Mutant glucose dehydrogenase

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

Reexamination Certificate

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C435S004000, C435S006120, C435S026000, C435S069100, C435S071100, C435S252300, C435S320100, C435S440000, C536S023200

Reexamination Certificate

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07604969

ABSTRACT:
A mutant glucose dehydrogenase having an improved substrate specificity to glucose, which is a protein comprising the amino acid sequence depicted in SEQ ID NO:3 or an amino acid sequence having the substitution, deletion, insertion or addition of one or more amino acid residues excluding amino acid 365 in the amino acid sequence depicted in SEQ ID NO:3 and having a glucose dehydrogenase activity, the amino acid residue corresponding to amino acid 365 being substituted by other amino acid residue.

REFERENCES:
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patent: 2006/0019328 (2006-01-01), Sode
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patent: 2003-274964 (2003-09-01), None
patent: WO 02/34919 (2002-05-01), None
Sode et al. Elucidation of the region responsible for EDTA tolerance in PQQ glucose dehydrogenases by constructingEscherichia coliand Acinetobacter calcoaceticus chimeric enzymes. Biochem Biophys Res Commun. Jun. 6, 1995;211(1):268-73.
Branden et al. Introduction to Protein Structure, Garland Publishing Inc., New York, p. 247, 1991.
Inose, et al., “Cloning and Expression of the Gene Encoding Catalytic Subunit of Thermostable Glucose Dehydrogenase fromBurkholderia cepaciainEscherichia coli,” Biochimica et Biophysica Acta, vol. 1645, pp. 133-138, 2003.
International Search Report dated Aug. 30, 2006.
Yoshida, et al. “Engineering a Chimeric Pyrroloquinoline Quinone Glucose Dehydrogenase: Improvement of EDTA Tolerance, Thermal Stability and Substrate Specificity,”Protein Engineering, vol. 12, No. 1, p. 63-70, 1999.
Supplementary European Search Report dated Sep. 8, 2008.

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