13038-85-2Relevant articles and documents
Structure activity relationships of human galactokinase inhibitors
Liu, Li,Tang, Manshu,Walsh, Martin J.,Brimacombe, Kyle R.,Pragani, Rajan,Tanega, Cordelle,Rohde, Jason M.,Baker, Heather L.,Fernandez, Elizabeth,Blackman, Burchelle,Bougie, James M.,Leister, William H.,Auld, Douglas S.,Shen, Min,Lai, Kent,Boxer, Matthew B.
, p. 721 - 727 (2015/01/30)
Classic Galactosemia is a rare inborn error of metabolism that is caused by deficiency of galactose-1-phosphate uridyltransferase (GALT), an enzyme within the Leloir pathway that is responsible for the conversion of galactose-1-phosphate (gal-1-p) and UDP-glucose to glucose-1-phosphate and UDP-galactose. This deficiency results in elevated intracellular concentrations of its substrate, gal-1-p, and this increased concentration is believed to be the major pathogenic mechanism in Classic Galactosemia. Galactokinase (GALK) is an upstream enzyme of GALT in the Leloir pathway and is responsible for conversion of galactose and ATP to gal-1-p and ADP. Therefore, it was hypothesized that the identification of a small-molecule inhibitor of human GALK would act to prevent the accumulation of gal-1-p and offer a novel entry therapy for this disorder. Herein we describe a quantitative high-throughput screening campaign that identified a single chemotype that was optimized and validated as a GALK inhibitor.
STRUCTURE AND BASICITY OF 2-GUANIDINOBENZIMIDAZOLES
Acerete, Carmen,Catalan, Javier,Fabero, Fernando,Sanchez-Cabezudo, Marta,Claramunt, Rosa Maria,Elguero, Jose
, p. 1581 - 1586 (2007/10/02)
A theoretical and experimental study of the basicity of three 2-guanidinobenzimidazoles has been carried out.The most abundant tautomer, the structure of the protonated molecule, and the reason of the relatively low pKa are disscused.In addition, a careful 1H and 13C nmr study provides information about the influence of intramolecular hydrogen bonds on annular tautomeric rates.
