Transformation of leukotriene D4 catalyzed by lysosomal cathepsin H of rat liver.
Among several intracellular protease tested, cathepsin H transformed leukotriene D4 to E4 with a release of glycine in a stoichiometric quantity. Under the optimal conditions the rate of leukotriene D4 transformation by cathepsin H was about 3% of the hydrolysis rate of alpha-N-benzoyl-DL-arginine-2-naphthylamide which is commonly utilized as a very efficient substrate to test the peptidase activity of the enzyme. Leukotriene C4 was not transformed to leukotriene D4 by cathepsin H. Neither cathepsin B nor C was active with leukotrienes C4 and D4.
D000818:Animals; D001711:Biotransformation; D002401:Cathepsin B; D056655:Cathepsin H; D002403:Cathepsins / Q000378:metabolism*; D003546:Cysteine Endopeptidases; D007700:Kinetics; D008099:Liver / Q000201:enzymology*; D008247:Lysosomes / Q000201:enzymology*; D051381:Rats; D013189:SRS-A / Q000378:metabolism*
D013189:SRS-A; D002403:Cathepsins; D003546:Cysteine Endopeptidases; D002401:Cathepsin B; D056655:Cathepsin H; C534128:Ctsh protein, rat