SHMT2 is a pyridoxal phosphate-dependent enzyme that catalyzes the reversible reaction of serine and tetrahydrofolate to glycine and 5,10-methylene tetrahydrofolate. It is primarily responsible for glycine synthesis and is considered the main source of intracellular glycine. SHMT2 is mainly localized in mitochondria and is involved in the conversion of serine to glycine, which is crucial for one-carbon unit metabolism. This process supports the synthesis of thymidine and purines, promoting tumor growth. SHMT2 is highly expressed in various human tumors, including hepatocellular carcinoma, breast cancer, and non-small-cell lung cancer (NSCLC). Its elevated expression is associated with poor prognosis, and it may serve as a prognostic marker and a target for anticancer therapies. In cancer cells, SHMT2 supports tumor cell proliferation by maintaining redox balance and cell survival. It is involved in metabolic reprogramming, which is a significant hallmark of cancer. Genetic variations in the SHMT2 gene are significantly associated with changes in metabolic parameters such as circulating lipids, body mass indexes, and diabetic indicators, suggesting that SHMT2 may influence the development and outcome of metabolic syndrome in humans.
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