Characterization of the 30-kDa enzyme from red blood cells that cleaves ubiquitin-protein conjugates.
A 30-kDa enzyme from red blood cells responsible for the recycling of free Ubiquitin has been characterized. This enzyme was previously known to have a Ubiquitin-C-terminal hydrolase activity on adducts of Ubiquitin to small compounds. In this study it was shown that the 30-kDa enzyme contained Ubiquitin-C-terminal hydrolase activity toward biosynthetic precursors of Ub as well as isopeptidase activity toward Ubiquitin histone conjugates. Detailed inhibition experiments with Ubiquitin aldehyde, iodoacetamide, and heat inactivation showed that the enzyme isopeptidase activity was affected differently from its hydrolase activity.
Moskovitz
J
J
Unit of Biochemistry, Faculty of Medicine, Technion-Israel Institute of Technology, Haifa.
D000447:Aldehydes; D000818:Animals; D002417:Cattle; D004795:Enzyme Stability; D004912:Erythrocytes / Q000201:enzymology*; D006358:Hot Temperature; D006801:Humans; D006867:Hydrolases / Q000097:blood / Q000302:isolation & purification*; D006868:Hydrolysis; D007460:Iodoacetamide; D014452:Ubiquitins / Q000378:metabolism*
D000447:Aldehydes; D014452:Ubiquitins; D006867:Hydrolases; D007460:Iodoacetamide