St Jules R, Kennard J, Setlik W, Holtzman E
Department of Biological Sciences, Columbia University, New York, NY 10027.
Eur J Cell Biol. 1991 Jun;55(1):94-103.
D-amino acid oxidase is a widely distributed peroxisomal enzyme whose principal natural substrates are still unknown. Thiazolidine carboxylates, their derivatives and relatives, and the intermediates in their metabolism are among the more plausible substrate candidates. Using a cytochemical procedure, we have explored the distribution of peroxide-generating enzymatic activity against two thiazolidine carboxylates. We find that these compounds are effective substrates for peroxisomal oxidation in a variety of tissues that contain peroxisomal D-amino acid oxidase. Reaction was seen in the "classical" peroxisomes of rat liver and kidney, the peroxisomes of the fat body of firefly and of Drosophila and the peroxisomes of frog retina. Interestingly, both with the thiazolidine compounds and with more traditional D-amino acid oxidase substrates, the fireflies' photocyte granules, which are peroxisomes, lack activity.
D-氨基酸氧化酶是一种广泛分布的过氧化物酶体酶，其主要天然底物仍然未知。噻唑烷羧酸盐、它们的衍生物及相关物，以及它们代谢过程中的中间体是较为合理的底物候选物。我们运用细胞化学方法，探究了针对两种噻唑烷羧酸盐的产过氧化氢酶活性的分布情况。我们发现，这些化合物在多种含有过氧化物酶体D-氨基酸氧化酶的组织中，是过氧化物酶体氧化的有效底物。在大鼠肝脏和肾脏的“经典”过氧化物酶体、萤火虫和果蝇脂肪体的过氧化物酶体以及青蛙视网膜的过氧化物酶体中均观察到了反应。有趣的是，无论是噻唑烷化合物还是更传统的D-氨基酸氧化酶底物，萤火虫作为过氧化物酶体的发光细胞颗粒均缺乏活性。
