TK1 Human

TK1 is a phosphotransferase enzyme that catalyzes the phosphorylation of thymidine to thymidine monophosphate (dTMP). This reaction is the first step in the salvage pathway, which regenerates thymidine for DNA synthesis. The enzyme’s activity is tightly regulated and peaks during the S phase of the cell cycle, coinciding with DNA replication .

Human TK1 exists in different forms, including dimeric and tetrameric structures. The tetrameric form has a higher affinity for thymidine and is more active than the dimeric form. The enzyme’s activity is also influenced by various factors, including pH and temperature .

TK1 is upregulated in proliferating cells and is often found at elevated levels in cancerous tissues. This makes it a valuable biomarker for cancer diagnosis and prognosis. High serum levels of TK1 are associated with advanced cancer stages and poor prognosis. As a result, TK1 is used in clinical settings to monitor cancer progression and response to treatment .

Recombinant human TK1 is produced using genetic engineering techniques, where the TK1 gene is cloned and expressed in suitable host cells, such as bacteria or yeast. This allows for the production of large quantities of the enzyme for research and clinical applications. Recombinant TK1 retains the same functional properties as the native enzyme and is used in various assays to study DNA synthesis and repair mechanisms .

Due to its role in DNA synthesis and repair, TK1 is a potential target for cancer therapy. Inhibitors of TK1 are being explored as therapeutic agents to disrupt the proliferation of cancer cells. Additionally, assays measuring TK1 activity are used to evaluate the effectiveness of cancer treatments and to detect early signs of cancer recurrence .