Abstract
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.
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