Fatty acyl-coenzyme A elongation in brain of normal and quaking mice.

Microsomal enzyme systems from mouse brain that catalyze, respectively, the elongation of palmitoyl-coenzyme A (palmitoyl-CoA), stearoyl-CoA, or arachidyl-CoA appear and reach maximal activity at different times after birth of the animal. A specific C(20)-CoA elongating system exists in mouse brain in addition to the previously recognized C(16)-CoA and C(l8)-CoA elongating enzymes. The C(20)-CoA elongation system is severely reduced in the mutant quaking mouse.

Origin of hydrogen atoms in the fatty acids synthesized with yeast fatty acid synthetase.

The mechanism of hydrogen incorporation into fatty acids was investigated with an enzyme preparation from baker's yeast. Fatty acids synthesized from malonyl-CoA and acetyl-CoA in the presence of D2O or stereospecifically deuterium-labeled NADPH were isolated and analyzed by mass chromatography to examine the localization of deuterium atoms in the molecule. The following results were obtained: 1. Hydrogen atoms from water were found on the even-numbered methylene carbon atoms (2-hydrogen atoms per carbon atom). The second hydrogen atom was incorporated as the result of hydrogen exchange phenomenon between the methylene group of malonyl CoA and water. 2. HB hydrogen of NADPH was used for beta-ketoacyl reductase. 3. HB hydrogen of NADPH was also used for enoyl reductase. 4. Hydrogen atoms from HB position of NADPH were found on the odd-numbered methylene carbon atoms (2-hydrogen atoms per carbon atom).

Propionyl-Coa induced synthesis of even-chain-length fatty acids by fatty acid synthetase from Brevibacterium ammoniagenes.

The product distribution of Brevibacterium ammoniagenes fatty acid synthetase has been investigated using propionyl-CoA instead of acetyl-CoA as the primer. The synthetase produces not only an odd-numbered fatty acid (heptadecanoic acid) but also even-numbered fatty acids (stearic and oleic acids) in the presence of propionyl-CoA. The amounts of heptadecanoic, stearic and oleic acids increased with increasing concentration of propionyl-CoA. However, the formation of heptadecenoic acid (C17:1) was not observed under any conditions tested. The failure of C17:1 synthesis suggested that the enzyme component catalyzing the beta, gamma-dehydration, which is responsible for the synthesis of unsaturated fatty acids, has a high degree of chain length specificity. Under standard assay conditions, stearic acid predominated and heptadecanoic and oleic acids were found in lesser amounts. Mass spectrometric analyses of fatty acids synthesized either from [2H]propionyl-CoA or in 2H2O revealed that propionyl-CoA is utilized as the priming substrate for the synthesis of heptadecanoic acid and that an acetyl residues, which is formed by the decarboxylation of malonyl-CoA, served as the priming substrate for the syntheses of stearic and oleic acids. No evidence was obtained for the direct decarboxylation of malonyl-CoA to acetyl-CoA in this reaction. It is concluded that the decarboxylation of the malonyl moiety bound to the synthetase occurs efficiently only in the course of fatty acid synthesis. A hypothetical scheme is presented to explain the propionyl-CoA-dependent decarboxylation of the malonyl moiety.

Biosynthesis of the novel fatty acid, 17-methyl-cis-9,10-methyleneoctadecanoic acid, by the parasitic protozoan, Herpetomonas megaseliae.

Herpetomonas megaseliae, a flagellate protozoan parasite of the gut of a dipteran, Megaselia scalaris, is shown by chromatographic, spectrometric and radiotracer methods to synthesize de novo an iso-branched chain cyclopropane fatty acid, 17-methyl-cis-9,10-methyleneoctadecanoic acid.