Thiamine diphosphokinase (EC 2.7.6.2) is an enzyme that catalyzes the 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 PDB: 1IG0, PDB: 1IG3, PDB: 2F17, PDB: 2G9Z, PDB: 2HH9, and PDB: 2OMK.
References
- ↑ Leuthardt F; Nielsen H (1952). "Phosphorylation biologique de la thiamine". Helv. Chim. Acta. 35 (4): 1196–1209. Bibcode:1952HChAc..35.1196L. 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.
- ↑ Enzyme 2.7.6.2 at KEGG Pathway Database.
