Plasmepsins are a class of at least 10 enzymes (EC 3.4.23.38 and EC 3.4.23.39) produced by the Plasmodium falciparum parasite. There are ten different isoforms of these proteins and ten genes coding them respectively in Plasmodium (Plm I, II, III, IV, V, VI, VII, IX, X and HAP). It has been suggested that the plasmepsin family is smaller in other human Plasmodium species. Expression of Plm I, II, IV, V, IX, X and HAP occurs in the erythrocytic cycle, and expression of Plm VI, VII, VIII, occurs in the exoerythrocytic cycle. Through their haemoglobin-degrading activity, they are an important cause of symptoms in malaria sufferers. Consequently, this family of enzymes is a potential target for antimalarial drugs.
There are four types of plasmepsins, closely related but varying in the specificity of cleavage site. Plasmepsins I and II cleave hemoglobin between residues Phenylalanine 33 and Leucine 34 of α-globin subunit.
The name plasmepsin may come from Plasmodium (the organism) and pepsin (a common aspartic acid protease with similar molecular structure).
The closest (non-pathogenic) enzymatic equivalent in humans is the beta-secretase enzyme.
Referencesedit
^Silva AM, Lee AY, Gulnik SV, Maier P, Collins J, Bhat TN, Collins PJ, Cachau RE, Luker KE, Gluzman IY, Francis SE, Oksman A, Goldberg DE, Erickson JW (September 1996). "Structure and inhibition of plasmepsin II, a hemoglobin-degrading enzyme from Plasmodium falciparum". Proc. Natl. Acad. Sci. U.S.A. 93 (19): 10034–9. Bibcode:1996PNAS...9310034S. doi:10.1073/pnas.93.19.10034. PMC38331. PMID 8816746.
Further readingedit
Dame JB, Reddy GR, Yowell CA, Dunn BM, Kay J, Berry C (1994). "Sequence, expression and modeled structure of an aspartic proteinase from the human malaria parasite Plasmodium falciparum". Mol. Biochem. Parasitol. 64 (2): 177–90. doi:10.1016/0166-6851(94)90024-8. PMID 7935597.
Bernstein NK, Cherney MM, Loetscher H, Ridley RG, James MN (1999). "Crystal structure of the novel aspartic proteinase zymogen proplasmepsin II from plasmodium falciparum". Nat. Struct. Biol. 6 (1): 32–7. doi:10.1038/4905. PMID 9886289. S2CID 2326003.
Karubiu W, Bhakat S, Soliman ME (2015). "Flap Dynamics of Plasmepsin Proteases: Proposed Parameters and Molecular Dynamics Insight". Mol. Biosyst. 11 (4): 1061–1066. doi:10.1039/C4MB00631C. PMID 25630418.
External linksedit
The MEROPS online database for peptidases and their inhibitors: Plasmepsin I A01.022, Plasmepsin II A01.023
plasmepsin, this, article, needs, additional, citations, verification, please, help, improve, this, article, adding, citations, reliable, sources, unsourced, material, challenged, removed, find, sources, news, newspapers, books, scholar, jstor, january, 2024, . This article needs additional citations for verification Please help improve this article by adding citations to reliable sources Unsourced material may be challenged and removed Find sources Plasmepsin news newspapers books scholar JSTOR January 2024 Learn how and when to remove this message Plasmepsins are a class of at least 10 enzymes EC 3 4 23 38 and EC 3 4 23 39 produced by the Plasmodium falciparum parasite There are ten different isoforms of these proteins and ten genes coding them respectively in Plasmodium Plm I II III IV V VI VII IX X and HAP It has been suggested that the plasmepsin family is smaller in other human Plasmodium species Expression of Plm I II IV V IX X and HAP occurs in the erythrocytic cycle and expression of Plm VI VII VIII occurs in the exoerythrocytic cycle Through their haemoglobin degrading activity they are an important cause of symptoms in malaria sufferers Consequently this family of enzymes is a potential target for antimalarial drugs Plasmepsin IIdentifiersEC no 3 4 23 38CAS no 180189 87 1DatabasesIntEnzIntEnz viewBRENDABRENDA entryExPASyNiceZyme viewKEGGKEGG entryMetaCycmetabolic pathwayPRIAMprofilePDB structuresRCSB PDB PDBe PDBsumSearchPMCarticlesPubMedarticlesNCBIproteins Plasmepsin IIPlasmepsin II complexed withinhibitor pepstatin A PDB 1SME 1 IdentifiersEC no 3 4 23 39CAS no 159447 18 4DatabasesIntEnzIntEnz viewBRENDABRENDA entryExPASyNiceZyme viewKEGGKEGG entryMetaCycmetabolic pathwayPRIAMprofilePDB structuresRCSB PDB PDBe PDBsumSearchPMCarticlesPubMedarticlesNCBIproteins Plasmepsins are aspartic acid proteases meaning their active site contains two aspartic acid residues These two aspartic acid residue act respectively as proton donor and proton acceptor catalysing the hydrolysis of peptide bond in proteins There are four types of plasmepsins closely related but varying in the specificity of cleavage site Plasmepsins I and II cleave hemoglobin between residues Phenylalanine 33 and Leucine 34 of a globin subunit The name plasmepsin may come from Plasmodium the organism and pepsin a common aspartic acid protease with similar molecular structure The closest non pathogenic enzymatic equivalent in humans is the beta secretase enzyme References edit Silva AM Lee AY Gulnik SV Maier P Collins J Bhat TN Collins PJ Cachau RE Luker KE Gluzman IY Francis SE Oksman A Goldberg DE Erickson JW September 1996 Structure and inhibition of plasmepsin II a hemoglobin degrading enzyme from Plasmodium falciparum Proc Natl Acad Sci U S A 93 19 10034 9 Bibcode 1996PNAS 9310034S doi 10 1073 pnas 93 19 10034 PMC 38331 PMID 8816746 Further reading editDame JB Reddy GR Yowell CA Dunn BM Kay J Berry C 1994 Sequence expression and modeled structure of an aspartic proteinase from the human malaria parasite Plasmodium falciparum Mol Biochem Parasitol 64 2 177 90 doi 10 1016 0166 6851 94 90024 8 PMID 7935597 Bernstein NK Cherney MM Loetscher H Ridley RG James MN 1999 Crystal structure of the novel aspartic proteinase zymogen proplasmepsin II from plasmodium falciparum Nat Struct Biol 6 1 32 7 doi 10 1038 4905 PMID 9886289 S2CID 2326003 Karubiu W Bhakat S Soliman ME 2015 Flap Dynamics of Plasmepsin Proteases Proposed Parameters and Molecular Dynamics Insight Mol Biosyst 11 4 1061 1066 doi 10 1039 C4MB00631C PMID 25630418 External links editThe MEROPS online database for peptidases and their inhibitors Plasmepsin I A01 022 Plasmepsin II A01 023 plasmepsin at the U S National Library of Medicine Medical Subject Headings MeSH Retrieved from https en wikipedia org w index php title Plasmepsin amp oldid 1193437808, wikipedia, wiki, book, books, library,
