Recombinant E. coli TST protein

Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

TST known as thiosulfate sulfurtransferase or rhodanese is an important enzyme involved in the detoxification of cyanide. It facilitates the transfer of sulfur to cyanide converting it into less harmful thiocyanate which the body can excrete. The enzyme has a molecular mass of approximately 33 kDa. It is highly expressed in the liver kidney and mitochondria of cells making it an important player in cellular detoxification processes.

Biological function summary

TST is important for maintaining sulfur metabolism and cyanide detoxification in the body. The enzyme is part of a multi-component system that helps neutralizing potentially toxic substances. By acting on substrates such as thiosulfate and cyanide TST forms an important partnership with other sulfurtransferases to support various cellular functions. Through its enzymatic actions TST contributes to oxidative stress regulation and cellular homeostasis.

Pathways

TST holds a significant position in the sulfur metabolism and detoxification pathways. It interacts with key proteins in these pathways like cysteine and methionine impacting amino acid metabolism. TST's function aligns with the mitochondrial respiratory chain helping to manage oxidative stress. Its activity also influences the levels of hydrogen sulfide a well-known signaling molecule linking TST to broader cellular activities involving oxidative stress responses.

TST has connections to conditions such as cyanide poisoning and hereditary rhodanese deficiency. Abnormal TST activity can disrupt normal detoxification and lead to metabolic imbalances affecting cellular health. Moreover insufficient TST function may associate with mitochondrial disorders given its close relationship with mitochondrial activity. This disruption in function can also correlate with oxidative stress leading to further cellular damage and health complications.