Cilastatin-sensitive dehydropeptidase I enzymes from three sources all catalyze carbapenem hydrolysis and conversion of leukotriene D4 to leukotriene E4.
The dipeptidase, dehydropeptidase I (EC 3.4.13.11), was purified to homogeneity from rat lung, rat kidney, and hog kidney. Analysis of physical parameters (subunit molecular weights, Km values for glycyldehydrophenylalanine, Ki values for dehydropeptidase I inhibitors, and immunoreactivity) showed the rat dipeptidases to be similar to each other but different from the hog dipeptidase. However, all three enzymes hydrolyzed imipenem and converted leukotriene D4 to leukotriene E4, and these activities were inhibited by cilastatin.
D000818:Animals; D002384:Catalysis; D002851:Chromatography, High Pressure Liquid; D015377:Cilastatin; D003521:Cyclopropanes / Q000494:pharmacology*; D004150:Dipeptidases / Q000037:antagonists & inhibitors / Q000302:isolation & purification / Q000378:metabolism*; D004591:Electrophoresis, Polyacrylamide Gel; D006868:Hydrolysis; D015378:Imipenem; D007668:Kidney / Q000201:enzymology; D007700:Kinetics; D017999:Leukotriene E4; D008168:Lung / Q000201:enzymology*; D051381:Rats; D013189:SRS-A / Q000031:analogs & derivatives* / Q000096:biosynthesis / Q000378:metabolism*; D013552:Swine; D013845:Thienamycins / Q000378:metabolism*
D003521:Cyclopropanes; D013189:SRS-A; D013845:Thienamycins; D015377:Cilastatin; D015378:Imipenem; D017999:Leukotriene E4; D004150:Dipeptidases; C038937:dipeptidase