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{{Short description|Group of Plasmodium enzymes}}
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{{enzyme
{{more citations needed|date=January 2024}}
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| Name = Plasmepsin I
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{{infobox enzyme
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| EC_number = 3.4.23.38
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| Name = Plasmepsin I
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| EC_number = 3.4.23.38
| CAS_number = 180189-87-1
| CAS_number = 180189-87-1
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| GO_code =
| IUBMB_EC_number = 3/4/23/38
| GO_code =
| image =
| image =
| width =
| width =
| caption =
| caption =
}}
}}
{{enzyme
{{infobox enzyme
| Name = Plasmepsin II
| Name = Plasmepsin II
| EC_number = 3.4.23.39
| EC_number = 3.4.23.39
| CAS_number = 159447-18-4
| CAS_number = 159447-18-4
| GO_code =
| IUBMB_EC_number = 3/4/23/39
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| image = Plasmepsin.png
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| GO_code =
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| width =
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| image = Plasmepsin.png
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| caption = Plasmepsin II complexed with<br/>inhibitor [[pepstatin|pepstatin A]] ({{PDB|1SME}}).<ref name="pmid8816746">{{cite journal |vauthors=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 | title = Structure and inhibition of plasmepsin II, a hemoglobin-degrading enzyme from Plasmodium falciparum | journal = Proc. Natl. Acad. Sci. U.S.A. | volume = 93 | issue = 19 | pages = 10034–9 |date=September 1996 | pmid = 8816746 | pmc = 38331 | doi = 10.1073/pnas.93.19.10034| bibcode = 1996PNAS...9310034S | doi-access = free }}</ref>
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| width =
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| caption = Plasmepsin II complexed with<br/>inhibitor [[pepstatin|pepstatin A]].<ref name="pmid8816746">{{PDB|1SME}}; {{cite journal | author = 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 | title = Structure and inhibition of plasmepsin II, a hemoglobin-degrading enzyme from Plasmodium falciparum | journal = Proc. Natl. Acad. Sci. U.S.A. | volume = 93 | issue = 19 | pages = 10034–9 | year = 1996 | month = September | pmid = 8816746 | pmc = 38331 | doi = 10.1073/pnas.93.19.10034| url = | issn = }}</ref>
}}
}}
'''Plasmepsins''' are a class of at least 10 enzymes ({{EC number|3.4.23.38}} and {{EC number|3.4.23.39}}) produced by the [[plasmodium]] parasite. There are ten different isoforms of these proteins and ten genes coding them respectively in plasmodium falciparum (Plm I, II, III, IV, V, VI, VII, IX, X and HAP). It has been suggested that the plasmpesin family is smaller in other human plasmodium species. Expression of Plm I, II, IV, V, IX, X and HAP occurs in erythrocytic cycle, and expression of Plm VI, VII, VIII, occurs in 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.the aspartic protease of ''Plasmodium''species are known as Plasmepsins
'''Plasmepsins''' are a class of at least 10 enzymes ({{EC number|3.4.23.38}} and {{EC number|3.4.23.39}}) produced by the ''[[Plasmodium|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.


Plasmepsins are [[aspartic acid]] [[proteases]], which means their [[active site]] contains two [[aspartic acid]] [[amino-acid|residue]]s. These two [[aspartic acid]] [[amino-acid|residue]] act respectively as proton donor and proton acceptor, catalysing the hydrolysis of [[peptide bond]] in [[proteins]].
Plasmepsins are [[aspartic acid]] [[proteases]], meaning their [[active site]] contains two [[aspartic acid]] [[amino-acid|residue]]s. These two [[aspartic acid]] [[amino-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 α-globin subunit.
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 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.
The closest (non-pathogenic) enzymatic equivalent in humans is the [[beta-secretase 1|beta-secretase]] enzyme.


== References ==
== References ==
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== Further reading ==
== Further reading ==
{{refbegin}}
{{refbegin}}
* {{cite journal |author=Dame JB, Reddy GR, Yowell CA, Dunn BM, Kay J, Berry C |title=Sequence, expression and modeled structure of an aspartic proteinase from the human malaria parasite Plasmodium falciparum |journal=Mol. Biochem. Parasitol. |volume=64 |issue=2 |pages=177–90 |year=1994 |pmid=7935597 |doi=10.1016/0166-6851(94)90024-8}}
* {{cite journal |vauthors=Dame JB, Reddy GR, Yowell CA, Dunn BM, Kay J, Berry C |title=Sequence, expression and modeled structure of an aspartic proteinase from the human malaria parasite Plasmodium falciparum |journal=Mol. Biochem. Parasitol. |volume=64 |issue=2 |pages=177–90 |year=1994 |pmid=7935597 |doi=10.1016/0166-6851(94)90024-8}}
* {{cite journal |author=Bernstein NK, Cherney MM, Loetscher H, Ridley RG, James MN |title=Crystal structure of the novel aspartic proteinase zymogen proplasmepsin II from plasmodium falciparum |journal=Nat. Struct. Biol. |volume=6 |issue=1 |pages=32–7 |year=1999 |pmid=9886289 |doi=10.1038/4905}}
* {{cite journal |vauthors=Bernstein NK, Cherney MM, Loetscher H, Ridley RG, James MN |title=Crystal structure of the novel aspartic proteinase zymogen proplasmepsin II from plasmodium falciparum |journal=Nat. Struct. Biol. |volume=6 |issue=1 |pages=32–7 |year=1999 |pmid=9886289 |doi=10.1038/4905|s2cid=2326003 }}
* {{cite journal |vauthors=Karubiu W, Bhakat S, Soliman ME |title=Flap Dynamics of Plasmepsin Proteases: Proposed Parameters and Molecular Dynamics Insight |journal=Mol. Biosyst. |year=2015 |volume=11 |issue=4 |pages=1061–1066 |doi=10.1039/C4MB00631C |pmid=25630418 }}
{{refend}}
{{refend}}


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{{Aspartic acid proteases}}
{{Aspartic acid proteases}}


[[Category:Plasmodium]]
[[Category:Plasmodium|*Plasmepsin]]

Latest revision as of 20:51, 3 January 2024

Plasmepsin I
Identifiers
EC no.3.4.23.38
CAS no.180189-87-1
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Search
PMCarticles
PubMedarticles
NCBIproteins
Plasmepsin II
Plasmepsin II complexed with
inhibitor pepstatin A (PDB: 1SME​).[1]
Identifiers
EC no.3.4.23.39
CAS no.159447-18-4
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Search
PMCarticles
PubMedarticles
NCBIproteins

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.

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 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.

References

[edit]
  1. ^ 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

[edit]
  • 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.
[edit]
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