Plasmepsin: Difference between revisions
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[[Plasmepsin]] (Plm) is a hemoglobin-degrading enzyme produced by the plasmodium parasite. It is an aspartic acid protease having 2 aspartic acid residues in the active site. Ten Plm isoforms are known which are named Plm I, II, etc and '''Histo-Aspartic Protease (HAP)'''. | [[Plasmepsin]] (Plm) is a hemoglobin-degrading enzyme produced by the plasmodium parasite. It is an aspartic acid protease having 2 aspartic acid residues in the active site. Ten Plm isoforms are known which are named Plm I, II, etc and '''Histo-Aspartic Protease (HAP)'''. | ||
*'''Proplasmepsin II''' exhibits a large shift between its domains which renders the protease inactive. | *'''Proplasmepsin II''' exhibits a large shift between its domains which renders the protease inactive<ref>PMID:9886289</ref>. | ||
==Relevance == | ==Relevance == | ||
Revision as of 07:54, 4 July 2016
Function
Plasmepsin (Plm) is a hemoglobin-degrading enzyme produced by the plasmodium parasite. It is an aspartic acid protease having 2 aspartic acid residues in the active site. Ten Plm isoforms are known which are named Plm I, II, etc and Histo-Aspartic Protease (HAP).
- Proplasmepsin II exhibits a large shift between its domains which renders the protease inactive[1].
Relevance
Plm is a potential target for anti-malaria drugs[2].
3D structures of plasmepsin
Updated on 04-July-2016
- ↑ Bernstein NK, Cherney MM, Loetscher H, Ridley RG, James MN. Crystal structure of the novel aspartic proteinase zymogen proplasmepsin II from plasmodium falciparum. Nat Struct Biol. 1999 Jan;6(1):32-7. PMID:9886289 doi:10.1038/4905
- ↑ Huizing AP, Mondal M, Hirsch AK. Fighting malaria: structure-guided discovery of nonpeptidomimetic plasmepsin inhibitors. J Med Chem. 2015 Jul 9;58(13):5151-63. doi: 10.1021/jm5014133. Epub 2015 Mar 17. PMID:25719272 doi:https://dx.doi.org/10.1021/jm5014133
References
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Alexander Berchansky, Michal Harel, Joel L. Sussman, Jaime Prilusky
