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

被引：59

作者：

Wyatt, DM ^{[1
]}

Berry, C ^{[1
]}

机构：

[1] Cardiff Univ, Cardiff Business Sch, Cardiff CF1 3US, S Glam, Wales

来源：

FEBS LETTERS | 2002年 / 513卷 / 2-3期

基金：

英国生物技术与生命科学研究理事会;

关键词：

malaria; aspartic proteinase; new plasmepsin; Plasmodium;

D O I：

10.1016/S0014-5793(02)02241-X

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

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. (C) 2002 Federation of European Biochemical Societies. Published by Elsevier Science B.V. All rights reserved.

引用

页码：159 / 162

页数：4

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