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Thiamine kinase

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Thiamin kinase
Identifiers
EC no.2.7.1.89
CAS no.62213-38-1
Databases
BRENDAenzyme data
ExPASyNiceZyme view
KEGGenzyme entry
MetaCycmetabolic pathway
Rheareactions
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
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PMCarticles
PubMedarticles
NCBIproteins

Thiamine kinase (EC 2.7.1.89) is an enzyme that catalyzes the chemical reaction

ATP +
 
 
 
 
Reversible left-right reaction arrow
 
 
 
ADP +
 

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]

References

[edit]
  1. ↑ Iwashima A, Nishino H, Nose Y (1972). "Conversion of thiamine to thiamine monophosphate by cell-free extracts of Escherichia coli". Biochim. Biophys. Acta. 258 (1): 333–6. doi:10.1016/0005-2744(72)90991-6. PMID 4550803.
  2. ↑ Enzyme 2.7.1.89 at KEGG Pathway Database.