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Plasmepsin

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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)'''.
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*'''Proplasmepsin II''' exhibits a large shift between its domains which renders the protease inactive.
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*'''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

Template:STRUCTURE 3fns

Contents

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

References

  1. ↑ 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
  2. ↑ 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:http://dx.doi.org/10.1021/jm5014133

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Michal Harel, Alexander Berchansky, Joel L. Sussman, Jaime Prilusky

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