Prodomain Processing of Recombinant Plasmepsin II and IV, the Aspartic Proteases of Plasmodium falciparum, Is Auto- and Trans-Catalytic

• Published in: Journal of biochemistry (Tokyo) Vol. 139; no. 2; pp. 189 - 195
• Main Authors: Kim, Yong Man, Lee, Mi Hyang, Piao, Tae Gwang, Lee, John Wha, Kim, Jong Ho, Lee, SungGa, Choi, Kyung Min, Jiang, Jing Hua, Kim, Tae Ue, Park, Hyun
• Format: Journal Article
• Language: English
• Published: England Oxford University Press 01.02.2006
• Subjects: active-site motif; ALLN; Animals; Aspartic Acid Endopeptidases - antagonists & inhibitors; Aspartic Acid Endopeptidases - genetics; Aspartic Acid Endopeptidases - metabolism; aspartic protease; Biotransformation - drug effects; calpain; Catalysis; food vacuole; Leupeptins - pharmacology; Mutation; N-acetyl-l-leucyl-l-leucyl-norleucinal; Pepstatins - pharmacology; plasmepsin; Plasmodium falciparum; Plasmodium falciparum - enzymology; Plasmodium falciparum - genetics; Protein Structure, Tertiary; Protozoan Proteins; Recombinant Fusion Proteins - genetics; Recombinant Fusion Proteins - metabolism; SDS; sodium dodecyl sulfate

Prodomain processing of the four food vacuole plasmepsins (PMs), the malarial aspartic proteases, is prerequisite for their activity on hemoglobin degradation of the parasite Plasmodium falciparum. Although previous studies have suggested the involvement of a calpain-like PM convertase in the proces...