Chemistry: molecular biology and microbiology – Enzyme – proenzyme; compositions thereof; process for... – Oxidoreductase
Reexamination Certificate
2006-08-01
2006-08-01
Achutamurthy, P. (Department: 1652)
Chemistry: molecular biology and microbiology
Enzyme , proenzyme; compositions thereof; process for...
Oxidoreductase
C435S252300, C435S320100, C435S069100, C435S071100, C435S004000, C435S006120, C435S325000, C435S440000, C536S023200, C536S023700
Reexamination Certificate
active
07083960
ABSTRACT:
The present invention provides soluble cytochrome p450 reductase (CPR) proteins fromCandidasp. having an altered N-terminal region which results in reduced hydrophobicity of the N-terminal region. Also provided are host cells comprising the subject soluble CPR proteins. In addition, the present invention provides nucleotide and corresponding amino acid sequences for soluble CPR proteins and vectors comprising the nucleotide sequences. Methods for producing a soluble CPR, for increasing production of a dicarboxylic acid, and for detecting a cytochrome P450 are also provided.
REFERENCES:
patent: 6331420 (2001-12-01), Wilson et al.
patent: WO 00/20566 (2000-04-01), None
Sutter et al. Isolation and characterization of the alkane-inducible NADPH-cytochrome P-450 oxidoreductase gene fromCandida tropicalis. Identification of invariant residues within similar amino acid sequences of divergent flavoporteins.
Sutter et al. NCBI Accession No. P37201-1994.
Shi et al. Effects of sequential deletions of residues from the N- or C-terminus on the functions of epsilon subunit of the chloroplast ATP synthase. Biochemistry. Sep. 11, 2001;40(36):10825-31.
Muller et al. A 36-residue peptide contains all of the information required for 7B2-mediated activation of prohormone convertas 2. J Biol Chem. Jul. 23, 1999;274(30):21471-7.
Ron et al. Expression of biologically active recombinant keratinocyte growth factor. Structure/function analysis of amino-termin truncation mutants. J Biol Chem. Feb. 5, 1993;268(4):2984-8.
Trevino et al. Truncations at the NH2 terminus of rhodanese destabilize the enzyme and decrease its heterologous expression J Biol Chem. Oct. 23, 1998;273(43):27841-7.
Smith et al. Dissection of NADPH-cytochrome P450 oxidoreductase into distinct functional domains. Proc Natl Acad Sci U S A Aug. 30, 1994;91(18):8710-4.
Sequence Alignment—SEQ ID No.:83 of Wilson et al. and SEQ ID No.:2 of instant invention.
Lamb et al. (1999) “Generation of a Complete, Soluble, and Catalytically Active Sterol 14α-Demethylase-Reductase Complex”Biochemistry, 38(27): 8733-8738.
Lamb et al. (2001) “Activities and Kinetic Mechanisms of Native and Soluble NADPH-Cytochrome P450 Reductase”Biochemical and Biophysical Research Communications, 286:48-54.
Venkateswarlu et al. (1998) “The N-Terminal Membrane Domain of Yeast NADPH-Cytochrome P450 (CYP) Oxidoreductase Is Not Required for Catalytic Activity in Sterol Biosynthesis or in Reconstitution of CYP Activity”The Journal of Biological Chemistry, 273(8):4492-4496.
Yabusaki et al. (1988) “Genetically Engineered Modification of P450 Monooxygenases: Functional Analysis of the Amino-Terminal Hydrophobic Region and Hinge Region of the P450/Reductase Fused Enzyme”,DNA, 7(10):701-711.
Achutamurthy P.
Cognis Corporation
Daniels John F.
Pak Yong D.
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