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 , 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.
- EC 2.7.4
- Enzymes of known structure
- EC 2.7 stubs