Thiamine kinase
Class of enzymes
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Thiamine kinase (EC 2.7.1.89) is an enzyme that catalyzes the chemical reaction
| Thiamin kinase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.7.1.89 | ||||||||
| CAS no. | 62213-38-1 | ||||||||
| 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 | ||||||||
| |||||||||
The enzyme characterised from Escherichia coli converts thiamine to thiamine monophosphate by transferring a phosphate group from the cofactor, adenosine triphosphate (ATP), which is converted to adenosine diphosphate (ADP).[1]
This enzyme is a transferase, specifically one transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is ATP:thiamine phosphotransferase. Other names in common use include thiamin kinase (phosphorylating), thiamin phosphokinase, ATP:thiamin phosphotransferase, and thiamin kinase. This enzyme participates in thiamine metabolism.[2]
