Department of Immunolgy, Faculty of Medicine and Dentistry, Palacky University in Olomouc, Olomouc, Czech Republic.
Med Mycol. 2013 Jul;51(5):449-54. doi: 10.3109/13693786.2013.794310.
Cysteine dioxygenase (CDO, EC 1.13.11.20) is a key enzyme involved in the homeostatic regulation of cysteine level and in production of important oxidized metabolites of cysteine such as pyruvate, sulphite, sulphate, hypotaurine, and taurine in all eukaryotic cells. The intracellular CDO concentration is regulated at both transcriptional and posttranslational levels. In several fungi, CDO plays an important role as a virulence factor involved in morphological transition from yeast to mycelial forms. CDO is crucial for oxidation of cysteine to cysteine sulphinic acid and therefore for sulphite production and secretion. Because sulphite cleaves disulphide bridges as a first unavoidable step in keratinolysis, it is hypothesized that in dermatophytes, CDO is a virulence factor crucial for keratin degradation.
半胱氨酸双加氧酶(CDO,EC 1.13.11.20)是一种参与半胱氨酸水平的动态平衡调节的关键酶,也是所有真核细胞中半胱氨酸的重要氧化代谢产物如丙酮酸、亚硫酸盐、硫酸盐、牛磺酸和牛磺酸的生成所必需的酶。细胞内 CDO 的浓度在转录和翻译后水平上受到调节。在几种真菌中,CDO 作为一种毒力因子,在从酵母到菌丝体形式的形态转变中起着重要作用。CDO 对半胱氨酸氧化为半胱氨酸亚磺酸至关重要,因此对亚硫酸盐的产生和分泌至关重要。因为亚硫酸盐作为角蛋白水解的第一步不可避免地切断二硫键,所以推测在皮肤真菌中,CDO 是一种对角蛋白降解至关重要的毒力因子。