TALDO1 Human

Transaldolase catalyzes the transfer of a three-carbon dihydroxyacetone unit from a ketose donor to an aldose acceptor. This reaction is crucial for the non-oxidative phase of the PPP, which interconverts sugar phosphates to produce ribose-5-phosphate for nucleotide synthesis and erythrose-4-phosphate for aromatic amino acid synthesis.

Recombinant human transaldolase is a form of the enzyme that is produced through recombinant DNA technology. This involves inserting the human transaldolase gene into a suitable expression system, such as Escherichia coli, to produce the enzyme in large quantities. The recombinant enzyme is typically purified to high levels of purity (>90%) and is used for various research and clinical applications .

Transaldolase deficiency (TALDO-D) is a rare autosomal recessive disorder caused by mutations in the TALDO1 gene. This deficiency disrupts the PPP, leading to a range of clinical symptoms including intrauterine growth restriction, dysmorphic facial features, congenital heart disease, anemia, thrombocytopenia, and hepatosplenomegaly . The condition can present either prenatally or later in life with varying severity.

Recombinant human transaldolase is used in research to study the enzyme’s structure, function, and role in metabolic pathways. It is also used to investigate the molecular mechanisms underlying TALDO-D and to develop potential therapeutic strategies. Additionally, studies have shown that transaldolase from Fusarium proliferatum can demonstrate IgE cross-reactivity with its human analogue, which has implications for understanding allergic responses and developing diagnostic tools .