Kawaguchi A, Tsubotani S, Seyama Y, Yamakawa T, Osumi T, Hashimoto T, Kikuchi T, Ando M, Okuda S
J Biochem. 1980 Nov;88(5):1481-6. doi: 10.1093/oxfordjournals.jbchem.a133118.
The stereochemical course of dehydrogenation catalyzed by acyl-CoA oxidase was investigated using the enzymes from rat liver peroxisomes and Candida lipolytica. Stearoyl-CoA and nonanoyl-CoA, stereospecifically labeled with deuterium at either C-2 or C-3, were incubated with the enzyme, the products were converted to methyl esters and their deuterium contents were measured by gas chromatography-mass spectrometry. The results suggested that acyl-CoA oxidase-catalyzed dehydrogenation occurred by anti-elimination of the pro 2R and pro-3R hydrogens of acyl-CoA.
利用大鼠肝脏过氧化物酶体和解脂假丝酵母中的酰基辅酶A氧化酶，研究了该酶催化脱氢反应的立体化学过程。将在C-2或C-3位置特异性标记氘的硬脂酰辅酶A和壬酰辅酶A与该酶一起孵育，产物转化为甲酯，并通过气相色谱-质谱法测定其氘含量。结果表明，酰基辅酶A氧化酶催化的脱氢反应是通过反式消除酰基辅酶A的前2R和前3R氢而发生的。
