Dunn P P, Slabas A R, Moore A L
Biochem J. 1986 Feb 1;233(3):839-44. doi: 10.1042/bj2330839.
The catalytic properties of cuckoo-pint (Arum maculatum) mitochondrial adenosine triphosphatase have been analysed. The pH profile, effect of inhibitors, cold-stability and substrate specificity are characteristic of mitochondrial adenosine triphosphatases, although a high guanosine triphosphatase activity does appear to be restricted to plant mitochondrial adenosine triphosphatases. The kinetic properties of nucleoside 5'-triphosphate hydrolysis by membrane-bound and soluble enzymes have been studied by means of double-reciprocal plots. These plots were linear in the absence of an activating anion, which may indicate that the catalytic and/or regulatory mechanism of Arum maculatum adenosine triphosphatase is different from that of other enzyme preparations. It is suggested that the differences in subunit composition of plant and mammalian adenosine triphosphatases reported previously [Dunn, Slabas & Moore (1985) Biochem. J. 225, 821-824] are structurally, rather than functionally, significant.
对斑叶疆南星（Arum maculatum）线粒体三磷酸腺苷酶的催化特性进行了分析。其pH曲线、抑制剂的作用、冷稳定性和底物特异性均为线粒体三磷酸腺苷酶的特征，不过较高的三磷酸鸟苷酶活性似乎仅限于植物线粒体三磷酸腺苷酶。通过双倒数作图法研究了膜结合酶和可溶性酶水解核苷5'-三磷酸的动力学特性。在没有激活阴离子的情况下，这些图呈线性，这可能表明斑叶疆南星三磷酸腺苷酶的催化和/或调节机制与其他酶制剂不同。有人提出，先前报道的植物和哺乳动物三磷酸腺苷酶亚基组成的差异在结构上而非功能上具有重要意义。
