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1. (WO2000063388) NOVEL DESENSITIZED ASPARTOKINASE
Latest bibliographic data on file with the International Bureau   

Pub. No.:    WO/2000/063388    International Application No.:    PCT/JP2000/002456
Publication Date: 26.10.2000 International Filing Date: 14.04.2000
Chapter 2 Demand Filed:    02.11.2000    
IPC:
C12N 9/12 (2006.01), C12P 13/08 (2006.01)
Applicants: KYOWA HAKKO KOGYO CO., LTD. [JP/JP]; 6-1, Ohtemachi 1-chome, Chiyoda-ku, Tokyo 100-8185 (JP) (For All Designated States Except US).
YOKOI, Haruhiko [JP/JP]; (JP) (For US Only).
OHNISHI, Junko [JP/JP]; (JP) (For US Only).
OCHIAI, Keiko [JP/JP]; (JP) (For US Only).
YONETANI, Yoshiyuki [JP/JP]; (JP) (For US Only).
OZAKI, Akio [JP/JP]; (JP) (For US Only)
Inventors: YOKOI, Haruhiko; (JP).
OHNISHI, Junko; (JP).
OCHIAI, Keiko; (JP).
YONETANI, Yoshiyuki; (JP).
OZAKI, Akio; (JP)
Priority Data:
11/110437 19.04.1999 JP
Title (EN) NOVEL DESENSITIZED ASPARTOKINASE
(FR) NOUVELLE ASPARTOKINASE DESENSIBILISEE
Abstract: front page image
(EN)A novel aspartokinase originating in a coryneform bacterium; a DNA encoding this enzyme; a recombinant DNA containing the above DNA; a coryneform bacterium having the above recombinant DNA or a coryneform bacterium having the DNA on its chromosome; and a process for producing L-lysine by culturing the above microorganism. Construction has been successfully made of a DNA encoding an aspartokinase with the relief of the synergistic feedback inhibition by L-lysine and L-threonine which originates in a corynebacterium and has a base sequence wherein the amino acid residue at the 311-position in the amino acid sequence represented by SEQ ID NO:18 is an amino acid other than Thr.
(FR)L'invention concerne une nouvelle aspartokinase provenant d'une bactérie du type coryne, un ADN codant cet enzyme; un ADN recombinant renfermant l'ADN précité; une bactérie du type coryne possédant l'ADN recombinant ou une bactérie du type coryne possédant l'ADN sur son chromosome; et un procédé de production de L-lysine par culture du micro-organisme précité. La construction a été réalisée avec succès à partir d'un ADN codant une aspartokinase avec l'assistance de la rétro-inhibition synergique par L-lysine et L-thréonine qui provient d'un corynebacterium et présente une séquence base dans laquelle le résidu d'acide aminé à la position 311 dans la séquence acide aminé représentée par SEQ ID NO: +18 est un acide aminé autre que Thr.
Designated States: AE, AG, AL, AM, AT, AU, AZ, BA, BB, BG, BR, BY, CA, CH, CN, CR, CU, CZ, DE, DK, DM, DZ, EE, ES, FI, GB, GD, GE, GH, GM, HR, HU, ID, IL, IN, IS, JP, KE, KG, KR, KZ, LC, LK, LR, LS, LT, LU, LV, MA, MD, MG, MK, MN, MW, MX, NO, NZ, PL, PT, RO, RU, SD, SE, SG, SI, SK, SL, TJ, TM, TR, TT, TZ, UA, UG, US, UZ, VN, YU, ZA, ZW.
African Regional Intellectual Property Organization (GH, GM, KE, LS, MW, SD, SL, SZ, TZ, UG, ZW)
Eurasian Patent Organization (AM, AZ, BY, KG, KZ, MD, RU, TJ, TM)
European Patent Office (AT, BE, CH, CY, DE, DK, ES, FI, FR, GB, GR, IE, IT, LU, MC, NL, PT, SE)
African Intellectual Property Organization (BF, BJ, CF, CG, CI, CM, GA, GN, GW, ML, MR, NE, SN, TD, TG).
Publication Language: Japanese (JA)
Filing Language: Japanese (JA)