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首页> 外文期刊>BMC Microbiology >Functions of the Clostridium acetobutylicium FabF and FabZ proteins in unsaturated fatty acid biosynthesis
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Functions of the Clostridium acetobutylicium FabF and FabZ proteins in unsaturated fatty acid biosynthesis

机译：丙酮丁醇梭菌FabF和FabZ蛋白在不饱和脂肪酸生物合成中的功能

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Background The original anaerobic unsaturated fatty acid biosynthesis pathway proposed by Goldfine and Bloch was based on in vivo labeling studies in Clostridium butyricum ATCC 6015 (now C. beijerinckii) but to date no dedicated unsaturated fatty acid biosynthetic enzyme has been identified in Clostridia. C. acetobutylicium synthesizes the same species of unsaturated fatty acids as E. coli, but lacks all of the known unsaturated fatty acid synthetic genes identified in E. coli and other bacteria. A possible explanation was that two enzymes of saturated fatty acid synthesis of C. acetobutylicium, 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). Results We report that the FabF homologue located within the fatty acid biosynthetic gene cluster of C. acetobutylicium functions in synthesis of both unsaturated fatty acids and saturated fatty acids. Expression of this protein in E. coli functionally replaced both the FabB and FabF proteins of the host in vivo and replaced E. coli FabB in a defined in vitro fatty acid synthesis system. In contrast the single C. acetobutylicium FabZ homologue, although able to functionally replace E. coli FabZ in vivo and in vitro, was unable to replace FabA, the key dehydratase-isomerase of E. coli unsaturated fatty acid biosynthesis in vivo and lacked isomerase activity in vitro. Conclusion Thus, C. acetobutylicium introduces the double of unsaturated fatty acids by use of a novel and unknown enzyme.
机译：背景技术由Goldfine和Bloch提出的最初的厌氧不饱和脂肪酸生物合成途径是基于在丁酸梭菌ATCC 6015（现为C.beijerinckii）中的体内标记研究，但是迄今为止，在梭菌中尚未鉴定出专用的不饱和脂肪酸生物合成酶。乙丁酸梭菌可合成与大肠杆菌相同种类的不饱和脂肪酸，但缺乏在大肠杆菌和其他细菌中鉴定出的所有已知不饱和脂肪酸合成基因。可能的解释是，乙酰丁酸梭菌，FabZ和FabF的两种饱和脂肪酸合成酶也可能在该途径的不饱和臂中起作用（已知FabZ同源物是肠球菌中的不饱和脂肪酸合成酶）。结果我们报告说，位于丙酮丁醇梭菌脂肪酸生物合成基因簇内的FabF同源物在不饱和脂肪酸和饱和脂肪酸的合成中起作用。该蛋白在大肠杆菌中的表达在体内功能上替代了宿主的FabB和FabF蛋白，并在确定的体外脂肪酸合成系统中替代了大肠杆菌FabB。相反，单个丙酮丁醇梭菌FabZ同源物，尽管能够在体内和体外功能上替代大肠杆菌FabZ，但无法替代FabA，FabA是体内大肠杆菌不饱和脂肪酸生物合成的关键脱水酶-异构酶，并且缺乏异构酶活性体外。结论因此，丙酮丁醇梭菌通过使用一种新颖的未知酶引入了两个不饱和脂肪酸。

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