Title:
炭化水素系基質の水酸化のための材料及びその利用
Document Type and Number:
Japanese Patent JP6679084
Kind Code:
B2
Abstract:
This disclosure provides: a first site that is a terminal structure capable of binding a decoy molecule, for hydroxylating a hydrocarbon-based substrate by a cytochrome P450 monooxygenase, to a substrate-binding site of the cytochrome P450 monooxygenase; a second site that is a non-fluorinated alkyl chain; and a linker that includes a peptide bond and that links the terminal structure and the alkyl chain.
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Inventors:
Shoji Chozo
Yoshito Watanabe
Yoshito Watanabe
Application Number:
JP2015201431A
Publication Date:
April 15, 2020
Filing Date:
October 09, 2015
Export Citation:
Assignee:
Nagoya University
International Classes:
C07C233/47; C12P7/02; C12P7/06; C12P7/22; C12Q1/26
Domestic Patent References:
| JP2012024009A |
Other References:
Donovan C. Haines et al.,A single active-site mutation of P450BM-3 dramatically enhances substrate binding and rate of produc,Biochemistry,2011年,Vol.50,p.8333-8341
Donovan C. Haines et al.,Crystal structure of inhibitor-bound P450BM-3 reveals open conformation of substrate access channel.,Biochemistry,2008年,Vol.47,p.3662-3670
Amita Hedge et al.,Interactions of substrates at the surface of P450s can greatly enhance substrate potency.,Biochemistry,2007年,Vol.46,p.14010-14017
Zhiqi Cong et al.,Activation of wild-type cytochlome P450BM3 by the next generation of decoy molecules: enhanced hydro,ACS Catalysis,2014年11月,Vol.5,p.150-156
Donovan C. Haines et al.,Crystal structure of inhibitor-bound P450BM-3 reveals open conformation of substrate access channel.,Biochemistry,2008年,Vol.47,p.3662-3670
Amita Hedge et al.,Interactions of substrates at the surface of P450s can greatly enhance substrate potency.,Biochemistry,2007年,Vol.46,p.14010-14017
Zhiqi Cong et al.,Activation of wild-type cytochlome P450BM3 by the next generation of decoy molecules: enhanced hydro,ACS Catalysis,2014年11月,Vol.5,p.150-156
Attorney, Agent or Firm:
Kaiyu International Patent Office