Chemistry: molecular biology and microbiology – Micro-organism – per se ; compositions thereof; proces of... – Bacteria or actinomycetales; media therefor
Reexamination Certificate
2001-05-01
2003-10-28
Prouty, Rebecca E. (Department: 1652)
Chemistry: molecular biology and microbiology
Micro-organism, per se ; compositions thereof; proces of...
Bacteria or actinomycetales; media therefor
C435S252320, C435S320100, C435S193000, C536S023100, C536S024300
Reexamination Certificate
active
06638753
ABSTRACT:
PRIOR ART
Amino acids, in particular L-lysine and L-glutamate, are used in human medicine, in the pharmaceuticals industry, in the foodstuffs industry, but in particular in animal nutrition.
It is known that amino acids are produced by fermentation from strains of coryneform bacteria, in particular
Corynebacterium glutamicum.
Because of their great importance, work is constantly being undertaken to improve the preparation methods. Improvements to the methods can relate to fermentation measures, such as e. g. stirring and supply of oxygen, or the composition of the nutrient media, such as e. g. the sugar concentration during the fermentation, or the working up to the product form by e.g. ion exchange chromatography, or the intrinsic output properties of the microorganism itself.
Methods of mutagenesis, selection and mutant selection are used to improve the output properties of these microorganisms. Strains which are resistant to antimetabolites, such as e.g. the lysine analogue S-(2-aminoethyl)-cysteine, or are auxotrophic for metabolites of regulatory importance and produce L-amino acids, such as e. g. L-lysine or L-glutamate, are obtained in this manner.
Methods of the recombinant DNA technique have also been employed for some years for improving the strain of Corynebacterium strains which produce amino acids, by amplifying individual amino acid biosynthesis genes and investigating the effect on the amino acid production. Review articles in this context are to be found, inter alia, in Kinoshita (“Glutamic Acid Bacteria”, in: Biology of Industrial Microorganisms, Demain and Solomon (Eds.) I.B.R., Benjamin Cummings, London, UK, 1985, 115-142), Hilliger (BioTec 2, 40-44 (1991)) I.B.R., Eggeling (Amino Acids 6:261-272 (1994)) I.B.R., Jetten and Sinskey (Critical Reviews in Biotechnology 15, 73-103 (1995)) I.B.R. and Sahm et al. (Annuals of the New York Academy of Science 782, 25-39 (1996)) I.B.R.
OBJECT OF THE INVENTION
The object of the present invention was to provide new aids for improved fermentative preparation of amino acids, in particular L-lysine and L-glutamate.
This object is achieved by a genetically modified coryneform bacterium, the cma gene of which, which codes for cyclopropane-mycolic acid synthase, is amplified.
Amino acids, in particular L-lysine and L-glutamate, are used in human medicine, in the pharmaceuticals industry, in the foodstuffs industry, and in particular in animal nutrition. There is therefore a general interest in providing new improved methods for the preparation of amino acids, in particular L-lysine and L-glutamate.
When L-lysine or lysine and L-glutamate or glutamate are mentioned in the following, not only the bases but also the salts, such as e. g. lysine monohydrochloride or lysine sulfate, are also meant by this.
SUMMARY OF THE INVENTION
The new DNA sequence of
C. glutamicum
which codes for the cma gene and which as a constituent of the present invention is SEQ ID NO 1 and related sequences. The amino acid sequence of the corresponding gene product of the cma gene has furthermore been derived from the present DNA sequence. The resulting amino acid sequence of the cma gene product is SEQ ID NO 2 and related sequences.
REFERENCES:
patent: 6441151 (2002-08-01), Gordon-Kamm et al.
Pub. No. US202/0197605 A1, Nakagawa S. et al, Novel polynucleotides, Dec. 26, 2002.*
Sulton J. E. et al. Toward a Complete Human Genome Sequence, Genome Research, 1998, 8/11, 1097-1108.
Eggeling Lothar
Möckel Bettina
Nampoothiri K. Madhavan
Sahm Hermann
Degussa - AG
Prouty Rebecca E.
Smith Gambrell & Russell
Walicka Malgorzata
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