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Cited non-patent literature indicated by the applicant |
CTNP |
Capdevila et al., "The Highly Stereoselective Oxidation of Polyunsaturated Fatty Acids by Cytochrome P450BM-3" J. of Biological Chemistry 271(37), 22663-22671 (1996). 1;
Cherry et al., "Directed Evolution of a Fungal Peroxidase" Nature Biotechnology 17, 379-384 (1999). 1;
Cleland et al., Protein Engineering (1996). 1;
Appel et al., "A P450 BM-3 mutant hydroxylates alkanes, cycloalkynes, arenes and heteroarenes" J. of Biotech. 88, 167-171 (2001). 1;
Bornscheuer, "Gerichtete Evolution von Enzymen" Angew Chem. 110(22), 3285-3288 (1998). 1;
Bernstein et al., "The Protein Data Bank: A Computer-based Archival File for Macromolecular Structures" J. Mol. Biol. 112, 535-542 (1997). 1;
Boddupalli et al., "Fatty Acid Monooxygenation by Cytochrome P-450BM-3" J. of Biological Chemistry 206(8), 4233-4239 (1990). 1;
Govindaraj et al., "Role of linker region connecting the reductase and heme domains in cytochrome P450BM-3" Biochem. 34, 11221-11226 (1995). 1;
Graham-Lorence et al., "An Active Site Substitution, F87V, Converts Cytochrome P450 BM-3 into a Regio- and Stereoselective (14S, 15R)-Arachidonie Acid Epoxygeanse" J. of Biological Chemistry 272(2), 1127-1135 (1997). 1;
Klein et al., "Critical Residues Involved in FMN Binding and Catalytic Activity in Cytochrome P450BM-3" J. of Biological Chemistry 268(10), 7553-7561 (1993). 1;
Kuchner et al., "Directed Evolution of Enzyme Catalysts" Tibtech 15, 523-530 (1997). 1;
Li et al., "The Structure of the Cytochrome p450BM-3 haem domain complexed with fatty acid substrate, palmitoleic acid" Nature Structural Biology 4(2), 140-146 (1997). 1;
Maves et al., "Decreased substrate affinity upon alteration of the substrate of the substrate-docking region in cytochrome P450BM-3" FEBS Letters 414, 213-218 (1997). 1;
Modi et al., "The catalytic mechanism of cytochrome P450 BM3 involves a 6 Å movement of the bound substrate of reduction" Nature Structural Biology 3(5), 414-417 (1996). 1;
Oliver et al., "A Single Mutation in Cytochrome P450 BM3 Changes Substrate Orientation in a Catalytic Intermediate and the Regiospecificity of Hyroxylation" Biochemistry 36, 1567-1572 (1997). 1;
Raner et al., "Stopped-flow spectrometric analysis of intermediates in the peroxo-dependent inactivation of cytochrome P450 by aldehydes" J. Inorg, Biochem. 81, 153-160 (2000). 1;
Ravichandran et al., "Crystal Structure of Hemoprotein Domain of P450BM-3, a Prototype for Microsomal P450's" Science 261, 731-736 (1993). 1;
Schwaneberg et al., "A Continuous Spectrophotomeric Assay for P450 BM-3, a Fatty Acid Hydroxylating Enzyme, and its Mutant F87A1" Analytical Biochemestry 269, 359-366 (1999). 1;
Schwaneberg et al., "P450 monooxyganase in Biotechnology I. Single-step, large scale purification method for cytochrome P450 BM-3 by anion-exchange chromatography" J. of Chromatography 848, 149-159 (1999). 1;
Stemmer, "Rapid evolution of a protein in vitro by DNA shuffling" Nature 370, 389-391 (1994). 1;
Truan et al., "Thr268 in Substrate Binding and Catalysis in P450BM-31" Archives of Biochemistry and Biophysics 349, 53-64 (1998). 1;
Yeom et al., "The Role of Thr268 in Oxygen Activation of Cytochrome P450BM-3" Biochemistry 34, 14733-14740 (1995). 1
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