4645-77-6Relevant academic research and scientific papers
Hydroxamate inhibitor profiling of both zn2+- and ni2+-activated glyoxalase i metalloenzymes having diverse quaternary structures
Suttisansanee, Uthaiwan,Honek, John F.
, p. 843 - 852 (2017/08/07)
Background: The glyoxalase enzyme system is a critical component in the detoxification of cellular metabolically generated alpha-ketoaldehydes, such as methylglyoxal. Inhibitors of these enzymes have been shown to have potential in the development of anti
Glutathione N-hydroxycarbamoyl thioesters and method of inhibiting neoplastic growth
-
, (2008/06/13)
A compound of the formula STR1 with R being hydrogen, alkyl, cycloalkyl or aryl, which may be substituted with halogen or alkyl, and R' and Ra being hydroxyl, or --O-alkyl, pharmaceutically acceptable salts thereof; or mixtures thereof. An anti
S-(N-Aryl-N-hydroxycarbamoyl)glutathione derivatives are tight-binding inhibitors of glyoxalase I and slow substrates for glyoxalase II
Murthy,Bakeris,Kavarana,Hamilton,Lan,Creighton
, p. 2161 - 2166 (2007/10/02)
S-(N-Aryl-N-hydroxycarbamoyl)glutathione derivatives are powerful competitive inhibitors of the anticancer target enzyme glyoxalase I. Indeed, the N-p-bromophenyl derivative is the strongest inhibitor of the enzyme from human erythrocytes yet reported (K(i) = 1.4 x 10-8 M). Structure-activity correlations indicate that the high affinities of the derivatives for both human and yeast glyoxalase I are due to the fact that the derivatives are hydrophobic analogs of the enediol(ate) intermediate associated with the glyoxalase I reaction. The derivatives also proved to be slow substrates for the thioester hydrolase glyoxalase II (bovine liver). Compounds of this type are of interest as potential tumor-selective anticancer agents, based on the abnormally low levels of glyoxalase II activity in some types of cancer cells.
