ULTRA HIGH RESOLUTION STUDIES OF CPO

来自海洋真菌的糖蛋白氯过氧化物酶 (CPO) Caldariomyces fumago 是所有血红素酶中用途最广泛的 已知。 除了催化过氧化物的生物功能外 依赖卤化反应，该酶可以催化 过氧化氢酶、过氧化物酶和细胞色素P450的反应。 它催化 多种有机底物的对映选择性氧化， 这使其成为一种潜在的工业酶。 从结构上来说，这 蛋白质具有独特的折叠和大量有序的碳水化合物。 我们报道了 CPO 的晶体结构，分辨率为 1.9 E。 早期测试表明 CPO 晶体可以衍射到更好的 1.4 同步加速器低温条件下的E分辨率 X 射线。 在更高分辨率下确定的 CPO 结构为 预计会显示出更有序的碳水化合物结构并增加我们的 了解糖蛋白的结构。

The glycoprotein chlorperoxidase (CPO) from the marine fungus Caldariomyces fumago is the most versatile of all the heme enzymes known. In addition to its biological function of catalyzing peroxide dependent halogenation reactions, this enzyme can catalyze the reactions of catalase, peroxidase and cytochrome P450. It catalyzes enantioselective oxidation of a wide range of organic substrates, which makes it a potential industrial enzyme. Structurally, this protein has a unique fold and a large number of ordered carbohydrates. We have reported the crystal structure of CPO at 1.9 E resolution. Earlier tests indicated that the CPO crystals can diffract to better 1.4 E resolution under cryogenic conditions in synchrotron X-radiation. CPO structure determined at higher resolution is expected to show more ordered carbohydrate structure and increase our understanding of the structure glycoproteins.