Recombinant Human GLDC protein

**Background of GLDC Recombinant Protein**

Glycine Decarboxylase (GLDC) is a mitochondrial enzyme central to the glycine cleavage system (GCS), a critical metabolic pathway responsible for glycine catabolism. GLDC, also known as the P-protein, catalyzes the decarboxylation of glycine, producing 5.10-methylene tetrahydrofolate, carbon dioxide, and ammonia. This reaction is essential for one-carbon metabolism, linking amino acid homeostasis to nucleotide synthesis, methylation processes, and energy production. Dysregulation of GLDC activity is strongly associated with non-ketotic hyperglycinemia (NKH), a rare autosomal recessive disorder characterized by glycine accumulation, leading to severe neurological impairments.

Recombinant GLDC protein is engineered using biotechnological methods to enable detailed functional and structural studies. By cloning the GLDC gene into expression vectors (e.g., bacterial, yeast, or mammalian systems), researchers produce purified GLDC protein with high specificity and activity. Mammalian systems, such as HEK293 cells, are often preferred to ensure proper post-translational modifications and folding, given GLDC’s mitochondrial localization and multi-subunit complexity.

The recombinant protein serves as a vital tool for investigating NKH pathogenesis, screening potential therapeutics, and elucidating structure-function relationships. For instance, studies using recombinant GLDC have identified disease-causing mutations and evaluated their impact on enzyme stability or cofactor binding. Additionally, it aids in developing enzyme replacement strategies or gene therapies for NKH. Beyond clinical applications, GLDC recombinant protein is used in metabolic research to dissect its role in cancer progression, as altered glycine metabolism is linked to tumor proliferation.

Overall, GLDC recombinant protein bridges gaps between molecular biology and translational medicine, offering insights into metabolic disorders and guiding therapeutic innovation.