The enzyme, characterized from cyanobacteria, introduces a cis double bond at carbon 6 of linoleoyl groups (18:2) attached to the sn-1 position of glycerolipids. The enzyme is a front-end desaturase, introducing the new double bond between a pre-existing double bond and the carboxyl-end of the fatty acid. It is nonspecific with respect to the polar head group of the glycerolipid.
Kurdrid, P.; Subudhi, S.; Cheevadhanarak, S.; Tanticharoen, M.; Hongsthong, A.
Effect of two intermediate electron donors, NADPH and FADH(2), on Spirulina DELTA6-desaturase co-expressed with two different immediate electron donors, cytochrome b5 and ferredoxin, in Escherichia coli
Hongsthong, A.; Subudhi, S.; Sirijuntarut, M.; Kurdrid, P.; Cheevadhanarak, S.; Tanticharoen, M.
Revealing the complementation of ferredoxin by cytochrome b5 in the Spirulina-DELTA6-desaturation reaction by N-terminal fusion and co-expression of the fungal-cytochrome b5 domain and Spirulina-DELTA6-acyl-lipid desaturase