He X Y, Shoukry K, Chu C, Yang J, Sprecher H, Schulz H
Department of Chemistry, City College City University of New York, New York 10031, USA.
Biochem Biophys Res Commun. 1995 Oct 4;215(1):15-22. doi: 10.1006/bbrc.1995.2428.
The presence of delta 3,5,delta 2,4-dienoyl-CoA isomerase in peroxisomes was demonstrated by determining the subcellular distribution of this enzyme in rat liver. The peroxisomal and mitochondrial forms of the isomerase exhibit similar chain length specificities and they are homologous as indicated by the recognition of the peroxisomal 66-kDa enzyme by an antiserum raised against the mitochondrial 32-kDa isomerase. This report demonstrates that peroxisomes contain all enzymes required for the beta oxidation of unsaturated fatty acids with odd-numbered double bonds by a novel pathway in which double bonds are reductively removed by the NADPH-dependent 2,4-dienoyl-CoA reductase.
通过测定大鼠肝脏中该酶的亚细胞分布,证实了δ3,5、δ2,4-二烯酰辅酶A异构酶存在于过氧化物酶体中。该异构酶的过氧化物酶体形式和线粒体形式表现出相似的链长特异性,并且如针对线粒体32 kDa异构酶产生的抗血清对过氧化物酶体66 kDa酶的识别所示,它们是同源的。本报告表明,过氧化物酶体含有通过一种新途径进行奇数双键不饱和脂肪酸β氧化所需的所有酶,在该途径中,双键由依赖NADPH的2,4-二烯酰辅酶A还原酶进行还原性去除。