Reach Us +44 7456035580

Abstract

Thioredoxin-dependent Redox-sensing Molecular Switches in Hydrogen Sulfide and/or Polysulfides Producing Enzyme, 3-Mercaptopyruvate Sulfurtransferase

The rat 3-mercaptopyruvate sulfurtransferase (MST), a multifunctional enzyme, has redox-sensing molecular switches, a catalytic Cys247 and two cysteines, Cys154 and Cys263, on the outer surface of the enzyme. These switches are reduced or oxidized according to the redox state of their surrounding environment and require a redox active cysteine in thioredoxin (Trx) to interact with MST. Recently, MST has been demonstrated to be involved in the production of possible signaling molecules such as hydrogen sulfide, polysulfides, and/or sulfur oxides. However, the relationship between the production of signaling molecule(s) and action of these redox-sensing molecular switches has not been clarified, and a precise investigation of this relationship is underway.


Author(s):

Noriyuki Nagahara



Abstract | Full-Text | PDF

Share this  Facebook  Twitter  LinkedIn  Google+
30+ Million Readerbase
Recommended Conferences
Flyer image
Abstracted/Indexed in
  • Google Scholar
  • China National Knowledge Infrastructure (CNKI)
  • Cosmos IF
  • Geneva Foundation for Medical Education and Research
  • Secret Search Engine Labs