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
2002-03-26
2004-10-05
Achutamurthy, Ponnathapu (Department: 1652)
Chemistry: molecular biology and microbiology
Micro-organism, tissue cell culture or enzyme using process...
Preparing alpha or beta amino acid or substituted amino acid...
C435S183000, C435S196000, C435S252300, C435S320100, C536S023200
Reexamination Certificate
active
06800464
ABSTRACT:
CROSS-REFERENCE TO RELATED APPLICATIONS
This application claims priority to German priority document 101 14 999.9, filed Mar. 26, 2001, that is hereby incorporated by reference.
REFERENCE TO SEQUENCE LISTING
The computer-readable sequence(s) on the attached compact disk are hereby incorporated by reference.
BACKGROUND OF THE INVENTION
1. Field of the Invention
D-carbamoylases and polypeptides having D-carbamoylase activity, especially those from Arthrobacter. D-carbamoylases that are more economical, efficient and conveniently used in commercial and industrical processes, such as those with superior activity or stability. Nucleic acids, vectors and host cells encoding or expressing these D-carbamoylases. Methods for making an enantiomerically enriched or purified amino acid using such a D-carbamoylase and methods for identifying and isolating a gene, gene cluster or operon encoding a D-carbamoylase.
2. Description of Related Art
Carbamoylases are enzymes which are capable of converting N-carbamoylamino acids stereoselectively into the L- or D-amino acid, while retaining the enantiomeric carbamoylamino acid, see equation 1 in FIG.
10
.
Racemic N-carbamoylamino acids can preferably be obtained quite easily from hydantoins by means of hydantoinases or by reaction of amino acids with KOCN, and for this reason such processes are used on an industrial scale for the preparation of enantiomerically concentrated amino acids (Drauz K, Kottenhahn M, Makryaleas K, Klenk H, Bernd M, Angew Chem, (1991). Chemoenzymatic synthesis of D-&ohgr;-ureidoaminoacids, 103, 704-706; See Equation 2 in FIG.
11
.
D-Carbamoylases are known in the literature (Syldatk et al. in “Enzymatic Catalysis in Organic Synthesis”, eds.: Drauz, Waldmann, VCH, 1
st
and 2
nd
Ed.), but these mostly do not work very efficiently or are unstable (Syldatk C, Müller R, Pietzsch M, Wagner F (1992). Biocatalytic production of amino acids & derivatives; eds.: Rozzell D, Wagner F, Hanser Publishers, Munich; 129-176; Louwrier A, Knowles C. J. (1996). The purification and characterization of a novel D-specific carbamoylase enzyme from Agrobacterium sp. Enzyme Microb Technol. 19; 562-571; Nanba H, Ikenaka Y, Yamada Y, Yajima K, Takano M Takahashi S (1998). Isolation of Agrobacterium sp. strain KNK712 that produces N-carbamyl-D-amino acid amidohydrolase, cloning of the gene for this enzyme, and properties of the enzyme. Biosci. Biotechnol. Biochem. 62 (5) 875-881; Kim D. M., Kim G. J., Kim H. S. (1994). Biotechnol Lett, (16) 11-16). Accordingly, there is a need for further improved carbamoylases, such as those with improved stability or activity.
BRIEF SUMMARY OF THE INVENTION
The present invention encompasses D-carbamoylases and polypeptides having D-carbamoylase activity, especially those from Arthrobacter. These D-carbamoylases provide a more economical, efficient and conveniently usable D-carbamoylase, for instance, a D-carbamoylase with superior stability or activity. The invention also encompasses nucleic acids encoding such a D-carbamoylases or polypeptide having a D-carbamoylase activity, as well as plasmids and microorganisms encompassing such a nucleic acid sequence. Methods for making an enantiomerically enriched or purified amino acid using such a D-carbamoylase and methods for identifying and isolating a gene, gene cluster or operon encoding a D-carbamoylase are also described.
The use of an enzymatic process for the synthesis of an organic compound, such as a D-amino acid is advantageous, particularly for large scale industrial process, since such a process often provides a superior product yield and improved reactant or product selectivity compared to a conventional chemical process. In nature, enzymatic process are of decisive importance, for instance, in the biosynthesis of proteins such as albumins. Accordingly, an efficient and convenient enzymatic process for producing enantiomerically concentrated amino acids is a preferred target of the present invention. Enantiomerically concentrated amino acids are important products for the synthesis of bioactive compounds or for the production of other products, such as those used for parenteral feeding.
REFERENCES:
patent: WO 94/00577 (1994-01-01), None
patent: WO94/00577 (1994-01-01), None
Attwood et al. Which craft is best in bioinformatics? Comput. Chem. 2001, vol. 25(4), pp. 329339.*
Ponting, C.P. Issues in predicting protein function from sequence. Brief. Bioinform. Mar. 2001, vol. 2(1), pp. 1929.*
Nelson et al. Accession AAQ54838. Jul. 7, 1994.*
D.-M. Kim, et al., Biotechnology Letters, vol. 16, No. 1, pp. 11-16, “Enhancement of Operational Stability of Immobilized Whole Cell D-Hydantoinase”, Jan. 1994.
A. Louwrier, et al., Enzyme and Microbial Technology, vol. 19, pp. 562-571, “The Purification and Characterization of a Novel D(—)-Specific Carbamoylase Enzyme from an Agrobacterium sp.”, Dec. 1996.
C. Syldatk, et al., Habilitationsarbeit, pp. 131-175, “Microbial and Enzymatic Production of L-Amino Acids from DL-5-Monosubstituted Hydantoins”, 1990.
H. Nanba, et al., Biosci. Biotechnol. Biochem., vol. 62, No. 5, pp. 875-881, “Isolation of Agrobacterium sp. Strain KNK712 that Produces N-Carbamyl-D-Amino Acid Amidohydrolase, Cloning of the Gene for this Enzyme, and Properties of the Enzyme”, 1998.
Syldatk, et al., Editors: Drauz & Waldmann, 1st and 2nd Edition, pp. 409-433 and 486-495, “Enzyme Catalysis in Organic Synthesis”.
A. Moeller, et al., Enzyme and Microbial Technology, vol. 10, No. 10, pp. 618-625, XP-008007367, “Stereo-and Substrate-Specificity of a D-Hydantoinase and a D-N-Carbamyl-Amino Acid Amidohydrolase ofArthrobacter CrystallopoietesAM 2”,, Jul. 1988.
R. Grifantini, et al., Microbiology, vol.144, No. 4, pp. 947-954, XP-002154848, “Efficient Conversion of 5-Substituted Hydantoins to D-&agr;-Amino Acids Using RecombinantEscherichia coliStrains”, Apr. 1998.
Y. Ikenaka, et al., Bioscience, Biotechnology, and Biochemistry, vol. 62, No. 5, pp. 882-886, XP-001074193, “Screening, Characterization, and Cloning of the Gene for N-Carbamyl-D-Amino Acid Amidohydrolase from Thermotolerant Soil Bacteria”, May 1998.
A. Buson, et al., FEMS Microbiology Letters, vol. 145, pp. 55-62, XP-002934364, “Identification, Sequencing and Mutagenesis of the Gene for a D-Carbamoylase fromAgrobacterium Radiobacter”, 1996.
H. Nanba, et al., Bioscience, Biotechnology, and Biochemistry, vol. 62, No. 5, pp. 875-881, XP-001074192, “Isolation of Agrobacterium sp. Strain KNK712 that Produces N-Carbamyl-D-Amino Acid Amidohydrolase, Cloning of the Gene for this Enzyme and Properties of the Enzyme”, May 1998.
C. Syldatk, et al., Biocatalytic Production of Amino Acids and Derivatives, pp. 75-128, XP-000991524, “Microbial and Enzymatic Production of D-Amino Acids from DL-5-Monosubstituted Hydantoins”, 1992.
Altenbuchner Josef
Bommarius Andreas
Drauz Karlheinz
May Oliver
Siemann-Herzberg Martin
Achutamurthy Ponnathapu
Degussa - AG
Fronda Christian L.
Oblon & Spivak, McClelland, Maier & Neustadt P.C.
LandOfFree
Arthrobacter D-carbamoylase and methods of preparing... does not yet have a rating. At this time, there are no reviews or comments for this patent.
If you have personal experience with Arthrobacter D-carbamoylase and methods of preparing..., we encourage you to share that experience with our LandOfFree.com community. Your opinion is very important and Arthrobacter D-carbamoylase and methods of preparing... will most certainly appreciate the feedback.
Profile ID: LFUS-PAI-O-3309419