Hovik R, Osmundsen H
Department of Physiology and Biochemistry, Dental School, University of Oslo, Norway.
Biochem J. 1993 Feb 15;290 ( Pt 1)(Pt 1):97-102. doi: 10.1042/bj2900097.
The activity of the enzyme acyl-CoA oxidase (EC 1.3.99.3) is influenced by detergents. At concentrations above the critical micellar concentration, Triton X-100, Triton X-114 and Thesit stimulate oxidase activity. Lower concentrations of Triton X-100 and Triton X-114 render the acyl-CoA oxidase less sensitive towards substrate inhibition by palmitoyl-CoA or dec-4-cis-enoyl-CoA. Other detergents inhibited the enzyme activity. CoA was found to be a relatively powerful competitive inhibitor of the enzyme, with a Ki,slope value of 63 +/- 3 microM. This inhibition is dependent on an intact CoA molecule, as dephospho-CoA, dethio-CoA and acetyl-CoA are less potent inhibitors of the enzyme. Dec-2-trans-enoyl-CoA is a product-inhibitor of acyl-CoA oxidase, with a Ki,slope value of 7 +/- 1 microM.
酰基辅酶A氧化酶(EC 1.3.99.3)的活性受去污剂影响。在高于临界胶束浓度时,Triton X-100、Triton X-114和Thesit会刺激氧化酶活性。较低浓度的Triton X-100和Triton X-114使酰基辅酶A氧化酶对棕榈酰辅酶A或癸-4-顺-烯酰辅酶A的底物抑制作用不那么敏感。其他去污剂则抑制该酶的活性。发现辅酶A是该酶相对较强的竞争性抑制剂,其Ki,斜率值为63±3微摩尔。这种抑制作用依赖于完整的辅酶A分子,因为去磷酸辅酶A、去硫辅酶A和乙酰辅酶A对该酶的抑制作用较弱。癸-2-反-烯酰辅酶A是酰基辅酶A氧化酶的产物抑制剂,其Ki,斜率值为7±1微摩尔。