Four plasmepsins are active in the Plasmodium falciparum food vacuole, including a protease with an active-site histidine

Ritu Banerjee, Jun Liu, Wandy Beatty, Lorraine Pelosof, Michael Klemba, Daniel E. Goldberg

Research output: Contribution to journalArticlepeer-review

350 Scopus citations

Abstract

Hemoglobin degradation is a metabolic process that is central to the growth and maturation of the malaria parasite Plasmodium falciparum. Two aspartic proteases that initiate degradation, plasmepsins (PMs) I and II, have been identified and extensively characterized. Eight additional PM genes are present in the P. falciparum genome. To better understand the enzymology of hemoglobin degradation, it is necessary to determine which of these genes are expressed when hemoglobin degradation is occurring, which encode active enzymes, and which gene products are found in the food vacuole where catabolism takes place. Our genome-wide analysis reveals that PM I, II, and IV and histoaspartic protease encode hemoglobin-degrading food vacuole proteases. Despite having a histidine in place of one of the catalytic aspartic acids conserved in other aspartic proteases, histo-aspartic protease is an active hydrolase.

Original languageEnglish (US)
Pages (from-to)990-995
Number of pages6
JournalProceedings of the National Academy of Sciences of the United States of America
Volume99
Issue number2
DOIs
StatePublished - Jan 22 2002

ASJC Scopus subject areas

  • General

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