Thiamin pyrophosphokinase (TPK)

Thiamin pyrophosphokinase (TPK) is an enzyme that catalyzes the transfer of a pyrophosphate group from ATP to thiamin (vitamin B1) to form thiamin pyrophosphate (TPP)[1][2][3]. TPP is essential as a coenzyme for multiple metabolic enzymes, including pyruvate dehydrogenase, α-ketoglutarate dehydrogenase, and transketolase, which are crucial for central energy metabolism[1][2]. Deficiency of thiamin or impairment of TPK function leads to severe neurological and cardiovascular disorders, such as Wernicke-Korsakoff syndrome and beriberi[1][2]. TPK operates as a dimer (and possibly tetramer) and shows a structural motif similar to the Rossmann fold, classifying it within the pyrophosphotransferase family[1][2][3].

Other names

Thiamine pyrophosphokinaseTPKEC 2.7.6.2

Catalyzes pyrophosphate transfer from ATP to thiamine, producing TPP (coenzyme for key metabolic enzymes)