Open AccessPurification and Properties of Rat Liver Microsomal Stearyl Coenzyme A Desaturase
Author(s) -
Philipp Strittmatter,
Lawrence Spatz,
Doris Corcoran,
Michael J. Rogers,
Barbara Setlow,
R. Redline
Publication year - 1974
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.71.11.4565
Subject(s) - coenzyme a , biochemistry , cofactor , reductase , cytochrome b5 , microsome , enzyme , stearoyl coa desaturase , chemistry , cytochrome , heme , gene , gene expression
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, cytochormeb 5 reductase (EC 1.6.2.2), cytochromeb 5 , and desaturase. Cytochromeb 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.