Chemistry: molecular biology and microbiology – Enzyme – proenzyme; compositions thereof; process for... – Hydrolase
Reexamination Certificate
2008-05-06
2008-05-06
Swope, Sheridan (Department: 1652)
Chemistry: molecular biology and microbiology
Enzyme , proenzyme; compositions thereof; process for...
Hydrolase
C510S300000
Reexamination Certificate
active
07368273
ABSTRACT:
An alkaline protease wherein an amino acid residue at (a) position 65, (b) position 101, (c) position 163, (d) position 17-0, (e) position 171, (f) position 273, (g) position 320, (h) position 359 or (i) position 387 of SEQ. ID NO: 2 or at a position corresponding thereto has been selected from the following amino acid residues: position (a): proline, position (b): asparagine, position (e): histidine, aspartic acid, phenylalanine, lysine, asparagine, seine, isoleucine, leucine, glutamine, threonine and valine, position (d): valine and leucine, position (e): alanine, glutamic acid, glycine and threonine, position (K): isoleucine, glycine and threonine, position (g): phenylalanine, valine, threonine, leucine, isoleucine and glycine, position (h): seine, leucine, valine, isoleucine and glutamine, position (i): alanine, lysine, glutamine, glutamic acid, arginine and histidine. A method to an alkaline protease having activity even in the presence of a highly concentrated fatty acid, and exhibiting excellent detergency for the removal of a complex stain containing protein, sebum and the like, and therefore useful as an ingredient in a detergent.
REFERENCES:
patent: 5891701 (1999-04-01), Sloma et al.
patent: 2003/0022351 (2003-01-01), Hatada, et al.
patent: 1 209 233 (2002-05-01), None
patent: WO 98/56927 (1998-12-01), None
patent: WO 99/18218 (1999-04-01), None
Witkowski et al, Conversion of a beta-ketoacyl synthase to a malonyl decarboxylase by replacement of the active-site cysteine with glutamine. Biochemistry. Sep. 7, 1999;38(36):11643-11650.
Wishart et al, A single mutation converts a novel phosphotyrosine binding domain into a dual-specificity phosphatase. J Biol Chem. Nov. 10, 1995;270(45):26782-26785.
Issued—Patents—NA Database US 5,891,701 Apr. 6, 1999 Sloma et al SEQ ID No. 41. Alignment with SEQ ID No. 2.
GenEmbl Database Accession No. AB046406 Jan. 23, 2001 from Saeki et al Biochem Biophys Res Commun. Dec. 20, 2000;279(2):313-9.
Ito et al, Alkaline detergent enzymes from alkaliphiles. enzymatic properties, genetics, and structures. Extremophiles. Aug. 1998;2(3):185-90. Review.
R. J. Siezen, et al., Protein Science, vol. 6, No. 3, pp. 501-523, XP-000856203, “Subtilases: The Superfamily of Subtilisin-Like Serine Proteases”, Mar. 1997.
K. Saeki, et al., Database Genbank ′Online !, NCBI; Database Accession No. AB046402, 1 page, XP-002260452, “PROA Protease FromBacillussp. D6”, retrieved from Genbank, Jun. 16, 2001.
K. Saeki, et al., Database Genbank ′Online !, NCBI; Database Accession No. AB046404, 1 page, XP-002260453, “Proc Protease FromBacillussp. Y”, retrieved from Genbank, Jan. 23, 2001.
K. Saeki, et al., Database Genbank ′Online !, NCBI; Database Accession No. AB046405, 1 page, XP-002260454, “Prod Protease FromBacillussp. SD521”, retrieved from Genbank, Jan. 23, 2001.
K. Saeki, et al., Database Genbank ′Online !, NCBI; Database Accession No. AB046406, 1 page, XP-002260455, “Proe Protease FromBacillussp. NV1”, retrieved from Genbank, Jan. 23, 2001.
K. Saeki, et al., Biochemical and Biophysical Research Communications, vol. 279, pp. 313-319, “Novel Oxidatively Stable Subtilisin-Like Serine Proteases from AlkaliphilicBacillusSpp.: Enzymatic Properties, Sequences, and Evolutionary Relationships”, 2000.
J. A. Wells, et al., Proc. Natl. Acad. Sci., vol. 84, pp. 1219-1223, “Designing Substrate Specificity by Protein Engineering of Electrostatic Interactions”, Mar. 1987.
J. A. Wells, et al., Proc. Natl. Acad. Sci., vol. 84, pp. 5167-5171, “Recruitment of Substrate-Specificity Properties From One Enzyme into a Related One by Protein Engineering”, Aug. 1987.
S. Taguchi, et al., Applied and Environmental Microbiology, vol. 64, No. 2, pp. 492-495, “Engineering of a Cold-Adapted Protease by Sequential Random Mutagenesis and a Screening System”, Feb. 1998.
H. Takagi, et al., Protein Engineering, vol. 11, No. 12, pp. 1205-1210, “Random Mutagenesis into the Conserved GLY 154 of Subtilisin E: Isolation and Characterization of the Reverant Enzymes”, 1998.
P. N. Bryan, Biochimica et Biophysica Acta, Vol. 1543, pp. 203-222, “Protein Engineering of Subtilisin”, 2000.
H. Takagi, et al., The Journal of Biological Chemistry, vol. 263, No. 36, pp. 19592-19596, “Mutant Subtilisin E With Enhanced Protease Activity Obtained by Site-Directed Mutagenesis”, 1988.
U.S. Appl. No. 09/985,689, filed Nov. 5, 2001, Hatada et al.
U.S. Appl. No. 10/385,662, filed Mar. 12, 2003, Okuda et al.
U.S. Appl. No. 10/456,479, filed Jun. 9, 2003, Sato et al.
Izawa Yoshifumi
Kobayashi Tohru
Nomura Masafumi
Okuda Mitsuyoshi
Saeki Katsuhisa
Kao Corporation
Oblon & Spivak, McClelland, Maier & Neustadt P.C.
Swope Sheridan
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