6-Aza-UMP disodium is a competitive inhibitor of the OMP decarboxylase domain of UMP synthase ( UMP synthase ), with a K i value of 0.51 μM against OMP decarboxylase. 6-Aza-UMP disodium reduces the production of UMP and increases the abundance of OMP. 6-Aza-UMP disodium promotes the formation of toxic 6-aza-UTP, thereby exerting cytotoxicity against bacterial. 6-Aza-UMP disodium can be used in studies related to bacterial infections [1] [2].
In Vitro, 6-Aza-UMP (10-250 μM; 20 min) disodium potently inhibits the activity of wild-type human UMPS in vitro, and a significant reduction in UMP production is observed at concentrations as low as 10 μM[1]. 6-Aza-UMP (0.02-2.0 mM; duration of the spectrophotometric absorbance recording) disodium serves as a substrate for UMP kinases from Bacillus subtilis and Escherichia coli[2].
References:
[1]. Cantor JR, et al. Physiologic Medium Rewires Cellular Metabolism and Reveals Uric Acid as an Endogenous Inhibitor of UMP Synthase. Cell. 2017 Apr 06;169(2):258-272.e17.
[2]. Gagyi C, et al. UMP kinase from the Gram-positive bacterium Bacillus subtilis is strongly dependent on GTP for optimal activity. European journal of biochemistry. 2003 Aug;270(15):3196-204.
[3]. Wu N, et al. Purification, crystallization and preliminary X-ray study of orotidine 5'-monophosphate decarboxylase. Acta crystallographica. Section D, Biological crystallography. 2000 Jul;56(Pt 7):912-4.
In Vitro, 6-Aza-UMP (10-250 μM; 20 min) disodium potently inhibits the activity of wild-type human UMPS in vitro, and a significant reduction in UMP production is observed at concentrations as low as 10 μM[1]. 6-Aza-UMP (0.02-2.0 mM; duration of the spectrophotometric absorbance recording) disodium serves as a substrate for UMP kinases from Bacillus subtilis and Escherichia coli[2].
References:
[1]. Cantor JR, et al. Physiologic Medium Rewires Cellular Metabolism and Reveals Uric Acid as an Endogenous Inhibitor of UMP Synthase. Cell. 2017 Apr 06;169(2):258-272.e17.
[2]. Gagyi C, et al. UMP kinase from the Gram-positive bacterium Bacillus subtilis is strongly dependent on GTP for optimal activity. European journal of biochemistry. 2003 Aug;270(15):3196-204.
[3]. Wu N, et al. Purification, crystallization and preliminary X-ray study of orotidine 5'-monophosphate decarboxylase. Acta crystallographica. Section D, Biological crystallography. 2000 Jul;56(Pt 7):912-4.