Functions of the <it>Clostridium acetobutylicium </it>FabF and FabZ proteins in unsaturated fatty acid biosynthesis

<p>Abstract</p> <p>Background</p> <p>The original anaerobic unsaturated fatty acid biosynthesis pathway proposed by Goldfine and Bloch was based on in <it>vivo </it>labeling studies in <it>Clostridium butyricum </it>ATCC 6015 (now <it>C. be...

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Main Authors: Zhu Lei, Cheng Juanli, Luo Biao, Feng Saixiang, Lin Jinshui, Wang Shengbin, Cronan John E, Wang Haihong
Format: Article
Language:English
Published: BMC 2009-06-01
Series:BMC Microbiology
Online Access:http://www.biomedcentral.com/1471-2180/9/119
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spelling doaj-6794151e88994b859929a41e7e3f7dfb2020-11-25T01:03:36ZengBMCBMC Microbiology1471-21802009-06-019111910.1186/1471-2180-9-119Functions of the <it>Clostridium acetobutylicium </it>FabF and FabZ proteins in unsaturated fatty acid biosynthesisZhu LeiCheng JuanliLuo BiaoFeng SaixiangLin JinshuiWang ShengbinCronan John EWang Haihong<p>Abstract</p> <p>Background</p> <p>The original anaerobic unsaturated fatty acid biosynthesis pathway proposed by Goldfine and Bloch was based on in <it>vivo </it>labeling studies in <it>Clostridium butyricum </it>ATCC 6015 (now <it>C. beijerinckii</it>) but to date no dedicated unsaturated fatty acid biosynthetic enzyme has been identified in Clostridia. <it>C. acetobutylicium </it>synthesizes the same species of unsaturated fatty acids as <it>E. coli</it>, but lacks all of the known unsaturated fatty acid synthetic genes identified in <it>E. coli </it>and other bacteria. A possible explanation was that two enzymes of saturated fatty acid synthesis of <it>C. acetobutylicium</it>, FabZ and FabF might also function in the unsaturated arm of the pathway (a FabZ homologue is known to be an unsaturated fatty acid synthetic enzyme in enterococci).</p> <p>Results</p> <p>We report that the FabF homologue located within the fatty acid biosynthetic gene cluster of <it>C. acetobutylicium </it>functions in synthesis of both unsaturated fatty acids and saturated fatty acids. Expression of this protein in <it>E. coli </it>functionally replaced both the FabB and FabF proteins of the host in <it>vivo </it>and replaced <it>E. coli </it>FabB in a defined in <it>vitro </it>fatty acid synthesis system. In contrast the single <it>C. acetobutylicium </it>FabZ homologue, although able to functionally replace <it>E. coli </it>FabZ in <it>vivo </it>and in <it>vitro</it>, was unable to replace FabA, the key dehydratase-isomerase of <it>E. coli </it>unsaturated fatty acid biosynthesis in <it>vivo </it>and lacked isomerase activity in <it>vitro</it>.</p> <p>Conclusion</p> <p>Thus, <it>C. acetobutylicium </it>introduces the double of unsaturated fatty acids by use of a novel and unknown enzyme.</p> http://www.biomedcentral.com/1471-2180/9/119
collection DOAJ
language English
format Article
sources DOAJ
author Zhu Lei
Cheng Juanli
Luo Biao
Feng Saixiang
Lin Jinshui
Wang Shengbin
Cronan John E
Wang Haihong
spellingShingle Zhu Lei
Cheng Juanli
Luo Biao
Feng Saixiang
Lin Jinshui
Wang Shengbin
Cronan John E
Wang Haihong
Functions of the <it>Clostridium acetobutylicium </it>FabF and FabZ proteins in unsaturated fatty acid biosynthesis
BMC Microbiology
author_facet Zhu Lei
Cheng Juanli
Luo Biao
Feng Saixiang
Lin Jinshui
Wang Shengbin
Cronan John E
Wang Haihong
author_sort Zhu Lei
title Functions of the <it>Clostridium acetobutylicium </it>FabF and FabZ proteins in unsaturated fatty acid biosynthesis
title_short Functions of the <it>Clostridium acetobutylicium </it>FabF and FabZ proteins in unsaturated fatty acid biosynthesis
title_full Functions of the <it>Clostridium acetobutylicium </it>FabF and FabZ proteins in unsaturated fatty acid biosynthesis
title_fullStr Functions of the <it>Clostridium acetobutylicium </it>FabF and FabZ proteins in unsaturated fatty acid biosynthesis
title_full_unstemmed Functions of the <it>Clostridium acetobutylicium </it>FabF and FabZ proteins in unsaturated fatty acid biosynthesis
title_sort functions of the <it>clostridium acetobutylicium </it>fabf and fabz proteins in unsaturated fatty acid biosynthesis
publisher BMC
series BMC Microbiology
issn 1471-2180
publishDate 2009-06-01
description <p>Abstract</p> <p>Background</p> <p>The original anaerobic unsaturated fatty acid biosynthesis pathway proposed by Goldfine and Bloch was based on in <it>vivo </it>labeling studies in <it>Clostridium butyricum </it>ATCC 6015 (now <it>C. beijerinckii</it>) but to date no dedicated unsaturated fatty acid biosynthetic enzyme has been identified in Clostridia. <it>C. acetobutylicium </it>synthesizes the same species of unsaturated fatty acids as <it>E. coli</it>, but lacks all of the known unsaturated fatty acid synthetic genes identified in <it>E. coli </it>and other bacteria. A possible explanation was that two enzymes of saturated fatty acid synthesis of <it>C. acetobutylicium</it>, FabZ and FabF might also function in the unsaturated arm of the pathway (a FabZ homologue is known to be an unsaturated fatty acid synthetic enzyme in enterococci).</p> <p>Results</p> <p>We report that the FabF homologue located within the fatty acid biosynthetic gene cluster of <it>C. acetobutylicium </it>functions in synthesis of both unsaturated fatty acids and saturated fatty acids. Expression of this protein in <it>E. coli </it>functionally replaced both the FabB and FabF proteins of the host in <it>vivo </it>and replaced <it>E. coli </it>FabB in a defined in <it>vitro </it>fatty acid synthesis system. In contrast the single <it>C. acetobutylicium </it>FabZ homologue, although able to functionally replace <it>E. coli </it>FabZ in <it>vivo </it>and in <it>vitro</it>, was unable to replace FabA, the key dehydratase-isomerase of <it>E. coli </it>unsaturated fatty acid biosynthesis in <it>vivo </it>and lacked isomerase activity in <it>vitro</it>.</p> <p>Conclusion</p> <p>Thus, <it>C. acetobutylicium </it>introduces the double of unsaturated fatty acids by use of a novel and unknown enzyme.</p>
url http://www.biomedcentral.com/1471-2180/9/119
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