Polypeptide having amidase activity and gene thereof

Chemistry: molecular biology and microbiology – Enzyme – proenzyme; compositions thereof; process for... – Hydrolase

Reexamination Certificate

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Details

C536S023100, C536S023200, C435S252330, C435S071100, C435S320100

Reexamination Certificate

active

07655450

ABSTRACT:
It is an object of the present invention to provide a novel amidase that is useful for production of an optically active amino acid, and in particular, a D-amino acid, and a production method thereof.The present invention relates to a novel D-amidase isolated and purified from theArthrobactersp. KNK1101J, a gene encoding the above amidase, a recombinant plasmid comprising the above gene, and a transformant into which the above amidase gene has been introduced. In addition, the present invention also relates to a method for producing the amidase, comprising culturing theArthrobactersp. KNK1101J or the above transformant, and collecting the above amidase.

REFERENCES:
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patent: 2004/0023257 (2004-02-01), Barton et al.
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Galye et al, Identification of regions in interleukin-1 alpha important for activity. J Biol Chem. Oct. 15, 1993;268(29):22105-11.
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Barton et al, US20040023257, Filing Date: Jan. 20, 2003 Seq ID No. 113&114. Alignment with Seq ID No. 1 & 3.
Takegawa et al, Cloning, sequencing, and expression of Arthrobacter protophormiae endo-beta-N-acetylglucosaminidase inEscherichia coli. Arch Biochem Biophys. Feb 1, 1997;338(1):22-8.
Ozaki, A. et al., “A D-Amidase Constitutive Mutant fromArthrobactersp. NJ-26,” Bioscience Biotechnology Biochemistry, vol. 57, No. 3, 1993, pp. 520-521.
International Preliminary Report on Patentability (Chapter I of the Patent Cooperation Treaty) from Corresponding International Application No. PCT/JP2005/000951, dated Sep. 19, 2006, 7 pages.
Y. Asano, et al., “Purification and Characterization of Amidase which Participates in Nitrile Degradation,”Agric. Biol. Chem., 46(5), 1175-81 (1982).
D.H. Baek, “Characterization of a Thermostable D-Stereospecific Alanine Amidase fromBrevibacillus borstelensisBCS-1,”Appl. Environ. Microbiol., 69(2) 980-86 (2003).
H. Komeda et al., “Gene Cloning, Nucleotide Sequencing, and Purification and Characterization of the D-Stereospecific Amino-acid Amidase fromOchrobactrum anthropiSV3,”Eur. J. Biochem.,267(7), 2028-35 (2000).
A. Ozaki, et al., “Enzymatic Production of D-Alanine from DL-Alaninamide by Novel D-Alaninamide Specific Amide Hydrolase,”Biosci. Biotech. Biochem., 56(12), 1980-84 (1992).

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