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Hydrogen peroxide-independent production of α-alkenes by OleT(JE) P450 fatty acid decarboxylase

BACKGROUND: Cytochrome P450 OleT(JE) from Jeotgalicoccus sp. ATCC 8456, a new member of the CYP152 peroxygenase family, was recently found to catalyze the unusual decarboxylation of long-chain fatty acids to form α-alkenes using H(2)O(2) as the sole electron and oxygen donor. Because aliphatic α-alk...

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Autores principales: Liu, Yi, Wang, Cong, Yan, Jinyong, Zhang, Wei, Guan, Wenna, Lu, Xuefeng, Li, Shengying
Formato: Online Artículo Texto
Lenguaje:English
Publicado: BioMed Central 2014
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3937522/
https://www.ncbi.nlm.nih.gov/pubmed/24565055
http://dx.doi.org/10.1186/1754-6834-7-28
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author Liu, Yi
Wang, Cong
Yan, Jinyong
Zhang, Wei
Guan, Wenna
Lu, Xuefeng
Li, Shengying
author_facet Liu, Yi
Wang, Cong
Yan, Jinyong
Zhang, Wei
Guan, Wenna
Lu, Xuefeng
Li, Shengying
author_sort Liu, Yi
collection PubMed
description BACKGROUND: Cytochrome P450 OleT(JE) from Jeotgalicoccus sp. ATCC 8456, a new member of the CYP152 peroxygenase family, was recently found to catalyze the unusual decarboxylation of long-chain fatty acids to form α-alkenes using H(2)O(2) as the sole electron and oxygen donor. Because aliphatic α-alkenes are important chemicals that can be used as biofuels to replace fossil fuels, or for making lubricants, polymers and detergents, studies on OleT(JE) fatty acid decarboxylase are significant and may lead to commercial production of biogenic α-alkenes in the future, which are renewable and more environmentally friendly than petroleum-derived equivalents. RESULTS: We report the H(2)O(2)-independent activity of OleT(JE) for the first time. In the presence of NADPH and O(2), this P450 enzyme efficiently decarboxylates long-chain fatty acids (C(12) to C(20)) in vitro when partnering with either the fused P450 reductase domain RhFRED from Rhodococcus sp. or the separate flavodoxin/flavodoxin reductase from Escherichia coli. In vivo, expression of OleT(JE) or OleT(JE)-RhFRED in different E. coli strains overproducing free fatty acids resulted in production of variant levels of multiple α-alkenes, with a highest total hydrocarbon titer of 97.6 mg·l(-1). CONCLUSIONS: The discovery of the H(2)O(2)-independent activity of OleT(JE) not only raises a number of fundamental questions on the monooxygenase-like mechanism of this peroxygenase, but also will direct the future metabolic engineering work toward improvement of O(2)/redox partner(s)/NADPH for overproduction of α-alkenes by OleT(JE).
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spelling pubmed-39375222014-03-01 Hydrogen peroxide-independent production of α-alkenes by OleT(JE) P450 fatty acid decarboxylase Liu, Yi Wang, Cong Yan, Jinyong Zhang, Wei Guan, Wenna Lu, Xuefeng Li, Shengying Biotechnol Biofuels Research BACKGROUND: Cytochrome P450 OleT(JE) from Jeotgalicoccus sp. ATCC 8456, a new member of the CYP152 peroxygenase family, was recently found to catalyze the unusual decarboxylation of long-chain fatty acids to form α-alkenes using H(2)O(2) as the sole electron and oxygen donor. Because aliphatic α-alkenes are important chemicals that can be used as biofuels to replace fossil fuels, or for making lubricants, polymers and detergents, studies on OleT(JE) fatty acid decarboxylase are significant and may lead to commercial production of biogenic α-alkenes in the future, which are renewable and more environmentally friendly than petroleum-derived equivalents. RESULTS: We report the H(2)O(2)-independent activity of OleT(JE) for the first time. In the presence of NADPH and O(2), this P450 enzyme efficiently decarboxylates long-chain fatty acids (C(12) to C(20)) in vitro when partnering with either the fused P450 reductase domain RhFRED from Rhodococcus sp. or the separate flavodoxin/flavodoxin reductase from Escherichia coli. In vivo, expression of OleT(JE) or OleT(JE)-RhFRED in different E. coli strains overproducing free fatty acids resulted in production of variant levels of multiple α-alkenes, with a highest total hydrocarbon titer of 97.6 mg·l(-1). CONCLUSIONS: The discovery of the H(2)O(2)-independent activity of OleT(JE) not only raises a number of fundamental questions on the monooxygenase-like mechanism of this peroxygenase, but also will direct the future metabolic engineering work toward improvement of O(2)/redox partner(s)/NADPH for overproduction of α-alkenes by OleT(JE). BioMed Central 2014-02-24 /pmc/articles/PMC3937522/ /pubmed/24565055 http://dx.doi.org/10.1186/1754-6834-7-28 Text en Copyright © 2014 Liu et al.; licensee BioMed Central Ltd. http://creativecommons.org/licenses/by/2.0 This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly credited. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated.
spellingShingle Research
Liu, Yi
Wang, Cong
Yan, Jinyong
Zhang, Wei
Guan, Wenna
Lu, Xuefeng
Li, Shengying
Hydrogen peroxide-independent production of α-alkenes by OleT(JE) P450 fatty acid decarboxylase
title Hydrogen peroxide-independent production of α-alkenes by OleT(JE) P450 fatty acid decarboxylase
title_full Hydrogen peroxide-independent production of α-alkenes by OleT(JE) P450 fatty acid decarboxylase
title_fullStr Hydrogen peroxide-independent production of α-alkenes by OleT(JE) P450 fatty acid decarboxylase
title_full_unstemmed Hydrogen peroxide-independent production of α-alkenes by OleT(JE) P450 fatty acid decarboxylase
title_short Hydrogen peroxide-independent production of α-alkenes by OleT(JE) P450 fatty acid decarboxylase
title_sort hydrogen peroxide-independent production of α-alkenes by olet(je) p450 fatty acid decarboxylase
topic Research
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3937522/
https://www.ncbi.nlm.nih.gov/pubmed/24565055
http://dx.doi.org/10.1186/1754-6834-7-28
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