Dec 1, 1978

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

Canadian Journal of Biochemistry
A C Wilson, R W Miller

Abstract

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

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Mentioned in this Paper

Desaturase
Acyl CoA Desaturases
Fusarium oxysporum vasinfectum extract
Sulfides
Fusarium oxysporum
Coenzyme A
Microsomes
Electron Transport
Sulfur
NADH

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