enzymology Enzymes () are proteins that act as biological catalysts by accelerating chemical reactions. The molecules upon which enzymes may act are called substrates, and the enzyme converts the substrates into different molecules known as products. A ...

, a thiamine diphosphokinase () is an enzyme that

catalyzes Catalysis () is the process of increasing the rate of a chemical reaction by adding a substance known as a catalyst (). Catalysts are not consumed in the reaction and remain unchanged after it. If the reaction is rapid and the catalyst recyc ...

the chemical reaction :ATP + thiamine

\rightleftharpoons

AMP + thiamine diphosphate Thus, the two substrates of this enzyme are

ATP ATP may refer to: Companies and organizations * Association of Tennis Professionals, men's professional tennis governing body * American Technical Publishers, employee-owned publishing company * ', a Danish pension * Armenia Tree Project, non ...

and thiamine, whereas its two products are AMP and thiamine diphosphate. This enzyme belongs to the family of transferases, specifically those transferring two phosphorus-containing groups (

diphosphotransferase Diphosphotransferase are phosphotransferase enzymes which act upon pyrophosphate In chemistry, pyrophosphates are phosphorus oxyanions that contain two phosphorus atoms in a P–O–P linkage. A number of pyrophosphate salts exist, such as diso ...

s). The systematic name of this enzyme class is ATP:thiamine diphosphotransferase. Other names in common use include thiamin kinase, thiamine pyrophosphokinase, ATP:thiamin pyrophosphotransferase, thiamin pyrophosphokinase, thiamin pyrophosphotransferase, thiaminokinase, thiamin:ATP pyrophosphotransferase, and TPTase. This enzyme participates in

thiamine metabolism Thiamine, also known as thiamin and vitamin B1, is a vitamin, an essential micronutrient, that cannot be made in the body. It is found in food and commercially synthesized to be a dietary supplement or medication. Phosphorylated forms of thia ...

Structural studies

As of late 2007, six structures have been solved for this class of enzymes, with PDB accession codes , , , , , and .

References

* * * EC 2.7.6 Enzymes of known structure {{2.7-enzyme-stub