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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.

Functions of the Clostridium acetobutylicium FabF and FabZ proteins in unsaturated fatty acid biosynthesis