752984-71-7Relevant academic research and scientific papers
Structure-based design of potent small-molecule binders to the S-component of the ECF transporter for thiamine
Swier, Lotteke J.Y.M.,Monjas, Leticia,Guskov, Albert,De Voogd, Alrik R.,Erkens, Guus B.,Slotboom, Dirk J.,Hirsch, Anna K. H.
, p. 819 - 826 (2015)
Energy-coupling factor (ECF) transporters are membrane-protein complexes that mediate vitamin uptake in prokaryotes. They bind the substrate through the action of a specific integral membrane subunit (S-component) and power transport by hydrolysis of ATP
Inhibition of thiamin diphosphate dependent enzymes by 3-deazathiamin diphosphate.
Mann, Stephane,Perez Melero, Concepcion,Hawksley, Dan,Leeper, Finian J
, p. 1732 - 1741 (2007/10/03)
3-Deazathiamin diphosphate (deazaTPP) and a second thiamin diphosphate (TPP) analogue having a benzene ring in place of the thiazolium ring have been synthesised. These compounds are both extremely potent inhibitors of pyruvate decarboxylase from Zymomonas mobilis; binding is competitive with TPP and is essentially irreversible even though no covalent linkage is formed. DeazaTPP binds approximately seven-fold faster than TPP and at least 25,000-fold more tightly (K(i) less than 14 pM). DeazaTPP is also a potent inhibitor of the E1 subunit of alpha-ketoglutarate dehydrogenase from E. coli and binds more than 70-fold faster than TPP. In this case slow reversal of the inhibition could be observed and a K(i) value of about 5 nM was calculated (ca. 500-fold tighter binding than TPP).
