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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.[1]

References

  1. Transformation of leukotriene D4 catalyzed by lysosomal cathepsin H of rat liver. Yokota, K., Shono, F., Yamamoto, S., Kominami, E., Katunuma, N. J. Biochem. (1983) [Pubmed]
 
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