Abstract：
Thiol oxidation to dioxygenated sulfinic acid is catalyzed by an enzyme family characterized by a cupin fold. These proteins act on free thiol-containing molecules to generate central metabolism precursors and signaling compounds in bacteria, fungi, and animal cells. In plants and animals, they also oxidize exposed N-cysteinyl residues, directing proteins to proteolysis. Enzyme kinetics, X-ray crystallography, and spectroscopy studies prompted the formulation and testing of hypotheses about the mechanism of action and the different substrate specificity of these enzymes. Concomitantly, the physiological role of thiol dioxygenation in prokaryotes and eukaryotes has been studied through genetic and physiological approaches. Further structural characterization is necessary to enable precise and safe manipulation of thiol dioxygenases (TDOs) for therapeutic, industrial, and agricultural applications.
摘要：
硫醇氧化成双氧化的亚磺酸是由以立方折叠为特征的酶家族催化的。这些蛋白质作用于游离的含巯基分子，在细菌中产生中枢代谢前体和信号化合物，真菌,和动物细胞。在植物和动物中，它们还氧化暴露的N-半胱氨酰残基，引导蛋白质进行蛋白水解。酶动力学，X射线晶体学,和光谱学研究促使有关这些酶的作用机理和不同底物特异性的假设的提出和测试。同时，已经通过遗传和生理方法研究了巯基双氧合在原核生物和真核生物中的生理作用。进一步的结构表征是必要的，以实现精确和安全的硫醇双加氧酶（TDOs）的治疗操作，工业,和农业应用。
