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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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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