Czuba B, Vessey D A
Biochim Biophys Acta. 1981 Sep 24;665(3):612-4. doi: 10.1016/0005-2760(81)90278-2.
The N-acyltransferase enzyme which catalyzes the conjugation of the CoA adducts of bile acids with amino acid has been partially purified from dog liver. Unlike the N-acyltransferase from five other mammalian species, the enzyme from dog liver was unable to synthesize glycine conjugates from cholyl-CoA in vitro even in the presence of 0.1 M glycine. The enzyme did catalyse the synthesis of taurine conjugates. Thus, the enzyme from dog liver resembles non-mammalian forms of the enzyme which also synthesize only taurine conjugates. However, the molecular weight of the enzyme from dog liver was found to be approximately 45 700, which is similar to values reported for other mammalian forms and considerably smaller than the molecular weight of 65 000 reported previously for a non-mammalian form of the enzyme.
催化胆汁酸辅酶A加合物与氨基酸结合的N-酰基转移酶已从狗肝脏中部分纯化出来。与其他五种哺乳动物的N-酰基转移酶不同，即使在存在0.1 M甘氨酸的情况下，狗肝脏中的这种酶在体外也无法从胆酰辅酶A合成甘氨酸共轭物。该酶确实催化了牛磺酸共轭物的合成。因此，狗肝脏中的这种酶类似于该酶的非哺乳动物形式，后者也只合成牛磺酸共轭物。然而，发现狗肝脏中这种酶的分子量约为45700，这与其他哺乳动物形式报道的值相似，并且比先前报道的该酶非哺乳动物形式的65000分子量要小得多。
