39180-69-3Relevant academic research and scientific papers
Deglycase-activity oriented screening to identify DJ-1 inhibitors
David, Yael,Finkin-Groner, Efrat,Fukase, Yoshiyuki,Huggins, David J.,Maksimovic, Igor,Michino, Mayako,Myers, Robert W.,Sun, Shan,Zheng, Qingfei
supporting information, p. 1232 - 1238 (2021/09/28)
The oncoprotein and Parkinson's disease-associated enzyme DJ-1/PARK7 has emerged as a promiscuous deglycase that can remove methylglyoxal-induced glycation adducts from both proteins and nucleotides. However, dissecting its structural and enzymatic functions remains a challenge due to the lack of potent, specific, and pharmacokinetically stable inhibitors targeting its catalytic site (including Cys106). To evaluate potential drug-like leads against DJ-1, we leveraged its deglycase activity in an enzyme-coupled, fluorescence lactate-detection assay based on the recent understanding of its deglycation mechanism. In addition, we developed assays to directly evaluate DJ-1's esterase activity using both colorimetric and fluorescent substrates. The resulting optimized assay was used to evaluate a library of potential reversible and irreversible DJ-1 inhibitors. The deglycase activity-oriented screening strategy described herein establishes a new platform for the discovery of potential anti-cancer drugs.
Structural Influences on the Isomerization of 4-Benzyl- and 4-Allyl-1,2-naphthoquinones to Quinonemethides and their Stereochemistry
Takuwa, Akio,Iwamoto, Hidetoshi,Soga, Osamu,Maruyama, Kazuhiro
, p. 1627 - 1632 (2007/10/02)
The isomerization of 4-benzyl-1,2-naphthoquinones and 4-allyl-1,2-naphthoquinones to quinonemethides has been studied.The steric interaction and extra ? conjugation in the quinonemethide, and acidity of methylene protons of the quinone, are controlling fa
