| 54 |
Title |
TI |
[EN] Modified cytochrome p450 monooxygenases |
| 71/73 |
Applicant/owner |
PA |
BASF AG, DE
|
| 72 |
Inventor |
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 |
Application date |
AD |
Jul 27, 2000 |
| 21 |
Application number |
AN |
3169500 |
|
Country of application |
AC |
US |
|
Publication date |
PUB |
May 12, 2009 |
33
31
32 |
Priority data |
PRC
PRN
PRD |
DE
10011723
Mar 10, 2000
|
33
31
32 |
PRC
PRN
PRD |
DE
19935115
Jul 27, 1999
|
33
31
32 |
PRC
PRN
PRD |
EP
0007252
Jul 27, 2000
|
| 51 |
IPC main class |
ICM |
C12N 9/02
(2006.01)
|
| 51 |
IPC secondary class |
ICS |
C07H 21/04
(2006.01)
C12N 1/20
(2006.01)
C12N 15/00
(2006.01)
C12P 21/04
(2006.01)
C12P 7/00
(2006.01)
C12Q 1/26
(2006.01)
|
|
IPC additional class |
ICA |
C12Q 1/00
(2006.01)
C12Q 1/68
(2006.01)
|
|
IPC index class |
ICI |
|
|
Cooperative patent classification |
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 main class |
MCM |
C12N 9/02
(2006.01)
C12M 1/40
(2006.01)
|
|
MCD secondary class |
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 7/00
(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 1/26
(2006.01)
|
|
MCD additional class |
MCA |
C12Q 1/00
(2006.01)
C12Q 1/68
(2006.01)
C12R 1/11
(2006.01)
C12R 1/19
(2006.01)
|
| 57 |
Abstract |
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 |
Cited documents identified in the search |
CT |
|
| 56 |
Cited documents indicated by the applicant |
CT |
GB000002294692A
WO002000031273A2
|
| 56 |
Cited non-patent literature identified in the search |
CTNP |
|
| 56 |
Cited non-patent literature indicated by the applicant |
CTNP |
Bernstein et al. "The Protein Data Bank: A Computer-based Archival File for Macromolecular Structures" J. Mol. Biol. vol. 112 (1997) pp. 535-542. 1;
Boddupalli et al. "Fatty Acid Monooxygenation by Cytochrome P-450 BM-3*" J. of Biological Chemistry vol. 206 No. 8, (1990) pp. 4233-4239. 1;
Capdevila et al."The Highly Stereoselective Oxidation of Polyunsaturated Fatty Acids by Cytochrome P450BM-3*" J. of Biological Chemistry vol. 271 No. 37 (1996) pp. 22663-22671. 1;
Cherry et al. "Directed Evolution of a Fungal Peroxidase" Nature Biotechnology vol. 17 (1999) pp. 379-384. 1;
Cleland et al. Protein Engineering (1996). 1;
Gerichtete Evolution von Enzymen, Bornscheuer, Angew Chem. 1998, 110, Nr. 22, 3285-3288. 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 vol. 272 No. 2, (1997) pp. 1127-1135. 1;
Klein et al. "Critical Residues Involved in FMN Binding and Catalytic Activity in Cytochrome P450BM-3*" J. of Biological Chemistry vol. 268, No. 10 (1993) pp. 7553-7561. 1;
Kuchner et al. "Directed Evolution of Enzyme Catalysts" Tibtech vol. 15 (1997) pp. 523-530. 1;
Li et al. "The Structure of the Cytochrome p450BM-3 haem domain complexed with fatty acid substrate, palmitoleic acid" Nature Structural Biology vol. 4 No. 2 (1997) pp. 140-146. 1;
Maves et al. "Decreased substrate affinity upon alteration of the substrate of the substrate-docking region in cytochrome P450BM-3" FEBS Letters vol. 414 (1997) pp. 213-218. 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 vol. 3 No. 5 (1996) pp. 414-417. 1;
Oliver et al. "A Single Mutation in Cytochrome P450 BM3 Changes Substrate Orientation in a Catalytic Intermediate and the Regiospecificity of Hyroxylation" Biochemistry vol. 36 (1997) pp. 1567-1572. 1;
Ravichandran et al. "Crystal Structure of Hemoprotein Domain of P450BM-3, a Prototype for Microsomal P450's" Science vol. 261 (1993) pp. 731-736. 1;
Schwaneberg et al. "A Continuous Spectrophotomeric Assay for P450 BM-3, a Fatty Acid Hydroxylating Enzyme, and its Mutant F87A1" Analytical Biochemestry vol. 269 (1999) pp. 359-366. 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 vol. 848 (1999) pp. 149-159. 1;
Stemmer "Rapid evolution of a protein in vitro by DNA shuffling" Nature vol. 370 (1994) pp. 389-391. 1;
Truan et al. "Thr268 in Substrate Binding and Catalysis in P450BM-31'' Archives of Biochemistry and Biophysics" vol. 349, (1998) pp. 53-64. 1;
Yeom et al. "The Role of Thr268 in Oxygen Activation of Cytochrome P450BM-3" Biochemistry vol. 34 (1995) pp. 14733-14740. 1
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Citing documents |
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Determine documents
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Sequence listings |
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Search file IPC |
ICP |
C07H 21/04
C12N 1/20
C12N 15/00
C12N 9/02
C12P 7/00
C12Q 1/00
C12Q 1/26
C12Q 1/68
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