Evidence that the multifunctional polypeptides of vertebrate and fungal fatty acid synthases have arisen by independent gene fusion events.
The enoyl reductase (NADPH binding site) of rabbit mammary fatty acid synthase has been radioactively labelled using pyridoxal phosphate and sodium [3H]borohydride. Using this method we have been able to add this site to the four sites whose location has already been mapped within the multifunctional polypeptide chain of the protein. The results show that the enoyl reductase lies between the 3-oxoacylsynthase and the acyl carrier. This confirms that the active sites occur in a different order on the single multifunctional polypeptide of vertebrate fatty acid synthase and the two multifunctional polypeptides of fungal fatty acid synthase, and suggests that these two systems have arisen by independent gene fusion events.
D000818:Animals; D001665:Binding Sites; D005075:Biological Evolution; D002874:Chromosome Mapping; D050753:Enoyl-(Acyl-Carrier-Protein) Reductase (NADH); D064429:Fatty Acid Synthases / Q000235:genetics*; D005815:Genetic Code; D008321:Mammary Glands, Animal / Q000201:enzymology*; D010088:Oxidoreductases / Q000235:genetics; D010455:Peptides / Q000302:isolation & purification / Q000502:physiology*; D011732:Pyridoxal Phosphate / Q000494:pharmacology; D011817:Rabbits; D012441:Saccharomyces cerevisiae / Q000201:enzymology*; D013045:Species Specificity
D010455:Peptides; D011732:Pyridoxal Phosphate; D010088:Oxidoreductases; D050753:Enoyl-(Acyl-Carrier-Protein) Reductase (NADH); D064429:Fatty Acid Synthases