Thiamine triphosphatase (THTPA)

Thiamine triphosphatase (THTPA) is a highly specific, soluble cytosolic enzyme of approximately 25 kDa, present in mammalian tissues and highly conserved among species[1][2][3]. It hydrolyzes thiamine triphosphate (ThTP) to generate thiamine diphosphate (the active cofactor form of vitamin B1) and inorganic phosphate, with an absolute requirement for divalent metal ions (e.g., magnesium) for its catalytic activity[1][2][3][6]. THTPA shows a unique tunnel-fold belonging to the triphosphate tunnel metalloenzyme (TTM) superfamily and the CYTH domain family, with high substrate specificity conferred by residues interacting with both the thiazolium and aminopyrimidine rings of thiamine[2]. The enzyme is crucial in thiamine phosphate metabolism and may indirectly influence cell signaling, especially in response to stress[2][3]. THTPA is not a current therapeutic target, and no drugs are known to act directly on this protein. Disruption of thiamine phosphate metabolism can, however, broadly affect neurological and metabolic health, reflecting the enzyme’s physiological importance[2][3][5][7].

Other names

ThTPaseTHTPaseThiamine-triphosphataseTHTPATHTPTHTPASE

Not applicable (No known drugs directly targeting this enzyme)