MPST is a cytoplasmic enzyme that consists of 317 amino acid residues and weighs approximately 35,250 Da . It contains two rhodanese domains with similar secondary structures, suggesting a common evolutionary origin. The catalytic cysteine residue is located in the C-terminal rhodanese domain . MPST can function as a monomer or as a disulfide-linked homodimer .
The primary function of MPST is to catalyze the transfer of sulfur from 3-mercaptopyruvate to various acceptor molecules, including cyanide, which is detoxified in the process . This enzyme is also involved in the biosynthesis of thiosulfate and the production of hydrogen sulfide (H₂S), a signaling molecule with various physiological roles .
MPST is widely distributed in the cytosol of mammalian cells and is conserved from bacteria to mammals . It plays a significant role in the detoxification of cyanide, a potent inhibitor of cellular respiration . Additionally, MPST is involved in the degradation of cysteine and the production of H₂S, which has been implicated in various biological processes, including vasodilation, neurotransmission, and anti-inflammatory responses .
Recent studies have highlighted the importance of MPST in cancer biology. For instance, MPST has been shown to regulate cellular proliferation, migration, and bioenergetics in murine colon cancer cells . Pharmacological inhibition of MPST has been found to suppress H₂S production and attenuate cancer cell proliferation and migration . These findings suggest that MPST could be a potential therapeutic target for cancer treatment.
Human recombinant MPST is a form of the enzyme that is produced using recombinant DNA technology. This allows for the production of large quantities of the enzyme for research and therapeutic purposes. Recombinant MPST is used in various biochemical assays to study its function and regulation, as well as in drug development to identify potential inhibitors that could be used in cancer therapy .