Thiamine pyrophosphokinase (TPK, EC:2.7.6.2, also spelled thiamin pyrophosphokinase) catalyzes the transfer of a pyrophosphate group from ATP to vitamin B1 (thiamine) to form the coenzyme thiamine pyrophosphate (TPP). TPP is required for central metabolic functions, and thiamine deficiency is associated with potentially fatal human diseases. The structure of thiamine pyrophosphokinase suggests that the enzyme may operate by a mechanism of pyrophosphoryl transfer similar to those described for pyrophosphokinases functioning in nucleotide biosynthesis.
Comment:The active site is located at the dimer interface, with residues from both monomers participating
Structure:2F17: Mouse TPK dimer binds AMP (or EPE), Mg, and the antibacterial compound pyrithiamin pyrophosphate, a substrate analog, at each of the two binding sites; contacts at 4A
Jiyao W et al.(2023). "The conserved domain database in 2023.",