3.4.23.B14: plasmepsin IV

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For detailed information about plasmepsin IV, go to the full flat file.

Reaction

cleavage of hemoglobin. In the S3 and S2 subsites, the plasmepsin 4 orthologs all prefer hydrophobic amino acid residues, Phe or Ile, but reject charged residues such as Lys or Asp. In S2' and S3' subsites these plasmepsins tolerate both hydrophobic and hydrophilic residues =

Synonyms

A01.059, PfPM4, PgPM4, plasmepsin 4, Plm IV, PM IV, PM-IV, PM4, PMIV, PmPM4, PoPM4, pPM IV, proplasmepsin IV, PSM4, PvPM4

ECTree

     3 Hydrolases

         3.4 Acting on peptide bonds (peptidases)

             3.4.23 Aspartic endopeptidases

                3.4.23.B14 plasmepsin IV

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Results	in table
4	AA Sequence
6	Application
1	CAS Registry Number
9	Cloned(Commentary)
5	Crystallization (Commentary)
3	General Information
65	IC50 Value
298	Inhibitors
2	kcat/KM [mM/s]
154	Ki Value [mM]
90	KM Value [mM]
21	Localization
2	Molecular Weight [Da]
7	Natural Substrates/ Products (Substrates)
34	Organism
4	pH Optimum
1	pH Range
1	pH Stability
4	Posttranslational Modification
1	Protein Variants
12	Purification (Commentary)
3	Reaction
1	Reaction Type
34	Reference
3	Renatured (Commentary)
3	Source Tissue
108	Substrates and Products (Substrate)
4	Subunits
45	Synonyms
2	Temperature Optimum [°C]
1	Temperature Range [°C]
2	Temperature Stability [°C]
90	Turnover Number [1/s]

Crystallization

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Crystallization on EC 3.4.23.B14 - plasmepsin IV

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CRYSTALLIZATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

hanging-drop vapor-diffusion method, crystals of PmPM4 in complex with the small-molecule inhibitor AG1776. The crystals are orthorhombic, with space group P2(1)2(1)2 and unit-cell parameters a = 95.88 A, b = 112.58 A, c = 90.40 A, two molecules per asymmetric unit

Plasmodium falciparum

-

667068

truncated proplasmepsin IV, sitting drop vapor diffusion method, using 100 mM sodium citrate pH 4.7, 25% (w/v) PEG 3350, 200 mM ammonium acetate

Plasmodium falciparum

Q8IM16

752400

hanging-drop vapor-diffusion method, crystal structure of plasmepsin 4 bound to the allophenylnorstatine-based compound KNI-764 at 3.3 A resolution. The PmPM4–inhibitor complex crystallized in the ortho-rhombic space group P2(1)2(1)2, with unit-cell parameters a = 95.9 A, b = 112.6 A, c = 90.4 A, with two molecules in the asymmetric unit

Plasmodium malariae

-

667064

pKa calculations for PM IV complexed with the inhibitor KNI-764. Residue Asp214 is protonated, while residue Asp34 is deprotonated. In the colmplex, the hydroxyl group interacts with the OD2 oxygen atom of Asp34 through a hydrogen bond. The hydroxyl group also presents a hydrogen bond interaction with acid aspartic protonated Asp214. The amino groups of Gly78 and Ser79 residues interact with KNI-764 forming hydrogen bonds at 2.02 and 2.20 A. The hydroxyl group of Thr217 forms hydrogen bonds with the inhibitor at 2.06 A

Plasmodium malariae

O60990

717492

analysis of 3D model of PM4 shows a typical aspartic protease structure with bi-lobed, compact and distinct peptide binding cleft

Plasmodium vivax

D4P4R3

717657