NSU Research Contributions

Title : Enzyme catalysis modulation through polysulfidation.

Authors : Md. Morshedul Alam

Abstract : Recent investigation in redox biology revealed the existence of a new biomolecule known as supersulfides, which are common in bacteria, mice, and human. Catenated sulfur atoms are defined as supersulfides. Some examples of supersulfides include cysteine per/tri-sulfide, glutathione per/tri-sulfides. Bunch of studies revealed various biological roles of the supersulfides such as signal transduction, protein modifications, inflammation, redox balance, understanding of host-pathogen interaction and so on. As research in this brand new filed is ongoing, a novel role of this biomolecule came in front and that was enzyme catalysis modulation capability of supersulfieds. In this review article, supersulfide-mediated enzyme catalysis modulation for a bifunctional enzyme, alcohol dehydrogenase 5 (ADH5) that has unique feature of GSNOR and FDH activity, is focused. For a long since, the mechanism of the bifunctional role of ADH5 was unknown. In this article, a focus was given on the supersulfidation-mediated regulation of ADH5 based on a recent finding of Kasamatsu et al (2023). This review will also unveil some possible clues to study some other enzymes/proteins functions due to polysulfidation-based posttranslational modification.

Journal : Annals in Review and Research	Volume : 11	Year : 2024	Issue : 4
Pages : 555816	City :	Edition :	Editors :
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