A family of aspartic proteases called plasmepsins is important for hemoglobin degradation in intraerythrocytic Plasmodium parasites. Plasmepsin II (PM II) is the best studied member of this family. PM II and its close orthologs and paralogs form homodimers with extensive interfaces in all known crystal structures. This raised the question whether the homodimer is the functional subunit of plasmepsins in solution. We have used gel filtration chromatography, site-directed mutagenesis, and analytical ultracentrifugation to study the oligomeric status of PM II in solution. Our results reveal that PM II exists mainly as a monomer in solution and that the monomer is fully functional for catalysis. A hydrophobic loop at the PM II monomer surface, which would be buried in a PM II dimer, is shown to be essential for the hemoglobin degradation capability of PM II.
Hemoglobin-degrading plasmepsin II is active as a monomer. Publishing Authors By Initials
Hemoglobin-degrading plasmepsin II is active as a monomer. Journal Published:
PUBLICATION TYPE: Research Support, N.I.H., Extr
Journal: The Journal of biological chemistry
VOLUME: 281
Page Numbers: 38682-8
Journal Abbreviation: J. Biol. Chem.
ISSN: 0021-9258
DAY: 13
MONTH: 10
YEAR: 2006
Hemoglobin-degrading plasmepsin II is active as a monomer. Information
Number of References:
LANGUAGE: eng
NlmUniqueID: 2985121
Hemoglobin-degrading plasmepsin II is active as a monomer. Keywords Mesh Terms:
KEYWORDS: Mutagenesis
MESH TERMS: metabolism
Chemical & Substance for Abstract: Hemoglobin-degrading plasmepsin II is active as a monomer. Information
Substance Name: plasmepsin II
Registry Number: EC 3.4.23.39
Grant and Affiliation Information for Hemoglobin-degrading plasmepsin II is active as a monomer.
AFFILIATION: Departments of Molecular Microbiology and Medicine, Washington University School of Medicine, Howard Hughes Medical Institute, 660 S. Euclid Avenue, St. Louis, MO 63110, USA.
Country: United States
AGENCY: United States NIAID
GRANT: AI 47798
ACRONYM: AI
MEDLINETA: J Biol Chem
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