Thiamine-phosphate kinase
| Thiamine-phosphate kinase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.7.4.16 | ||||||||
| CAS no. | 9068-23-9 | ||||||||
| Databases | |||||||||
| BRENDA | enzyme data | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | enzyme entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| Rhea | reactions | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
Thiamine-phosphate kinase (EC 2.7.4.16) is an enzyme that catalyzes the chemical reaction
The enzyme characterised from Escherichia coli converts thiamine monophosphate to thiamine pyrophosphate by transferring a phosphate group from the cofactor, adenosine triphosphate (ATP), which is converted to adenosine diphosphate (ADP).[1]
Nomenclature
The enzyme is a transferase, specifically onee 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.[2]
Structural studies
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code PDB: 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.
- ↑ Enzyme 2.7.4.16 at KEGG Pathway Database.