Activity and inhibition of plasmepsin IV, a new aspartic proteinase from the malaria parasite, Plasmodium falciparum

FEBS Letters

Wyatt, David M¹  Berry, Colin¹ 

[1] Cardiff School of Biosciences, Cardiff University, P.O. Box 911, Cardiff CF1 3US, Wales, UK

关键词: Malaria;    Aspartic proteinase;    New plasmepsin;    Plasmodium;    Nph;    para-nitrophenylalanine;    three letter amino acid code;    Z;    para-nitrophenylalanine;    single letter amino acid code;   

DOI  :  10.1016/S0014-5793(02)02241-X

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown