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.
Declaration of interest: The authors report no conflicts of interest. The authors alone are responsible for the content and the writing of the paper.
Supported by the grants CZ.1.07/2.3.00/20.0164 (Ministry of Education, Youth and Sport, Czech Republic) and internal grant LF_2012_011 (Faculty of Medicine and Dentistry, Palacky University in Olomouc, Czech Republic).