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Distal Substrate Interactions Enhance Plasmepsin Activity
2004
Journal of Biological Chemistry
Plasmepsin II (PM II) is an aspartic protease active in hemoglobin (Hb) degradation in the protozoan parasite Plasmodium falciparum. A fluorescence-quenched octapeptide substrate based on the initial hemoglobin cleavage site is recognized well by PM II. C-terminal extension of this peptide has little effect, but N-terminal extension results in higher maximal velocity and dramatic concentration-dependent substrate inhibition. This inhibition, but not the rate stimulation, depends on the presence
doi:10.1074/jbc.m412086200
pmid:15574427
fatcat:ruvbyw6afnadla5ynmqv42radu