Bibliografische Daten

Dokument US000007981652B2 (Seiten: 23)

Bibliografische Daten Dokument US000007981652B2 (Seiten: 23)
INID Kriterium Feld Inhalt
54 Titel TI [EN] Modified cytochrome P450 monooxygenases
71/73 Anmelder/Inhaber PA BASF AG, DE
72 Erfinder IN FISCHER MARKUS, DE ; HAUER BERNHARD, DE ; LI QING-SHAN, JP ; PLEISS JUERGEN, DE ; SCHMID ROLF, DE ; SCHMITT JUTTA, DE ; SCHWANEBERG ULRICH, DE
22/96 Anmeldedatum AD 13.04.2009
21 Anmeldenummer AN 42266609
Anmeldeland AC US
Veröffentlichungsdatum PUB 19.07.2011
33
31
32
Priorität PRC
PRN
PRD
DE
10011723
10.03.2000
33
31
32
PRC
PRN
PRD
DE
19935115
27.07.1999
33
31
32
PRC
PRN
PRD
EP
0007252
27.07.2000
33
31
32
PRC
PRN
PRD
US
3169502
23.01.2002
51 IPC-Hauptklasse ICM C12N 9/02 (2006.01)
51 IPC-Nebenklasse ICS C07H 21/04 (2006.01)
C12N 1/20 (2006.01)
C12N 15/00 (2006.01)
C12P 21/04 (2006.01)
C12Q 1/00 (2006.01)
C12Q 1/68 (2006.01)
IPC-Zusatzklasse ICA
IPC-Indexklasse ICI
Gemeinsame Patentklassifikation CPC C12N 9/0071
C12N 9/0077
C12P 17/10
C12P 17/165
C12P 7/02
C12P 7/04
C12P 7/22
C12P 7/42
C12P 7/6409
C12Q 1/26
G01N 2333/90245
MCD-Hauptklasse MCM C12M 1/40 (2006.01)
C12N 9/02 (2006.01)
MCD-Nebenklasse MCS C07H 21/04 (2006.01)
C12N 1/20 (2006.01)
C12N 1/21 (2006.01)
C12N 15/00 (2006.01)
C12N 15/09 (2006.01)
C12P 17/10 (2006.01)
C12P 17/16 (2006.01)
C12P 21/04 (2006.01)
C12P 7/02 (2006.01)
C12P 7/04 (2006.01)
C12P 7/22 (2006.01)
C12P 7/42 (2006.01)
C12P 7/64 (2006.01)
C12Q 1/00 (2006.01)
C12Q 1/26 (2006.01)
C12Q 1/68 (2006.01)
MCD-Zusatzklasse MCA C12R 1/11 (2006.01)
C12R 1/19 (2006.01)
57 Zusammenfassung AB [EN] The present invention relates to modified cytochrome P450 monooxygenases with an altered substrate profile, to nucleic acid sequences coding therefor, to expression constructs and vectors, to recombinant microorganisms which comprise these vectors, and to processes for the microbiological production of terminally or subterminally hydroxylated aliphatic carboxylic acids.
56 Entgegengehaltene Patentdokumente/Zitate,
in Recherche ermittelt
CT
56 Entgegengehaltene Patentdokumente/Zitate,
vom Anmelder genannt
CT GB000002294692A
US000007211420B1
WO002000031273A2
56 Entgegengehaltene Nichtpatentliteratur/Zitate,
in Recherche ermittelt
CTNP Branden et al. Introduction to Protein Structure, Garland Publishing Inc., New York, p. 247, 1991. 0
56 Entgegengehaltene Nichtpatentliteratur/Zitate,
vom Anmelder genannt
CTNP Appel et al., "A P450 BM-3 mutant hydroxylates alkanes, cycloalkynes, arenes and heteroarenes" J. of Biotech. 88, 167-171 (2001). 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;
Bornscheuer, "Gerichtete Evolution von Enzymen" Angew Chem. 110(22), 3285-3288 (1998). 1;
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;
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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Sequenzprotokoll
Prüfstoff-IPC ICP C07H 21/04
C12N 1/20
C12N 15/00
C12N 9/02
C12P 21/04
C12P 7/40
C12Q 1/00