PYCR2 Human

Pyrroline-5-Carboxylate Reductase 2 (PYCR2) is an enzyme that plays a crucial role in the biosynthesis of proline, an amino acid essential for protein synthesis and cellular function. PYCR2 is a member of the pyrroline-5-carboxylate reductase family, which includes PYCR1 and PYCR3. These enzymes catalyze the final step in the conversion of pyrroline-5-carboxylate (P5C) to proline, a reaction that is vital for maintaining cellular homeostasis and metabolic processes .

PYCR2 is a mitochondrial enzyme that shares a high degree of structural homology with PYCR1, with both enzymes being involved in the glutamate-P5C-proline pathway. The enzyme operates as a decameric structure, consisting of five homodimer subunits, each containing catalytic sites for substrate and cofactor binding . The primary function of PYCR2 is to facilitate the reduction of P5C to proline using NADH as a cofactor .

Proline plays a significant role in various cellular processes, including protein synthesis, cell signaling, and stress response. The production of proline is particularly important in rapidly proliferating cells, such as cancer cells, where it supports protein synthesis and redox balance . Overexpression of PYCR2 has been linked to the progression of certain cancers, making it a potential target for therapeutic intervention .

Human recombinant PYCR2 is produced using recombinant DNA technology, which involves inserting the PYCR2 gene into a suitable expression system, such as bacteria or yeast. This allows for the large-scale production of the enzyme, which can be used for research and therapeutic purposes. Recombinant PYCR2 retains the same structural and functional properties as the naturally occurring enzyme, making it a valuable tool for studying proline metabolism and its role in disease .