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PMID:11904142
| Citation |
Wyatt, DM and Berry, C (2002) Activity and inhibition of plasmepsin IV, a new aspartic proteinase from the malaria parasite, Plasmodium falciparum. FEBS Lett. 513:159-62 |
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| Abstract |
A new aspartic proteinase from the human malaria parasite Plasmodium falciparum is able to hydrolyse human haemoglobin at a site known to be the essential primary cleavage site in the haemoglobin degradation pathway. Thus, plasmepsin IV may play a crucial role in this critical process which yields nutrients for parasite growth. Furthermore, synthetic inhibitors known to inhibit parasite growth in red cells in culture are able to inhibit the activity of this enzyme in vitro. As a result, plasmepsin IV appears to be a potential target for the development of new antiparasitic drugs. |
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| Keywords |
Amino Acid Sequence; Animals; Aspartic Acid Endopeptidases/antagonists & inhibitors; Aspartic Acid Endopeptidases/metabolism; Molecular Sequence Data; Plasmodium falciparum/enzymology; Recombinant Proteins/antagonists & inhibitors; Recombinant Proteins/metabolism |
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Significance
Annotations
| Gene product | Qualifier | GO Term | Evidence Code | with/from | Aspect | Extension | Notes | Status |
|---|---|---|---|---|---|---|---|---|
| GO:0042540: hemoglobin catabolic process |
ECO:0000314: |
P |
Figure 1 shows that incubation with plasmepsin IV causes the 17kDa hemoglobin protein to be degraded into an intermediate 14kDa protein. |
complete | ||||
See also
References
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