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Title: Regioselective alkane hydroxylation with a mutant CYP153A6 enzyme

Abstract

Cytochrome P450 CYP153A6 from Myobacterium sp. strain HXN1500 was engineered using in-vivo directed evolution to hydroxylate small-chain alkanes regioselectively. Mutant CYP153A6-BMO1 selectively hydroxylates butane and pentane at the terminal carbon to form 1-butanol and 1-pentanol, respectively, at rates greater than wild-type CYP153A6 enzymes. This biocatalyst is highly active for small-chain alkane substrates and the regioselectivity is retained in whole-cell biotransformations.

Inventors:
;
Issue Date:
Research Org.:
California Institute of Technology (CalTech), Pasadena, CA (United States)
Sponsoring Org.:
USDOE
OSTI Identifier:
1082682
Patent Number(s):
8361769
Application Number:
12/619,033
Assignee:
U.S. Department of Energy (Washington, DC)
Patent Classifications (CPCs):
C - CHEMISTRY C12 - BIOCHEMISTRY C12P - FERMENTATION OR ENZYME-USING PROCESSES TO SYNTHESISE A DESIRED CHEMICAL COMPOUND OR COMPOSITION OR TO SEPARATE OPTICAL ISOMERS FROM A RACEMIC MIXTURE {
C - CHEMISTRY C12 - BIOCHEMISTRY C12N - MICROORGANISMS OR ENZYMES
DOE Contract Number:  
FG02-06ER15762
Resource Type:
Patent
Resource Relation:
Patent File Date: 2009 Nov 16
Country of Publication:
United States
Language:
English
Subject:
59 BASIC BIOLOGICAL SCIENCES

Citation Formats

Koch, Daniel J., and Arnold, Frances H. Regioselective alkane hydroxylation with a mutant CYP153A6 enzyme. United States: N. p., 2013. Web.
Koch, Daniel J., & Arnold, Frances H. Regioselective alkane hydroxylation with a mutant CYP153A6 enzyme. United States.
Koch, Daniel J., and Arnold, Frances H. Tue . "Regioselective alkane hydroxylation with a mutant CYP153A6 enzyme". United States. https://www.osti.gov/servlets/purl/1082682.
@article{osti_1082682,
title = {Regioselective alkane hydroxylation with a mutant CYP153A6 enzyme},
author = {Koch, Daniel J. and Arnold, Frances H.},
abstractNote = {Cytochrome P450 CYP153A6 from Myobacterium sp. strain HXN1500 was engineered using in-vivo directed evolution to hydroxylate small-chain alkanes regioselectively. Mutant CYP153A6-BMO1 selectively hydroxylates butane and pentane at the terminal carbon to form 1-butanol and 1-pentanol, respectively, at rates greater than wild-type CYP153A6 enzymes. This biocatalyst is highly active for small-chain alkane substrates and the regioselectivity is retained in whole-cell biotransformations.},
doi = {},
journal = {},
number = ,
volume = ,
place = {United States},
year = {2013},
month = {1}
}

Works referenced in this record:

Engineered Alkane-Hydroxylating Cytochrome P450BM3 Exhibiting Nativelike Catalytic Properties
journal, November 2007


Engineering cytochrome P450cam into an alkane hydroxylase
journal, January 2003


Alkane hydroxylases involved in microbial alkane degradation
journal, January 2007


Regio- and Enantioselective Alkane Hydroxylation with Engineered Cytochromes P450 BM-3
journal, November 2003


In Vivo Evolution of Butane Oxidation by Terminal Alkane Hydroxylases AlkB and CYP153A6
journal, November 2008