Nakabayashi T, Uchida S, Ikezawa H
Biochem Int. 1985 Dec;11(6):781-8.
Metal ion-activated acid ATPase was present in chicken liver lysosomes. The enzyme catalyzed the hydrolysis of nucleoside tri-, di-, and monophosphates and cleaved the phosphodiester linkage. Among the substrates studied, ATP was hydrolyzed at the highest rate at pH 5.4. The enzyme activity was stimulated 3.5 approximately 7.5-fold by divalent cations such as Ca2+, Mg2+, and Zn2+, but inhibited by EDTA or Hg2+.
金属离子激活的酸性ATP酶存在于鸡肝溶酶体中。该酶催化核苷三磷酸、二磷酸和单磷酸的水解，并裂解磷酸二酯键。在所研究的底物中，ATP在pH 5.4时水解速率最高。该酶的活性受到Ca2+、Mg2+和Zn2+等二价阳离子的约3.5至7.5倍的刺激，但受到EDTA或Hg2+的抑制。
