Encoding PEP Synthase,”Mol. Gen. Genet. 231:332-336 (1992).
Parsons, et al., “Solution Structure and Functional Ligand Screening of H10719, a Highly Conserved Protein from Bacteria to Humans in the YjgF/YER057c/UK114 Family,”

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