|
|
Article: Research results from D. Ragheb and co-authors update knowledge of falciparum malaria.
- Article from:
- Malaria Weekly (Atlanta, GA)
- Article date:
- November 9, 2009
CopyrightCOPYRIGHT 2009 NewsRX. This material is published under license from the publisher through the Gale Group, Farmington Hills, Michigan. All inquiries regarding rights should be directed to the Gale Group. (Hide copyright information)
|
"The metalloenzyme aminopeptidase P catalyzes the hydrolysis of amino acids from the amino termini of peptides with a prolyl residue in the second position. The human malaria parasite Plasmodium falciparum expresses a homolog of aminopeptidase P during its asexual intraerythrocytic cycle. P. falciparum aminopeptidase P (PfAPP) shares with mammalian cytosolic aminopeptidase P a three-domain, homodimeric organization and is most active with Mn(II) as the cofactor," scientists in the United States report (see also Falciparum Malaria).
"A distinguishing feature of PfAPP is a 120-amino acid amino-terminal extension that appears to be removed from the mature protein. ...
Related newspaper, magazine, and journal articles:
|