Del Campo G, Puente J, Valenzuela M A, Traverso-Cori A, Cori O
Biochem J. 1977 Dec 1;167(3):525-9. doi: 10.1042/bj1670525.
A highly purified isoenzyme of apyrase obtained from potatoes (Solanum tuberosum var. Pimpernel) exhibits a low specificity for the organic moiety of synthetic pyro- and triphosphates. Methyl di- and tri-phosphates were hydrolysed at higher rates than ADP and ATP, but their Km values were also higher. Steric hindrance at the carbon atom linked to the pyrophosphate chain decreases both binding and maximum rate, whereas length or polarity of the organic chain do not have systematic effects. t-Butyl diphosphate, inorganic pyrophosphate, adenosine 5'-[alpha,beta-methylene]triphosphate and adenosine 5'-[beta,gamma-methylene]triphosphate are competitive inhibitors of the hydrolysis of ATP and ADP.
从马铃薯（Solanum tuberosum var. Pimpernel）中获得的一种高度纯化的腺苷三磷酸双磷酸酶同工酶，对合成焦磷酸和三磷酸的有机部分表现出低特异性。甲基二磷酸和三磷酸的水解速率高于二磷酸腺苷（ADP）和三磷酸腺苷（ATP），但其米氏常数（Km值）也更高。与焦磷酸链相连的碳原子处的空间位阻会降低结合力和最大反应速率，而有机链的长度或极性则没有系统性影响。叔丁基二磷酸、无机焦磷酸、腺苷5'-[α,β-亚甲基]三磷酸和腺苷5'-[β,γ-亚甲基]三磷酸是ATP和ADP水解的竞争性抑制剂。
