Abstract
The time course of hydrogenation of linoleic acid to trans-11-octadecenoic acid was observed in a growing culture of Treponema (Borrelia) strain B25. A conjugated fatty acid, cis-9, trans-11-octadecadienoic acid, was identified as an intermediate in the process. The isomerase responsible for the conversion of linoleic acid to the conjugated fatty acid was found to be associated with a particulate fraction characterized by a high protein and lipid content in a 2:1 ratio. Optimum pH for isomerase activity was found to be 7.0 in 0.05 m potassium phosphate buffer. No cofactor requirements could be demonstrated for the isomerase. The sulfhydryl inhibiting agents, iodoacetamide, N-ethylmaleimide, and p-chloromercuribenzoate, inhibited isomerase activity. Isomerase activity was also inhibited by the metal chelators, o-phenanthroline, α, α′-bipyridyl, ethylenediaminetetraacetic acid, and 8-hydroxyquinoline. Linoleic (Δ9, 12), linolenic (Δ9, 12, 15), and gamma-linolenic (Δ6, 9, 12) acids served as effective substrates for the isomerase; however, the derivatives of linoleic and linolenic acid did not.
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Selected References
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