Abstract
Abstract Stearyl acyl carrier protein, chemically prepared from 1-14C stearic acid and Escherichia coli acyl carrier protein, is desaturated to oleic acid by extracts of photoauxotrophic Euglena gracilis and of spinach. The soluble stearyl acyl carrier protein desaturase system from Euglena has been separated into three components, a reduced triphosphopyridine nucleotide oxidase, the desaturase, and a nonheme iron protein (ferredoxin). The enzyme requires reduced triphosphopyridine nucleotide and molecular oxygen. Desaturation is inhibited by KCN but is not affected by carbon monoxide.
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