Kurihara T, Ueda M, Tanaka A
Department of Industrial Chemistry, Faculty of Engineering, Kyoto University, Japan.
FEBS Lett. 1988 Feb 29;229(1):215-8. doi: 10.1016/0014-5793(88)80830-5.
Two kinds of 3-ketoacyl-CoA thiolases were found in the peroxisomes of Candida tropicalis cells grown on n-alkanes (C10-C13). One was a typical acetoacetyl-CoA thiolase specific only to acetoacetyl-CoA, while another was 3-ketoacyl-CoA thiolase showing high activities on the longer chain substrates. A high level of the latter thiolase activity in alkane-grown cells was similar to that of other enzymes constituting the fatty acid beta-oxidation system in yeast peroxisomes. These facts suggest that the complete degradation of fatty acids to acetyl-CoA is carried out in yeast peroxisomes by the cooperative contribution of acetoacetyl-CoA thiolase and 3-ketoacyl-CoA thiolase.
在以正构烷烃（C10 - C13）为碳源生长的热带假丝酵母细胞的过氧化物酶体中发现了两种3 - 酮酰基辅酶A硫解酶。一种是典型的仅对乙酰乙酰辅酶A具有特异性的乙酰乙酰辅酶A硫解酶，而另一种是对较长链底物具有高活性的3 - 酮酰基辅酶A硫解酶。在烷烃培养的细胞中，后一种硫解酶的高活性水平与构成酵母过氧化物酶体中脂肪酸β - 氧化系统的其他酶的活性水平相似。这些事实表明，在酵母过氧化物酶体中，脂肪酸完全降解为乙酰辅酶A是由乙酰乙酰辅酶A硫解酶和3 - 酮酰基辅酶A硫解酶共同作用完成的。
