Thiamine diphosphokinase

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thiamin diphosphokinase
Identifiers
EC number 2.7.6.2
CAS number 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 / EGO

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

ATP + thiamine \rightleftharpoons AMP + thiamine diphosphate

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[edit]

As of late 2007, 6 structures have been solved for this class of enzymes, with PDB accession codes 1IG0, 1IG3, 2F17, 2G9Z, 2HH9, and 2OMK.

References[edit]

  • Leuthardt F and Nielsen H (1952). "Phosphorylation biologique de la thiamine". Helv. Chim. Acta 35 (4): 1196–1209. doi:10.1002/hlca.19520350415. 
  • Shimazono N, Mano Y, Tanaka R and Kajiro Y (Tokyo). "Mechanism of transpyrophosphorylation with thiamine pyrophosphokinase". J. Biochem.: 959–961.  Check date values in: |date= (help)
  • Steyn-Parve EP (1952). "Partial purification and properties of thiaminokinase from yeast". Biochim. Biophys. Acta 8: 310–324. doi:10.1016/0006-3002(52)90046-2. PMID 14934742.