Chemistry: molecular biology and microbiology – Micro-organism – tissue cell culture or enzyme using process... – Preparing oxygen-containing organic compound
Reexamination Certificate
2006-07-25
2006-07-25
Patterson, Jr., Charles L. (Department: 1652)
Chemistry: molecular biology and microbiology
Micro-organism, tissue cell culture or enzyme using process...
Preparing oxygen-containing organic compound
C435S410000, C435S468000, C435S320100
Reexamination Certificate
active
07081357
ABSTRACT:
The gene encoding a 4-hydroxybutyryl-CoA transferase has been isolated from bacteria and integrated into the genome of bacteria also expressing a polyhydroxyalkanoate synthase, to yield an improved production process for 4HB-containing polyhydroxyalkanoates using transgenic organisms, including both bacteria and plants. The new pathways provide means for producing 4HB containing PHAs from cheap carbon sources such as sugars and fatty acids, in high yields, which are stable. Useful strains are obtaining by screening strains having integrated into their genomes a gene encoding a 4HB-CoA transferase and/or PHA synthase, for polymer production. Processes for polymer production use recombinant systems that can utilize cheap substrates. Systems are provided which can utilize amino acid degradation pathways, α-ketoglutarate, or succinate as substrate.
REFERENCES:
patent: 4430430 (1984-02-01), Momose et al.
patent: 4876331 (1989-10-01), Doi
patent: 5245023 (1993-09-01), Peoples et al.
patent: 5250430 (1993-10-01), Peoples et al.
patent: 5286842 (1994-02-01), Kimura
patent: 5292860 (1994-03-01), Shiotani et al.
patent: 5378616 (1995-01-01), Tujimoto et al.
patent: 5461139 (1995-10-01), Gonda et al.
patent: 5502273 (1996-03-01), Bright et al.
patent: 5516883 (1996-05-01), Hori et al.
patent: 5534432 (1996-07-01), Peoples et al.
patent: 5563239 (1996-10-01), Hubbs et al.
patent: 5602321 (1997-02-01), John
patent: 5610041 (1997-03-01), Somerville et al.
patent: 5650555 (1997-07-01), Somerville et al.
patent: 5663063 (1997-09-01), Peoples et al.
patent: 6117658 (2000-09-01), Dennis et al.
patent: 2006506 (1998-03-01), None
patent: 91/00917 (1991-01-01), None
patent: 93/02187 (1992-07-01), None
patent: 93/02194 (1992-07-01), None
patent: 92/19747 (1992-11-01), None
patent: 93/06225 (1993-04-01), None
patent: 94/11519 (1994-05-01), None
patent: 94/12014 (1994-06-01), None
patent: 94/20614 (1994-11-01), None
patent: 94/20615 (1995-08-01), None
patent: 96/20621 (1996-07-01), None
Abe, et al., “Biosynthesis from gluconate of a random copolyester consisting of 3-hydroxybutyrate and medium-chain-length 3-hydroxyalkanoates byPseudomonas sp. 61-3.,”Int. J. Biol. Macromol. 16:115-119 (1994).
Aidoo, et al., “Coling, sequencing and disruption of a gene fromStreptomyces clavuligerusInvolved in clavulanic acid biosynthesis,”Gene147:41 (1994).
Allen, et al., “DNA sequence of the putA gene fromSalmonella typhimurium: a bifunctional membrane-associated dehydrogenase that binds DNA,”Nucleic Acids Res. 21:1676 (1993).
Amarasingham & Davis, “Regulation of alpha-ketoglutarate dehydrogenase formation inEscherichia coli,”J. Biol. Chem. 240: 3664-3668 (1965).
Amos & McInerey, “Composition of poly-β-hydroxyalkanoate fromSyntrophomonas wotteigrown on unsaturated fatty acid substrates,”Arch. Microbiol. 155:103-06 (1991).
Amuro, et al., “Isolation and characterization of the two distinct genes for human glutamate dehydrogenase,”Biochem. Biophys. Acta1049:216-218 (1990).
André and Jauniaux, “Nucleotide sequence of the yeast UGA1 gene encoding GABA transaminase,”Nucl. Acid Res. 18:3049 (1990).
Bartsch, et al., “Molecular analysis of two genes of theEscherichia coligab cluster: nucleotide sequence of the glutamate:succinic semlaidehyde transaminase gene (gabT) and characterization of the succinic semiaidehyde dehydrogenase gene (gabD),”J. Bacteriol. 172:7035-7042 (1990).
Baum, et al., “A plant glutamate decarboxylase containing a calmodulin binding domain, Cloning, sequence, and functional analysis,”J. Biol. Chem. 268:19610-19617 (1993).
Bell and Malmberg, “Analysis of a cDNA encoding arginine decarboxylase from oat reveals similarity to theEscherichia coliarginien decarboxylase and evidence of protein processing,”Mol. Gen. Genet. 224:431 (1990).
Benachenhous-Lahfa, et al., “PCR-mediated cloning and sequencing of the gene encoding glutamate dehydrogenase from the archaeon Sulfolobus shilbatae: Identification of putative amino-acid signatures for extremophilic adaptation,”Gene140:17-24 (1994).
Blattner, et al., “The complete genome sequence ofEscherichia coliK-12,”Science 277:1453 (1997).
Botsford, et al., “Acculmulation of glutamate bySalmonella typhimuriumin response to osmotic stress,”Appl. Environ. Microbiol. 60:2568 (1994).
Brandl, et al., “Ability of the phototrophic bacteriumRhodospirillum rubrumto produce various poly (beta-hydroxyalkanoates): potential sources for biodegradable polyesters,”Int. J. Biol. Macromol. 11:49-55 (1989).
Bu, et al., “the exon-intron organization of the genes (GAD1 and GAD2) encoding two human glutamate decarboxylases (GAD67 and GAD65) suggests that they derive from a common ancestral GAD,”Genomics21:222-228 (1994).
Bult, et al., “Complete genome sequence of the methanogenic archaeon,Methanococcus jarnnaschil,”Science723:1058-1073 (1996).
Chang, et al., “Nucleotide Sequence of cDNA (Accession No. U63832) Encoding Arginine Decarboxylase from Camation Flowers,”Plant Physiol. 112:863 (1996).
Chavez, et al., “The NADP-glutamate dehydrogenase of the cyanobacterium Synechocystis 6803: cloning, transcriptional analysis and disruption of the gdhA gene,”Plant Mol. Biol. 28:173-188 (1995).
Chen & Maloy, “Regulation of proline utilization in enteric bacteria: cloning and characterization of the Kiebsiella put control region,”J. Bacteriol. 173:783 (1991).
Cho, et al., “Identification ofAgrobacterium tumefaciensgenes that direct the complete catabolism of octopine,”J. Bacteriol. 178:1872 (1996).
Chu, et al., “Enzymatically active truncated cat brain glutamate decarboxylase: expression, purification, and absorption spectrum,”Arch. Biochem. Biophys. 313:287-295 (1994).
Cock, et al., “A nuclear gene with many introns encoding ammonium-inductible chloroplastic NADP-specific glutamate dehydrogenase(s) inChlorella sorokiniana,”Plant Mol. biol. 17:1023-144 (1991).
Cogoni, et al., “Saccharomyces cerevisiaehas a single glutamate synthase gene coding for a plant-like high-molecular-weight polypeptide,”J. Bacteriol. 177:792 (1995).
Cole, et al., “Deciphering the biology ofMycobacterium tuberculosisfrom the complete genome sequence,”Nature393:537 (1998).
Deckert, et al., “The complete genome of the hyperthermophilic bacteriumAquifex aeolicus,”Nature392:353 (1998).
Delauney & Verma, “A soybean gene encoding delta 1-pyrroline-5-carboxylate reductase was isolated by functional complementation inEscherichia coliand is found to be osmoregulated,”Mol. Gen. Genet. 221:299 (1990).
Desmet, et al., “Characterization of intracellular inclusions formed byPseudomonas oleovoransduring growth on octane,”J. Bacteriol. 154:870-878 (1983).
Diruggiero, et al., “Expression and in vitro assembly of recombinant glutamate dehydrogenase from the hyperthermophilic archaeonPyrococcus turiosus,”Appl. Environ. Microbiol. 61:159-164 (1995).
Doi, “Microbial Synthesis, Physical Properties, and Biodegradability of Polyhydroxyalkanoates,”Macromol. Symp. 98:585-599 (1995).
Doi, et al., “biosynthesis and characterization of poly(3-hydroxybutyrate-co-4-hydroxybutyrate) inAlcaligenes eutrophus,”Int. J. Biol. Macromol. 12: 106 (1990).
Doi, et al., “Nuclear Magnetic Resonance Studies on Unusual Bacterial Copolyesters of 3-Hydroxybutyrate and 4-Hydroxybutyrate,”Macromolecules21:2722-2727 (1988).
Duncan, et al., “Purification and properties of NADP-dependent glutamate dehydrogenase fromRuminococcus flavefaciensFD-1,”Appl. Environ. Microbiol. 58:4032-4037 (1992).
Eggen, et al., “The glutamate dehydrogenase-encoding gene of the hyperthermophilic archaeonPyrococcus furiosus: sequence, transcription and analysis of the deduced amino acid sequence,”Gene132:143-148 (1
Huisman Gjalt W.
Martin David P.
Peoples Oliver P.
Skraly Frank
Metabolix Inc.
Pabst Patent Group LLP
Patterson Jr. Charles L.
LandOfFree
Biological systems for manufacture of polyhydroxyalkanoate... does not yet have a rating. At this time, there are no reviews or comments for this patent.
If you have personal experience with Biological systems for manufacture of polyhydroxyalkanoate..., we encourage you to share that experience with our LandOfFree.com community. Your opinion is very important and Biological systems for manufacture of polyhydroxyalkanoate... will most certainly appreciate the feedback.
Profile ID: LFUS-PAI-O-3528504