Chemistry: molecular biology and microbiology – Enzyme – proenzyme; compositions thereof; process for...
Reexamination Certificate
2007-05-01
2007-05-01
Slobodyansky, Elizabeth (Department: 1652)
Chemistry: molecular biology and microbiology
Enzyme , proenzyme; compositions thereof; process for...
C536S023200
Reexamination Certificate
active
11253665
ABSTRACT:
L-arginine, citrulline and pyrimidine derivatives including orotic acid, uridine, uridine 5′-monophosphate (UMP), cytidine and cytidine 5′-monophosphate (CMP) are produced using a bacterium belonging to the genusEscherichiaharboring a mutant carbamoylphosphate synthetase in which the amino acid sequence corresponding to positions from 947 to 951 in a wild type carbamoylphosphate synthetase is replaced with any one of amino acid sequences of SEQ ID NOS: 1 to 9, and feedback inhibition by uridine 5′-monophosphate in the bacterium is desensitized.
REFERENCES:
H. Nyunoya, et al., “The carB Gene ofEscherichia coli: A Duplicated Gene Coding for the Large Subunit of Carbamoyl-Phosphate Synthetase”, Proc. Natl. Acad. Sci., USA, vol. 80, Aug. 1983, pp. 4629-4633.
J. Thoden, et al., “Structure of Carbamoyl Phosphate Synthetase: A Journey of 96 Å from Substrate to Product”, Biochemistry, 1997, 36, pp. 6305-6316.
J. Thoden, et al., “The Structure of Carbamoyl Phosphate Synthetase Determined to 2.1 Å Resolution”, Acta Crystallographica Section D, vol. 55, 1999, pp. 8-24.
S. Delannay, et al., “Serein 948 and Threonine 1042 are Crucial Residues for Allosteric Regulation ofEscherichia coliCarbamoylphosphate Synthetase and Illustrate Coupling Effects of Activation and Inhibition Pathways” J. Mol. Biol., 1999, 286, pp. 1217-1228.
F. Blattner, et al., , Science, Accession No. AE000113 U00096, 1997, pp. 1-8. (Abstract Only of vol. 277, No. 5331, pp. 1453-1474).
Altman Irina Borisovna
Gusyatiner Mikhail Markovich
Kotliarova Veronika Aleksandrovna
Novikova Anna Eugenievna
Ptitsyn Leonid Romanovich
Ajinomoto Co. Inc.
Slobodyansky Elizabeth
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