Draye J P, Van Hoof F, de Hoffmann E, Vamecq J
Laboratoire de Chimie Physiologique, Université de Louvain, Brussels, Belgium.
Eur J Biochem. 1987 Sep 15;167(3):573-8. doi: 10.1111/j.1432-1033.1987.tb13374.x.
A previously unreported metabolite of mammalian phytanic acid catabolism, 2-oxophytanic acid, was identified by gas chromatography/mass spectrometry analysis. The formation of 2-oxophytanic acid was demonstrated to result from the oxidation of L-2-hydroxyphytanic acid, a reaction catalysed by a rat-kidney-cortex H2O2-generating oxidase. The pH optimum for the L-2-hydroxyphytanate oxidase activity was 8.5 and its apparent Km and Vm were about 0.15 mM and 0.35 mumol min-1 (g tissue)-1, respectively. L-2-Hydroxyisocaproate, a substrate of rat kidney L-alpha-hydroxyacid oxidase type B, inhibited the formation of 2-oxophytanate from L-2-hydroxyphytanic acid. Fractionation studies have indicated that 40% of L-2-hydroxyphytanate oxidase was associated with a particulate fraction and that the activity distribution of the oxidase closely paralleled that of catalase, a well known peroxisomal marker enzyme.
通过气相色谱/质谱分析鉴定出一种哺乳动物植烷酸分解代谢中以前未报道的代谢产物——2-氧代植烷酸。已证明2-氧代植烷酸的形成是由L-2-羟基植烷酸氧化产生的，该反应由大鼠肾皮质产生H2O2的氧化酶催化。L-2-羟基植烷酸氧化酶活性的最适pH为8.5，其表观Km和Vm分别约为0.15 mM和0.35 μmol min-1（g组织）-1。大鼠肾B型L-α-羟酸氧化酶的底物L-2-羟基异己酸抑制了L-2-羟基植烷酸生成2-氧代植烷酸。分级分离研究表明，40%的L-2-羟基植烷酸氧化酶与颗粒部分相关，并且该氧化酶的活性分布与过氧化氢酶（一种众所周知的过氧化物酶体标记酶）的活性分布密切平行。
