Omega-3 fatty acids are oxygenated at the n-7 carbon by the lipoxygenase domain of a fusion protein in the cyanobacterium Acaryochloris marina.

ABSTRACT: Lipoxygenases (LOX) are found in most organisms that contain polyunsaturated fatty acids, usually existing as individual genes although occasionally encoded as a fusion protein with a catalase-related hemoprotein. Such a fusion protein occurs in the cyanobacterium Acaryochloris marina and herein we report the novel catalytic activity of its LOX domain. The full-length protein and the C-terminal LOX domain were expressed in Escherichia coli, and the catalytic activities characterized by UV, HPLC, GC-MS, and CD. All omega-3 polyunsaturates were oxygenated by the LOX domain at the n-7 position and with R stereospecificity: alpha-linolenic and the most abundant fatty acid in A. marina, stearidonic acid (C18.4omega3), are converted to the corresponding 12R-hydroperoxides, eicosapentaenoic acid

SUBMITTER: Gao B 

PROVIDER: S-EPMC2787963 | biostudies-literature | 2010 Jan

REPOSITORIES: biostudies-literature