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):
- 8,361,769
- Application Number:
- 12/619,033
- Assignee:
- U.S. Department of Energy (Washington, DC)
- 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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