April 9, 2020

The Banerjee lab publishes a paper in the Journal of Biological Chemistry

Thioredoxin regulates human mercaptopyruvate sulfurtransferase at physiologically relevant concentrations

Model for thioredoxin-mediated regulation of MPST

3-Mercaptopyruvate sulfur transferase (MPST) catalyzes the desulfuration of 3-mercaptopyruvate (3-MP) and transfers sulfane sulfur from an enzyme-bound persulfide intermediate to thiophilic acceptors such as thioredoxin (Trx) and cysteine. Hydrogen sulfide (H2S), a signaling molecule implicated in many physiological processes, can be released from the persulfide product of the MPST reaction. Members of the Banerjee lab and their collaborators characterized the poorly studied cytosolic form of MPST1 and used results from kinetic experiments and simulations to propose a model for how thioredoxin modulates the MPST-catalyzed reaction in a physiologically relevant concentration range.

Read the JBC article HERE.