Erythrocyte membrane acyl : CoA synthetase activity

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Abstract
The presence of long-chain acyl : CoA synthetases in mammalian microsomes and mitochondria has been established previously [(1971) Biochim. Biophys. Acta 231, 32-47]. The presence of a plasma membrane-associated enzyme was investigated in human erythrocyte ghost plasma membranes, where an enzyme exhibiting high activity, and with a preferred substrate of 18 carbon chain length, was discovered. The results are consistent with the presence of a single enzyme. The effect of the degree of Unsaturation of the fatty acid substrates was not as pronounced as that arising from the length of the carbon chain. The pattern of substrate preference of the enzyme was ω3 polyenoics > ω6 polyenoics > ω9 monoenoics > saturated fatty acids. This may relate to the similar substrate preference pattern exhibited by the fatty acyl desaturase enzymes. However, the role played by long-chain acyl: CoA synthetase in erythrocyte metabolism is uncertain, but may relate to the transportation of polyenoic fatty acids in the circulation.

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