1355331-53-1Relevant articles and documents
Synthesis and evaluation of potential inhibitors of human and Escherichia coli histidine triad nucleotide binding proteins
Bardaweel, Sanaa K.,Ghosh, Brahma,Wagner, Carston R.
, p. 558 - 560 (2012)
Based on recent substrate specificity studies, a series of ribonucleotide based esters and carbamates were synthesized and screened as inhibitors of the phosphoramidases and acyl-AMP hydrolases, Escherichia coli Histidine Triad Nucleotide Binding Protein (ecHinT) and human Histidine Triad Nucleotide Binding Protein 1 (hHint1). Using our established phosphoramidase assay, Ki values were determined. All compounds exhibited non-competitive inhibition profiles. The carbamate based inhibitors were shown to successfully suppress the Hint1-associated phenotype in E. coli, suggesting that they are permeable intracellular inhibitors of ecHinT.