Thiamine diphosphokinase

In enzymology, a thiamine diphosphokinase (EC 2.7.6.2) is an enzyme that catalyzes the chemical reaction

ATP + thiamine ${\displaystyle \rightleftharpoons }$ AMP + thiamine diphosphate

thiamin diphosphokinase
Identifiers
EC no.	2.7.6.2
CAS no.	9026-24-8
Databases
IntEnz	IntEnz view
BRENDA	BRENDA entry
ExPASy	NiceZyme view
KEGG	KEGG entry
MetaCyc	metabolic pathway
PRIAM	profile
PDB structures	RCSB PDB PDBe PDBsum
Gene Ontology	AmiGO / QuickGO
Search PMC articles PubMed articles NCBI proteins

Thus, the two substrates of this enzyme are ATP 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 (diphosphotransferases). 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.

Structural studies

As of late 2007, six structures have been solved for this class of enzymes, with PDB accession codes 1IG0, 1IG3, 2F17, 2G9Z, 2HH9, and 2OMK.