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. 1974 Nov;71(11):4565-9.
doi: 10.1073/pnas.71.11.4565.

Purification and properties of rat liver microsomal stearyl coenzyme A desaturase

P Strittmatter, L Spatz, D Corcoran, M J Rogers, B Setlow, R Redline

Purification and properties of rat liver microsomal stearyl coenzyme A desaturase

P Strittmatter et al. Proc Natl Acad Sci U S A. 1974 Nov.

Abstract

The terminal enzyme of the NADH-dependent stearyl coenzyme A desaturase system has been isolated from rat liver microsomes. This desaturase is a single polypeptide of 53,000 daltons containing 62% nonpolar amino-acid residues and one atom of non-heme iron. The purified protein forms high molecular weight aggregates that can be dispersed by detergent procedures. Desaturase activity requires NADH, stearyl coenzyme A, oxygen, lipid, and the three enzymes, cytochorme b(5) reductase (EC 1.6.2.2), cytochrome b(5), and desaturase. Cytochrome b(5) is the direct electron donor to the desaturase, which appears to utilize the iron in the oxidation-reduction sequence during desaturation of stearyl coenzyme A.

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