Understanding and exploiting bacterial sulfatases

细菌硫酸酯酶参与环境养分循环并参与细菌的发病机制。这些酶催化硫酸盐酯的水解，并具有不寻常的翻译后活性位点修饰，其中半胱氨酸残基被氧化为甲酰甘氨酸。我们将详细研究这些酶的作用机制，并设计利用这种氨基酸的反应性的抑制剂。这项工作具有重要意义，因为它可以应用于治疗癌症和细菌感染等领域。此外，我们将从肝素降解细菌黄杆菌中克隆新的碳水化合物硫酸酯酶。这些磺化酶将在生物技术中用于表征磺化糖缀合物。

Bacterial sulfatases participate in environmental nutrient cycling and are implicated in bacterial pathogenesis mechanisms. These enzymes catalyze the hydrolysis of sulfate esters and possess an unusual posttranslational active-site modification where a cysteine residue is oxidized to formylglycine. We will study the mechanism of these enzymes in detail and design inhibitors that exploit the reactivity of this aminoacid. This work has significance because of application to areas that include the treatment of cancer and bacterial infections. Additionally, we will clone novel carbohydrate sulfatases from the heparin-degrading bacterium Flavobacterium heparinum. These sulfatases will have use in biotechnology for characterization of sulfated glycoconjugates.