Biology:Thiamine diphosphokinase
| Thiamine 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 / QuickGO | ||||||||
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Thiamine diphosphokinase (EC 2.7.6.2) is an enzyme that catalyzes the chemical reaction
- REDIRECT Template:Chemical reaction
The enzyme characterised from rat liver and yeast converts thiamine to thiamine pyrophosphate by transferring a pyrophosphate group from the cofactor, adenosine triphosphate (ATP), which is converted to adenosine monophosphate (AMP).[1][2][3]
This enzyme is a transferase, specifically one 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.[4]
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.
References
- ↑ Leuthardt F; Nielsen H (1952). "Phosphorylation biologique de la thiamine". Helv. Chim. Acta 35 (4): 1196–1209. doi:10.1002/hlca.19520350415. Bibcode: 1952HChAc..35.1196L.
- ↑ "Mechanism of transpyrophosphorylation with thiamine pyrophosphokinase". J. (Tokyo) Biochem.: 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. PMID 14934742.
- ↑ Enzyme 2.7.6.2 at KEGG Pathway Database.
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