Substrate specificity of acyl-lipid Δ9-desaturase from Prochlorothrix hollandica cyanobacterium producing myristoleic acid

Substrate specificity of acyl-lipid Δ9-desaturase from Prochlorothrix hollandica cyanobacterium... Chlorophyll b-containing cyanobacterium Prochlorothrix hollandica is characterized by a high content of esterified fatty acids (FA) with 14 and 16 carbon atoms in the membrane lipids. Depending on the conditions of cultivation, the relative amount of myristic (C14:0) and myristoleic (C14:1) acids can reach 35%, and palmitic (С16:0) and palmitoleic (С16:1) acids can reach 60% of the sum of all fatty acids in cells. Monounsaturated FAs are represented by C14:1, and C16:1 with an olefinic bond presumably located in the Δ9 position. We cloned the gene of acyl-lipid Δ9-desaturase, desC1, from Prochlorothrix hollandica and characterized its specificity to the length of the substrate using the heterologous expression in Escherichia coli cells adding C14:0 or stearic (C18:0) acids as exogenous substrates. The results show that DesC1 Δ9 desaturase generates olefinic bonds in the FAs with a length of 14 to 18 carbon atoms with an approximately equal efficiency. This indicates that the length of the FA chain in P. hollandica is determined by the activity of the FA synthase, and the chain is desaturated at the Δ9 position nonspecifically relatively to its length. Russian Journal of Plant Physiology Springer Journals

Substrate specificity of acyl-lipid Δ9-desaturase from Prochlorothrix hollandica cyanobacterium producing myristoleic acid

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Pleiades Publishing
Copyright © 2017 by Pleiades Publishing, Ltd.
Life Sciences; Plant Physiology; Plant Sciences
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