Inhibition by streptozotocin of the activity of succinyl-CoA synthetase in vitro and in vivo.
The activity of succinyl-CoA synthetase from mouse liver and kidney was inhibited by streptozotocin in vitro. Streptozotocin behaved essentially as a non-competitive inhibitor, and the following kinetic values were obtained (in the presence of 10 nM streptozotocin): apparent Km 1.7 mM, apparent Ki 10 nM, and kcat 440 nkat X kg-1. Compared with non-diabetic control mice, the succinyl-CoA synthetase activity was significantly decreased in the islets and kidneys of mice with early (1 h) and manifest (greater than or equal to 2 days) streptozotocin diabetes, whereas the activity in the liver was not significantly altered. Inhibited succinyl-CoA synthetase activity is believed to play a prominent role in the cellular effects of streptozotocin.
D000818:Animals; D003066:Coenzyme A Ligases / Q000037:antagonists & inhibitors*; D003921:Diabetes Mellitus, Experimental / Q000201:enzymology; D005260:Female; D066298:In Vitro Techniques; D007668:Kidney / Q000201:enzymology; D007700:Kinetics; D008099:Liver / Q000201:enzymology; D008297:Male; D051379:Mice; D008810:Mice, Inbred C57BL; D013311:Streptozocin / Q000494:pharmacology*; D013389:Succinate-CoA Ligases / Q000037:antagonists & inhibitors*
D013311:Streptozocin; D003066:Coenzyme A Ligases; D013389:Succinate-CoA Ligases