Understanding human thiol dioxygenase enzymes: structure to function, and biology to pathology.

摘要: Amino acid metabolism is a significant metabolic activity in humans, especially of sulphur-containing amino acids, methionine and cysteine (Cys). Cys cytotoxic neurotoxic nature; hence, mammalian cells maintain constant intracellular level Cys. Metabolism mainly regulated by two thiol dioxygenases: dioxygenase (CDO) 2-aminoethanethiol (ADO). CDO ADO are the only human dioxygenases reported with role localized to mitochondria. This pathway important various disorders, as it responsible for synthesis antioxidant glutathione also hypotaurine taurine. most extensively studied protein, whose high-resolution crystallographic structures have been solved. As compared CDO, less studied, even though has key cysteamine metabolism. To further understand ADO's structure function, three-dimensional predicted from I-TASSER SWISS-MODEL servers validated PROCHECK software. Structural superimposition approach using iPBA web server confirmed near-identical (including active sites) protein models CDO. In addition, protein-protein interaction their association patho-physiology crucial understanding functions. Both interacting partner profiles presented STRING database. this study, we 3D model summarized biological roles pathological consequences which associated altered expression functioning case cancer, neurodegenerative disorders other diseases.