Strittmatter P, Spatz L, Corcoran D, Rogers M J, Setlow B, Redline R
Proc Natl Acad Sci U S A. 1974 Nov;71(11):4565-9. doi: 10.1073/pnas.71.11.4565.
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.
依赖NADH的硬脂酰辅酶A去饱和酶系统的末端酶已从大鼠肝脏微粒体中分离出来。这种去饱和酶是一种分子量为53,000道尔顿的单一多肽，含有62%的非极性氨基酸残基和一个非血红素铁原子。纯化后的蛋白质形成高分子量聚集体，可通过去污剂处理使其分散。去饱和酶活性需要NADH、硬脂酰辅酶A、氧气、脂质以及三种酶，即细胞色素b(5)还原酶（EC 1.6.2.2）、细胞色素b(5)和去饱和酶。细胞色素b(5)是去饱和酶的直接电子供体，在硬脂酰辅酶A去饱和过程中，去饱和酶似乎在氧化还原序列中利用铁。
