3’-Phosphoadenosine 5’-Phosphosulfate Synthase 1 (PAPSS1) is a crucial enzyme in the biosynthesis of 3’-Phosphoadenosine 5’-Phosphosulfate (PAPS), a key molecule involved in sulfation reactions. Sulfation is an essential biochemical process that modifies various molecules, including hormones, drugs, and xenobiotics, enhancing their solubility and excretion.
PAPSS1 is a bifunctional enzyme that catalyzes two sequential reactions. It first converts adenosine 5’-phosphosulfate (APS) to PAPS using ATP as a phosphate donor. This enzyme is composed of two domains: an ATP sulfurylase domain and an APS kinase domain . The ATP sulfurylase domain catalyzes the formation of APS from ATP and sulfate, while the APS kinase domain phosphorylates APS to form PAPS .
PAPS is the most common coenzyme in sulfotransferase reactions, which are part of the sulfation pathways . These pathways are vital for the metabolism and detoxification of various endogenous and exogenous compounds. In humans, PAPSS1 and its isoform PAPSS2 are responsible for the endogenous synthesis of PAPS .
Recombinant PAPSS1 is produced using Escherichia coli (E. coli) expression systems. The recombinant protein is typically a non-glycosylated polypeptide chain containing 626 amino acids and has a molecular mass of approximately 70.9 kDa . It is purified using proprietary chromatographic techniques to ensure high purity and activity .
Recombinant PAPSS1 is typically stored at -20°C for long-term storage and at 4°C for short-term use. To maintain its stability, it is recommended to avoid multiple freeze-thaw cycles and to add a carrier protein, such as human serum albumin (HSA) or bovine serum albumin (BSA), for long-term storage .