PSAT1 catalyzes the reversible conversion of 3-phosphohydroxypyruvate to phosphoserine, which is the second step in the de novo serine synthesis pathway . This reaction is essential for the production of serine, a non-essential amino acid that serves as a precursor for several biomolecules, including glycine, cysteine, and sphingolipids .
The enzyme requires pyridoxal-5’-phosphate (PLP) as a cofactor to facilitate the transfer of amino groups . The activity of PSAT1 is measured by its ability to produce 3-phosphooxypyruvate, with a specific activity greater than 130 pmol/min/μg under specified conditions .
Recombinant human PSAT1 is typically expressed in Escherichia coli (E. coli) and is purified with a C-terminal 6-His tag for ease of purification and detection . The recombinant protein has a predicted molecular mass of approximately 41 kDa, although it may appear as a 40 kDa band on SDS-PAGE under reducing conditions .
Mutations in the PSAT1 gene can lead to phosphoserine aminotransferase deficiency, a rare metabolic disorder characterized by low levels of serine and glycine in the blood and cerebrospinal fluid . This condition can result in severe neurological symptoms, including seizures, microcephaly, and psychomotor retardation .
Additionally, altered expression of PSAT1 has been implicated in various cancers. Overexpression of PSAT1 has been observed in certain types of cancer, suggesting that the enzyme may play a role in tumor growth and survival .
Recombinant human PSAT1 is widely used in biochemical and medical research to study the serine biosynthesis pathway and its regulation . It is also utilized in the development of therapeutic strategies for conditions associated with serine deficiency and in cancer research to explore potential targets for drug development .