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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}
}

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Works referenced in this record:

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


Alkane hydroxylases involved in microbial alkane degradation
journal, January 2007


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


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


Engineering cytochrome P450cam into an alkane hydroxylase
journal, January 2003