Feb 1, 1981

Isolation of a stearoyl CoA Desaturase form Tetrahymena thermophila

The Journal of protozoology
J Bertram, J ERWIN

Abstract

Cell free preparations of Tetrahymena thermophila contain an enzyme that catalyzes the direct desaturation of stearoyl CoA to octadecenoic acid. The enzyme is associated with the microsomal fraction of the ciliate. Substrate of the enzyme consists of either free stearic acid or stearoyl CoA. Both ATP and CoA are required when free stearate is the substrate and are also highly stimulatory when stearoyl CoA is the substrate. With stearoyl CoA as the substrate, either NADH or NADPH are required for desaturase activity. In presence of ATP and CoA, either NAD or NADP can replace NADH and NADPH. Desaturase activity is optimal when the enzyme is incubated at pH of 7.2 and a temperature of 30-35 degrees C. Highest levels of the stearoyl CoA desaturase are found in stationary phase ciliates grown at 35 degrees C.

  • References11
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Citations

Mentioned in this Paper

Stearic Acids
Desaturase
Solocyte
Acyl CoA Desaturases
Microsomes
Tetrahymena thermophila
Peptide Hydrolases
NADH
Stearic acid
Tetrahymena

About this Paper

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