glpE E.Coli

Thiosulfate sulfurtransferase, also known as rhodanese, is an enzyme that plays a crucial role in the sulfur metabolism of various organisms, including bacteria like Escherichia coli (E. coli). This enzyme is involved in the detoxification of cyanide and the assimilation of sulfur, which are essential processes for cellular function and survival.

The recombinant form of thiosulfate sulfurtransferase from E. coli is typically produced using genetic engineering techniques. The enzyme is a single polypeptide chain containing 131 amino acids, with a molecular mass of approximately 14.5 kDa . It is often fused to a His-tag at the N-terminus to facilitate purification through chromatographic techniques .

Thiosulfate sulfurtransferase catalyzes the transfer of a sulfur atom from thiosulfate to cyanide, forming thiocyanate and sulfite. This reaction is crucial for the detoxification of cyanide, a potent inhibitor of cellular respiration. The enzyme also plays a role in the sulfur assimilation pathway, converting thiosulfate to sulfite, which can then be further reduced to sulfide and incorporated into amino acids like cysteine and methionine .

Sulfur is an essential element for all living organisms, as it is a component of amino acids, vitamins, and coenzymes. In E. coli, the assimilation of sulfur from thiosulfate is particularly advantageous because it requires less energy compared to sulfate assimilation . This makes thiosulfate a preferred sulfur source under certain conditions, enhancing microbial growth and biotechnological applications such as the fermentative overproduction of L-cysteine .

The recombinant thiosulfate sulfurtransferase from E. coli has several applications in biotechnology and industrial processes. It is used in the production of L-cysteine, an amino acid with numerous applications in food, pharmaceuticals, and cosmetics . Additionally, the enzyme’s role in cyanide detoxification makes it valuable for bioremediation efforts to clean up cyanide-contaminated environments .