3.4.23.38: plasmepsin I
This is an abbreviated version!
For detailed information about plasmepsin I, go to the full flat file.
Word Map on EC 3.4.23.38
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3.4.23.38
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plasmepsins
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falciparum
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plasmodium
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malarial
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antimalarial
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cathepsin
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vacuole
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aspartyl
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proteinases
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hemoglobin-degrading
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intraerythrocytic
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autocatalytic
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proplasmepsins
- 3.4.23.38
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plasmepsins
- falciparum
- plasmodium
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malarial
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antimalarial
- cathepsin
- vacuole
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aspartyl
- proteinases
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hemoglobin-degrading
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intraerythrocytic
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autocatalytic
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proplasmepsins
Reaction
hydrolysis of the -Phe33-/-Leu- bond in the alpha-chain of hemoglobin, leading to denaturation of the molecule =
Synonyms
AH I, aspartic hemoglobinase I, malaria aspartic hemoglobinase, PFAPG, PfPM1, plasmepsin 1, plasmepsin I, plasmepsin-I, PLm I, PM I, PM-I, PMI
ECTree
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Substrates Products
Substrates Products on EC 3.4.23.38 - plasmepsin I
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REACTION DIAGRAM
4-[[4'-(dimethylamino)phenyl]azo]-benzoyl-Glu-Arg-Met-Phe + Leu-Ser-Phe-Pro-(gamma-aminobutyryl)-5-[(2'-aminoethyl)-amino]naphthalenesulfonic acid + H2O
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?
4-[[4'-(dimethylamino)phenyl]azo]-benzoyl-Glu-Arg-Met-Phe-Leu-Ser-Phe-Pro-(gamma-aminobutyryl)-5-[(2'-aminoethyl)-amino]naphthalenesulfonic acid + H2O
4-[[4'-(dimethylamino)phenyl]azo]-benzoyl-Glu-Arg-Met-Phe + Leu-Ser-Phe-Pro-(gamma-aminobutyryl)-5-[(2'-aminoethyl)-amino]naphthalenesulfonic acid
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?
4-[[4'-(dimethylamino)phenyl]azo]-benzoyl-Glu-Arg-Met-Phe-Leu-Ser-Phe-Pro-(gamma-aminobutyryl)-5-[(2'-aminoethyl)-amino]naphthalenesulfonic acid + H2O
?
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?
4-[[4'-(dimethylamino)phenyl]azo]-benzoyl-Glu-Arg-Nle-Phe-Leu-Ser-Phe-Pro-5-[(2'-aminoethyl)-amino]naphthalenesulfonic acid + H2O
4-[[4'-(dimethylamino)phenyl]azo]-benzoyl-Glu-Arg-Nle-Phe + Leu-Ser-Phe-Pro-5-[(2'-aminoethyl)-amino]naphthalenesulfonic acid
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?
Ala-Leu-Glu-Arg-Thr-Phe-Leu-Ser-Phe-Pro-Thr + H2O
Ala-Leu-Glu-Arg-Thr-Phe + Leu-Ser-Phe-Pro-Thr
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EDANS-CO-CH2-CH2-CO-Ala-Leu-Glu-Arg-Met-Phe-Leu-Ser-Phe-Pro-Dap-(DABCYL)-OH + H2O
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hemoglobin beta-chain + H2O
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cleavage sites: Leu31-/-Leu32, Phe41-/-Phe43, Ala129-/-Tyr130
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Leu-Glu-Arg-Ile-Phe-(p-nitro)Phe-Ser-Phe + H2O
Leu-Glu-Arg-Ile-Phe + (p-nitro)Phe-Ser-Phe
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?
Leu-Glu-Arg-Ile-Phe-Phe(NO2)-Ser-Phe + H2O
Leu-Glu-Arg-Ile-Phe + Phe(NO2)-Ser-Phe
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Leu-Glu-Arg-Val-Phe-Phe(NO2)-Ser-Phe + H2O
Leu-Glu-Arg-Val-Phe + Phe(NO2)-Ser-Phe
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?
Lys-Glu-Leu-Val-Phe-(p-nitro)Phe-Ala-Leu-Lys + H2O
Lys-Glu-Leu-Val-Phe + (p-nitro)Phe-Ala-Leu-Lys
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?
Lys-Glu-Leu-Val-Phe-Phe(NO2)-Ala-Leu-Lys + H2O
Lys-Glu-Leu-Val-Phe + Phe(NO2)-Ala-Leu-Lys
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?
Lys-Glu-Phe-Asn-Phe-Phe(NO2)-Ala-Leu-Lys + H2O
Lys-Glu-Phe-Asn-Phe + Phe(NO2)-Ala-Leu-Lys
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?
Lys-Glu-Phe-Val-Phe-Phe(NO2)-Ala-Leu-Lys + H2O
Lys-Glu-Phe-Val-Phe + Phe(NO2)-Ala-Leu-Lys
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?
Lys-Glu-Phe-Val-Phe-Phe(NO2)-Arg-Leu-Lys + H2O
Lys-Glu-Phe-Val-Phe + Phe(NO2)-Arg-Leu-Lys
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?
Lys-Pro-Ile-Leu-Phe-(p-nitro)Phe-Arg-Leu + H2O
Lys-Pro-Ile-Leu-Phe + (p-nitro)Phe-Arg-Leu
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-
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?
Lys-Pro-Ile-Lys-Phe-Phe(NO2)-Arg-Leu + H2O
Lys-Pro-Ile-Lys-Phe + Phe(NO2)-Arg-Leu
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Hemoglobin + H2O
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enzyme is involved in initial steps of Plasmodium hemoglobin degradation
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Hemoglobin + H2O
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the enzyme initiates the hemoglobin degradation pathway in Plasmodium
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Hemoglobin + H2O
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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
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hemoglobin alpha-chain + H2O
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cleavage of the Phe33-/-Leu34- bond
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hemoglobin alpha-chain + H2O
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cleavage sites: Phe33-/-Leu34, Phe46-/-Asp47, Phe98-/-Lys99
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plasmepsin I is 5 to 9times less effective than plasmepsin II at cleaving substrates which mimic the proposed initial cleavage site in the alpha-chain of hemoglobin
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additional information
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plasmepsin I is synthesized and processed to the mature form soon after the parasite invades the red blood cell
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additional information
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S1' subsite prefers hydrophobic residues and the S2' subsite shifts its preferences more to polar residues. Serine is a preferred P1' substitution
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additional information
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S1' subsite prefers hydrophobic residues and the S2' subsite shifts its preferences more to polar residues. Serine is a preferred P1' substitution
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?