TPI1 Human

TPI is a homodimer, meaning it consists of two identical protein subunits . The enzyme’s active site is highly conserved and is responsible for its catalytic activity. The structure of TPI has been extensively studied, revealing key residues involved in its function and stability . The enzyme’s efficiency is attributed to its precise structural configuration, which facilitates the rapid interconversion of DHAP and G3P .

Mutations in the TPI1 gene can lead to a rare genetic disorder known as triosephosphate isomerase deficiency . This autosomal recessive disorder is characterized by chronic hemolytic anemia, cardiomyopathy, susceptibility to infections, severe neurological dysfunction, and often results in early childhood death . The deficiency is caused by a significant reduction in TPI activity, leading to an accumulation of DHAP, which is toxic to cells .

Human recombinant TPI1 refers to the enzyme produced through recombinant DNA technology. This involves inserting the human TPI1 gene into a suitable expression system, such as bacteria or yeast, to produce the enzyme in large quantities. Recombinant TPI1 is used in various research applications to study the enzyme’s structure, function, and role in metabolic pathways. It also serves as a tool for investigating the molecular mechanisms underlying TPI deficiency and for developing potential therapeutic interventions .

Recent studies have uncovered additional roles for TPI beyond its glycolytic function. These include potential nuclear functions and involvement in cancer pathogenesis and chemotherapy resistance . Such findings suggest that TPI may have multiple functions independent of its catalytic activity, a phenomenon known as moonlighting .