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Literature summary for 3.4.23.39 extracted from

  • Tyas, L.; Moon, R.P.; Loetscher, H.; Dunn, B.M.; Kay, J.; Ridley, R.G.; Berry, C.
    Plasmepsins I and II from the malarial parasite Plasmodium falciparum (1998), Adv. Exp. Med. Biol., 436, 407-411.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Plasmodium falciparum

Inhibitors

Inhibitors Comment Organism Structure
N'1-[(E)-(2,3-dihydroxyphenyl)methylidene]-N'3-[(Z)-(2,3-dihydroxyphenyl)methylidene]benzene-1,3-dicarbohydrazide
-
Plasmodium falciparum
Ro40-4388
-
Plasmodium falciparum
Ro40-5576
-
Plasmodium falciparum

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.006
-
Lys-Pro-Ile-Val-Phe-Phe(NO2)-Arg-Leu pH 4.7, 37°C Plasmodium falciparum
0.02
-
Leu-Glu-Arg-Val-Phe-Phe(NO2)-Ser-Phe pH 4.4, 37°C Plasmodium falciparum
0.025
-
Leu-Glu-Arg-Ile-Phe-Phe(NO2)-Ser-Phe pH 4.4 Plasmodium falciparum
0.06
-
Ala-Leu-Glu-Arg-Thr-Phe-Phe(NO2)-Ser-Phe-Pro-Thr pH 4.7, 37°C Plasmodium falciparum

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
Hemoglobin + H2O Plasmodium falciparum during the infection of erythrocytes by the human malaria parasite Plasmodium falciparum, up to 80% of the host cell hemoglobin is degraded to provide amino acids for parasite nutrition. Plasmepsin I and plasmepsin II are believed to be responsible for initiating the catabolic process ?
-
?

Organism

Organism UniProt Comment Textmining
Plasmodium falciparum
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Ala-Leu-Glu-Arg-Thr-Phe-Phe(NO2)-Ser-Phe-Pro-Thr + H2O
-
Plasmodium falciparum Ala-Leu-Glu-Arg-Thr-Phe + Phe(NO2)-Ser-Phe-Pro-Thr
-
?
Hemoglobin + H2O during the infection of erythrocytes by the human malaria parasite Plasmodium falciparum, up to 80% of the host cell hemoglobin is degraded to provide amino acids for parasite nutrition. Plasmepsin I and plasmepsin II are believed to be responsible for initiating the catabolic process Plasmodium falciparum ?
-
?
Leu-Glu-Arg-Ile-Phe-Phe(NO2)-Ser-Phe + H2O
-
Plasmodium falciparum Leu-Glu-Arg-Ile-Phe + Phe(NO2)-Ser-Phe
-
?
Leu-Glu-Arg-Val-Phe-Phe(NO2)-Ser-Phe + H2O
-
Plasmodium falciparum Leu-Glu-Arg-Val-Phe + Phe(NO2)-Ser-Phe
-
?
Lys-Pro-Ile-Lys-Phe-Phe(NO2)-Arg-Leu + H2O
-
Plasmodium falciparum Lys-Pro-Ile-Lys-Phe + Phe(NO2)-Arg-Leu
-
?
Lys-Pro-Ile-Val-Phe-Phe(NO2)-Arg-Leu + H2O
-
Plasmodium falciparum Lys-Pro-Ile-Val-Phe + Phe(NO2)-Arg-Leu
-
?
additional information the enzyme has a preference for a small hydrophobic residue in the P3 position of the substrate. The S2 and S3 subsites of plasmepsin II are hydrophobic in nature and on this basis the hemoglobin-related substrate, with Arg and Thr in the P3 and P2 positions respectively may not represent the optimal substrate Plasmodium falciparum ?
-
?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.04
-
Lys-Pro-Ile-Lys-Phe-Phe(NO2)-Arg-Leu pH 4.7, 37°C Plasmodium falciparum
3.6
-
Lys-Pro-Ile-Val-Phe-Phe(NO2)-Arg-Leu pH 4.7, 37°C Plasmodium falciparum
6
-
Ala-Leu-Glu-Arg-Thr-Phe-Phe(NO2)-Ser-Phe-Pro-Thr pH 4.7, 37°C Plasmodium falciparum
9
-
Leu-Glu-Arg-Val-Phe-Phe(NO2)-Ser-Phe pH 4.4, 37°C Plasmodium falciparum
15
-
Leu-Glu-Arg-Ile-Phe-Phe(NO2)-Ser-Phe pH 4.4 Plasmodium falciparum

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
5
-
-
Plasmodium falciparum

pH Range

pH Minimum pH Maximum Comment Organism
3.5 6.5 active over the range Plasmodium falciparum

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.00025
-
Ro40-5576 pH 4.4, 37°C Plasmodium falciparum
0.0005
-
Ro40-4388 pH 4.4, 37°C Plasmodium falciparum
0.004
-
N'1-[(E)-(2,3-dihydroxyphenyl)methylidene]-N'3-[(Z)-(2,3-dihydroxyphenyl)methylidene]benzene-1,3-dicarbohydrazide pH 4.4, 37°C Plasmodium falciparum