Uyeda M, Nagao K, Kido Y, Suzuki K, Hara Y, Yamamura R
Faculty of Pharmaceutical Sciences, Kumamoto University, Japan.
J Enzyme Inhib. 1992;6(2):157-64. doi: 10.3109/14756369209040747.
5838-DNI, an inhibitor of deoxyribonuclease (DNase) II from porcine spleen was produced by Streptomyces sp. strain No. A-5838. The structure of 5838-DNI was shown to be 1,4,4a,5,12,12a-hexahydro-4,4a,11,12a-tetrahydroxy-3,8-dimethoxy-9- methoxycarbonyl-10-methyl-1,5,12-trioxo naphthacene. Although similar in structure to tetracenomycin C, which is an antibiotic against Gram-positive bacteria, 5838-DNI has different antibacterial activity. 5838-DNI was distinguished from 5923-DNI, a previously reported DNase II inhibitor, in inhibitory activity against each enzyme. 5838-DNI showed dependency of inhibition on pH and temperature, and inhibited phosphodiesterase I in a competitive manner. These data suggest that 5838-DNI is the first reported example of an inhibitor of microbial origin which is able to inhibit DNase II and phosphodiesterase I.
5838-DNI是由链霉菌属A-5838菌株产生的一种猪脾脏脱氧核糖核酸酶（DNase）II抑制剂。5838-DNI的结构为1,4,4a,5,12,12a-六氢-4,4a,11,12a-四羟基-3,8-二甲氧基-9-甲氧基羰基-10-甲基-1,5,12-三氧萘并四苯。尽管5838-DNI在结构上与对革兰氏阳性菌有抗菌活性的四环素霉素C相似，但它具有不同的抗菌活性。5838-DNI在对每种酶的抑制活性方面与先前报道的DNase II抑制剂5923-DNI有所不同。5838-DNI的抑制作用表现出对pH和温度的依赖性，并以竞争性方式抑制磷酸二酯酶I。这些数据表明，5838-DNI是首次报道的来源于微生物且能够抑制DNase II和磷酸二酯酶I的抑制剂实例。
