In enzymology, a thiamine diphosphokinase (EC 2.7.6.2) is an enzyme that catalyzes the chemical reaction
| 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 | ||||||||
| |||||||||
- ATP + thiamine 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
editAs of late 2007, six structures have been solved for this class of enzymes, with PDB accession codes 1IG0, 1IG3, 2F17, 2G9Z, 2HH9, and 2OMK.
References
edit- Leuthardt F; 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, Kajiro Y. "Mechanism of transpyrophosphorylation with thiamine pyrophosphokinase". J. Biochem. Tokyo: 959–961.
- Steyn-Parve EP (1952). "Partial purification and properties of thiaminokinase from yeast". Biochim. Biophys. Acta. 8 (3): 310–324. doi:10.1016/0006-3002(52)90046-2. hdl:1874/23856. PMID 14934742.
