Collect. Czech. Chem. Commun. 1983, 48, 327-335

Interactions of 2-furylethylenes with thiol enzymes

Ernest Šturdík, Ľudovít Drobnica and Štefan Baláž

Department of Microbiology and Biochemistry, Slovak Institute of Technology, 812 37 Bratislava


Furylethylenes are inhibitors of glyceraldehyde 3-phosphate dehydrogenase (GAPDH; EC, glucose 6-phosphate dehydrogenase (EC, glutathione reductase (GR; EC, and, in part, also malate dehydrogenase (EC These four enzymes served as model thiolproteins employing the SH groups of the embodied cysteine for catalytic activity. The inhibition degree of the afore-mentioned enzymes is proportional to the reactivity of furylethylenes towards thiols. The inhibition of GAPDH and GR with 1-(5-nitro-2-furyl)-2-nitro-2-methoxycarbonylethylene (I) was characterized by inhibition constants Ki and also, its type was estimated. A direct chemical modification of SH groups of cysteine residues was found in GAPDH, a fact that could be closely connected with the inactivation of the enzyme.