Novel ways to prevent proteolysis - prophytepsin and proplasmepsin II.
The recently determined crystal structures of two aspartic proteinase zymogens, prophytepsin from barley and proplasmepsin II from the malarial parasite Plasmodium falciparum, have provided new insights into zymogen inactivation. Prophytepsin shows a variation of the mechanism of inhibition used by the well-known gastric aspartic proteinase zymogens, whereas proplasmepsin II uses a completely new mode of inactivation.
Bernstein
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Department of Biochemistry, Medical Research Council Group in Protein Structure and Function, University of Alberta, Edmonton, T6G 2H7, Canada.
James
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MN
D016282:Aspartic Acid Endopeptidases / Q000737:chemistry / Q000378:metabolism*; D002403:Cathepsins / Q000737:chemistry / Q000378:metabolism*; D004789:Enzyme Activation; D004791:Enzyme Inhibitors / Q000494:pharmacology; D004792:Enzyme Precursors / Q000037:antagonists & inhibitors / Q000737:chemistry / Q000378:metabolism*; D006868:Hydrolysis; D008958:Models, Molecular; D011487:Protein Conformation; D013270:Stomach / Q000201:enzymology
D004791:Enzyme Inhibitors; D004792:Enzyme Precursors; D002403:Cathepsins; D016282:Aspartic Acid Endopeptidases; C116755:proplasmepsin II; C109797:phytepsin