Thiamine-phosphate kinase
| thiamin phosphate kinase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.7.4.16 | ||||||||
| CAS no. | 9068-23-9 | ||||||||
| 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 | ||||||||
| |||||||||
In enzymology, a thiamine-phosphate kinase (EC 2.7.4.16) is an enzyme that catalyzes the chemical reaction
- ATP + thiamine phosphate ADP + thiamine diphosphate
Thus, the two substrates of this enzyme are ATP and thiamine phosphate, whereas its two products are ADP and thiamine diphosphate.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with a phosphate group as acceptor. The systematic name of this enzyme class is ATP:thiamine-phosphate phosphotransferase. Other names in common use include thiamin-monophosphate kinase, thiamin monophosphatase, and thiamin monophosphokinase. This enzyme participates in thiamine metabolism.
Structural studies
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 1VQV.
References
- Nishino H (November 1972). "Biogenesis of cocarboxylase in Escherichia coli. Partial purification and some properties of thiamine monophosphate kinase". Journal of Biochemistry. 72 (5): 1093–100. doi:10.1093/oxfordjournals.jbchem.a129996. PMID 4567662.
