Thiol dioxygenases: from structures to functions

Trends Biochem Sci. 2024 Apr 15:S0968-0004(24)00073-2. doi: 10.1016/j.tibs.2024.03.007. Online ahead of print.ABSTRACTThiol 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.PMID:38622038 | DOI:10.1016/j.tibs.2024.03.007

Source: Trends in Biochemical Sciences - April 15, 2024 Category: Biochemistry Authors: Monica Perri Francesco Licausi Source Type: research