PSAT1 Protein, Human (N-His)

The PSAT1 protein plays a central role in cellular metabolism by catalyzing the reversible conversion of 3-phosphohydroxypyruvate to phosphoserine and 3-hydroxy-2-oxo-4-phosphonooxybutyrate to phosphohydroxythreonine. These enzyme activities are key steps in the biosynthetic pathway of the essential amino acids serine and threonine. PSAT1 Protein, Human (N-His) is the recombinant human-derived PSAT1 protein, expressed by E. coli , with N-6*His labeled tag. The total length of PSAT1 Protein, Human (N-His) is 354 a.a., .

The PSAT1 (Phosphoserine aminotransferase 1) protein is an enzyme that catalyzes the reversible conversion of 3-phosphohydroxypyruvate to phosphoserine and 3-hydroxy-2-oxo-4-phosphonooxybutanoate to phosphohydroxythreonine. This enzymatic activity is a key step in the serine biosynthetic pathway, contributing to the synthesis of essential amino acids and cellular processes such as nucleotide and protein biosynthesis. Phosphoserine and phosphohydroxythreonine generated by PSAT1 serve as precursors for the production of serine and glycine, both of which are crucial for various metabolic pathways and cellular functions. PSAT1's role in serine biosynthesis underscores its importance in maintaining cellular homeostasis and provides potential insights into therapeutic approaches for conditions involving dysregulated amino acid metabolism.

Human

E. coli

N-6*His

Q9Y617 (L17-L370)

29968

Greater than 90% as determined by reducing SDS-PAGE.

<1 EU/μg, determined by LAL method.