Chain elongation, 20hydroxylation, and decarboxylation of long chain fatty acids by yeast.
نویسنده
چکیده
Chain elongation and 2-hydroxylation pathways, which are specific for very long chain fatty acids ( >C&), have been found in the yeast, Candida utitis. The chain elongation system acts specifically on fatty acids of chain length C2,, to CZ4; there is no detectable elongation of Cl* and only trace . . . actrvrty with C&,. The product of the elongation enzyme or enzymes is C& when Co, C&, or C24 is substrate and is a mixture of C& and Cn when the substrates are CZl and C23. The 2-hydroxylation enzyme converts C26 acid, formed in situ by chain elongation, to 2-hydroxyhexacosanoic acid. The enzyme seems quite specific for the C&, chain length, although there may be some activity for chain lengths C24, c25, and c27. In addition to the chain elongation and 2-hydroxylation systems, a relatively nonspecific system for the oxidative decarboxylation of 2-hydroxy acids has been studied in C. utilis. All 2-hydroxy fatty acids tested (Cl8 through C26 contaming an even number of carbons) were converted, in part, to the unsubstituted acid containing 1 carbon less than the substrate. Decarboxylation was most efficient with Z-OHCl8 and least with 2-OH-C26 acids. Another product arising from the decarboxylation reaction was the aldehyde containing 1 carbon less than the 2-hydroxy acid substrate. The aldehydes were detected in trace amounts with the shorter chain substrates but were major products from the decarboxylation of 2-OH-C24 and Z-OH-C&. Presumably, the aldehyde is an intermediate between the 2-hydroxy acid substrate and the unsubstituted fatty acid which results as the final product in the oxidative decarboxylation process.
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ورودعنوان ژورنال:
- The Journal of biological chemistry
دوره 242 16 شماره
صفحات -
تاریخ انتشار 1967