Wanders B J, Denis S W, Dacremont G
Department of Clinical Biochemistry, University Hospital Amsterdam, The Netherlands.
J Biochem. 1993 May;113(5):577-82. doi: 10.1093/oxfordjournals.jbchem.a124086.
We have studied the substrate specificity of the inducible (acyl-CoA oxidase I) and non-inducible (acyl-CoA oxidase II) oxidases in peroxisome-enriched fractions from rat kidney. The two oxidases were separated by means of ion-exchange chromatography and shown to accept a variety of acyl-CoA esters as substrates, including lignoceroyl-CoA, palmitoyl-CoA, lauroyl-CoA, caproyl-CoA, and trimethyltridecanoyl-CoA. Glutaryl-CoA was found to react exclusively with the inducible enzyme, and pristanoyl-CoA exclusively with the non-inducible enzyme. We conclude that under normal non-induced conditions both acyl-CoA oxidase I and II contribute to the oxidation of the various acyl-CoA esters with the exception of pristanoyl-CoA and glutaryl-CoA, although the extent to which each enzyme contributes to the oxidation was found to differ between the various acyl-CoA esters.
我们研究了大鼠肾脏富含过氧化物酶体的组分中诱导型（酰基辅酶A氧化酶I）和非诱导型（酰基辅酶A氧化酶II）氧化酶的底物特异性。通过离子交换色谱法分离出这两种氧化酶，结果表明它们能接受多种酰基辅酶A酯作为底物，包括木蜡酰辅酶A、棕榈酰辅酶A、月桂酰辅酶A、己酰辅酶A和三甲基十三烷酰辅酶A。发现戊二酰辅酶A仅与诱导型酶反应，而降植烷酰辅酶A仅与非诱导型酶反应。我们得出结论，在正常未诱导的条件下，酰基辅酶A氧化酶I和II都参与了除降植烷酰辅酶A和戊二酰辅酶A之外的各种酰基辅酶A酯的氧化，尽管发现每种酶对氧化的贡献程度在不同的酰基辅酶A酯之间有所不同。
