Blemings K P, Crenshaw T D, Swick R W, Benevenga N J
Department of Meat and Animal Science, University of Wisconsin, Madison 53706.
J Nutr. 1994 Aug;124(8):1215-21. doi: 10.1093/jn/124.8.1215.
In rat liver, comparisons of marker enzyme activities (beta-hexosaminidase, lysosomes; catalase, peroxisomes; cytochrome oxidase, mitochondrial-inner membrane; monoamine oxidase, mitochondrial outer membrane; ornithine aminotransferase, mitochondrial matrix) show that lysine-alpha-ketoglutarate reductase and saccharopine dehydrogenase, the initial enzymes of saccharopine-dependent lysine degradation, are found only in the mitochondrial matrix. These results are consistent with obligatory uptake of lysine into the matrix for lysine catabolism and raise the possibility that lysine transport into the mitochondrion may control lysine degradation.
在大鼠肝脏中，对标记酶活性（β-己糖胺酶，溶酶体；过氧化氢酶，过氧化物酶体；细胞色素氧化酶，线粒体内膜；单胺氧化酶，线粒体外膜；鸟氨酸转氨酶，线粒体基质）进行比较后发现，依赖于酵母氨酸的赖氨酸降解的起始酶，即赖氨酸-α-酮戊二酸还原酶和酵母氨酸脱氢酶，仅存在于线粒体基质中。这些结果与赖氨酸分解代谢时赖氨酸必须进入基质的情况一致，并增加了赖氨酸转运到线粒体中可能控制赖氨酸降解的可能性。
