Growth temperature-dependent stearoyl coenzyme A desaturase activity of Fusarium oxysporum microsomes.

摘要: The characteristics of the microsomal stearoyl CoA desaturase (EC 1.14.99.5) vegetative Fusarium oxysporum cells grown at different temperatures were studied. enzyme had an unusual preference for NADPH (Km = 38 micrometers) over NADH 89 as electron donor, and a relatively high optimum pH 8.3. Enzyme activity was highest in microsomes from 37 degrees C lowest 15 C. This result correlated well with observed changes oleic acid content lipids. Both NADPH-linked reductase activities hemoprotein Spectrophotometric analysis hemoproteins indicated absence cytochrome b5 presence b-type heme pyridine hemochrome alpha band absorption maximum 565 nm. Labile sulfide inhibitor studies thenoyltrifluoroacetone suggested role iron-sulfur protein transfer system associated desaturase.