Fatty acid metabolism and its regulation, Volume 7 (New by Shosaku Numa

By Shosaku Numa

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41 for review). The hydrolytic cleavage of the fatty acid chain is carried out by a thioesterase, shown to be an integral part of the multienzyme complex. However, fatty acids with chain lengths of 4-24 carbons are found in vivo 36 in various animal tissues. Several factors have been discovered which are responsible for regulating the chain length of the fatty acids in vivo. Studies involving chain length regulation have been primarily performed with enzymes purified from animal mammary glands or the sebaceous gland of waterfowl.

The acyl group is transferred from ACP to a cysteine SH of P-keto-acyl-ACP synthase (condensing enzyme) liberating free ACP (reaction 3). The liberated SH group of ACP is then available to accept a malonyl group from malonyl-CoA in a reaction catalyzed by malonyl transacylase forming malonyl-ACP (reaction 4). This reaction is analogous to the acyl transacylase reaction. The critical elongation reaction of fatty acid synthesis is catalyzed by the condensing enzyme, P-keto-acyl-ACP synthase. In this reaction the acyl group linked to a cysteine sulfhydryl linkage on the enzyme (reaction 3) is condensed with malonyl-ACP (reaction 5) resulting in the decarboxylation of malonyl-ACP with the formation of a P-keto-acyl-ACP derivative.

63] showed this apparent dependence of ,the FAS activity on addition of CoA was probably due to the need to unload bound acetyl or malonyl groups from common binding sites on the synthetase in order to facilitate the continuation of the reaction. The factors which regulate the length of the acyl chain in Escherichia coli have also been investigated. Greenspan et al. [64] showed that purified P-ketoacyl-ACP synthetase was unable to elongate palmitoyl and cis-vaccenyl acyl carrier proteins although shorter chain lengths could be further elongated.

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