Substrate Specificity of Acyl-Lipid Δ9-Desaturase from Cyanobacterium sp. IPPAS B-1200, a Cyanobacterium with Unique Fatty Acid Composition

Alexander Starikov, Aizhan A. Usserbayeva, Kirill S. Mironov, Roman A. Sidorov, Bolatkhan K. Zayadan, Vladimir S. Bedbenov, Maria A. Sinetova, Dmitry A. Los

2018

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DOI 10.1134/s102144371804009x

Data confidence 70 medium

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Abstract

Cyanobacterium sp. IPPAS B-1200 is characterized by a high content of rare fatty acids (FAs), both myristic (14:0–30%) and myristoleic (14:1Δ9–10%) in the membrane lipids. Thus, short-chain FAs reach 40% of the sum of all FAs in cells, which is unusual for Cyanobacteria. Monounsaturated palmitoleic acids (16:1Δ9) also reach 40% of the sum of the FAs. We determined the complete nucleotide sequence of the genome of this cyanobacterium and found the only gene for the acyl-lipid Δ9-desaturase, desC1 . We cloned this gene and characterized its specificity to the length of the substrate using heterologous expression in Escheriсhia coli . The results show that DesC1 nonspecifically generates olefin bond in FAs with a length of 14, 16, and 18 carbon atoms. This finding confirms that all monoesterifed FAs in Cyanobacterium sp. IPPAS B-1200 are generated by one acyl-lipid Δ9-desaturase.