3.4.23.39: plasmepsin II
This is an abbreviated version!
For detailed information about plasmepsin II, go to the full flat file.
Word Map on EC 3.4.23.39
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3.4.23.39
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plasmepsins
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plasmodium
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falciparum
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antimalarial
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piperaquine
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artemisinin
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pfmdr1
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cambodia
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proplasmepsins
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hemoglobin-degrading
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pfcrt
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artemisinin-based
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dihydroartemisinin-piperaquine
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prosegment
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molecular biology
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falcipains
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analysis
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medicine
- 3.4.23.39
-
plasmepsins
- plasmodium
- falciparum
-
antimalarial
-
piperaquine
- artemisinin
-
pfmdr1
-
cambodia
-
proplasmepsins
-
hemoglobin-degrading
-
pfcrt
-
artemisinin-based
-
dihydroartemisinin-piperaquine
- prosegment
- molecular biology
-
falcipains
- analysis
- medicine
Reaction
Hydrolysis of the bonds linking certain hydrophobic residues in hemoglobin or globin. Also cleaves the small molecule substrates such as Ala-Leu-Glu-Arg-Thr-Phe!Phe(NO2)-Ser-Phe-Pro-Thr =
Synonyms
AH II, aspartic hemoglobinase II, malarial aspartic protease, PFAPD, pfpm2, plasmepsin 2, plasmepsin II, PLm II, PLMII, PM II, PMII, PSM2
ECTree
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Substrates Products
Substrates Products on EC 3.4.23.39 - plasmepsin II
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REACTION DIAGRAM
4-(4-dimethylaminophenylazo)benzoyl-CH2-CH2-CO-ALERMFLSFP-diaminopimelate-5-[(2-aminoethyl)amino]naphthalene-1-sulfonic acid + H2O
?
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?
4-(4-dimethylaminophenylazo)benzoyl-CH2-CH2-CO-CO-ALERMFLSFP-diaminopimelate-5-[(2-aminoethyl)amino]naphthalene-1-sulfonic acid + H2O
?
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?
4-(4-dimethylaminophenylazo)benzoyl-CH2-CH2-CO-ERMFLSFP-diaminopimelate-5-[(2-aminoethyl)amino]naphthalene-1-sulfonic 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
?
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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
?
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?
Abz-Thr-Ile-Nle-(4-nitro)Phe-Gln-Arg-NH2 + H2O
Abz-Thr-Ile-Nle + (4-nitro)Phe-Gln-Arg-NH2
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-
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?
Ala-Leu-Glu-Arg-Nle-Phe-Phe(NO2)-Ser-Phe-Pro + H2O
Ala-Leu-Glu-Arg-Nle-Phe + Phe(NO2)-Ser-Phe-Pro
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-
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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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?
Ala-Leu-Glu-Arg-Thr-Phe-Phe(NO2)-Ser-Phe-Pro-Thr + H2O
Ala-Leu-Glu-Arg-Thr-Phe + Phe(NO2)-Ser-Phe-Pro-Thr
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-
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?
Ala-Leu-Glu-Arg-Thr-Phe-Phe(p-NO2)-Ser-Phe-Pro-Thr + H2O
Ala-Leu-Glu-Arg-Thr-Phe + Phe(p-NO2)-Ser-Phe-Pro-Thr
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?
Arg-Gln-Phe-Phe(p-NO2)-Ile-Thr + H2O
Arg-Gln-Phe + Phe(p-NO2)-Ile-Thr
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?
DABCYL-Glu-Arg-Nle-Phe-Leu-Ser-Phe-Pro-EDANS + H2O
?
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FRET substrate, substrate is designed to mimic the hemoglobin cleavage site. The substrate is conjugated with the fluorescent donor EDANS and the quencher DABCYL
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?
DABCYL-L-Glu-L-Arg-L-Nle-L-Phe-L-Leu-L-Ser-L-Phe-L-Pro-EDANS + H2O
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FRET-based substrate
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?
EDANS-CO-CH2-CH2-CO-L-Ala-L-Leu-L-Glu-L-Arg-L-Met-L-Phe-L-Leu-L-Ser-L-Phe-L-Pro-Dap(DABCYL)-OH + H2O
?
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?
EDANS-CO-CH2-CH2-COALERMFLSFP-diaminopimelate-(DABCYL)OH + H2O
?
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?
GST-SH3 peptide + H2O
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Y-/-V and L-/-L are major cleavage sites
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?
hemoglobin alpha-chain + H2O
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cleavage sites: Phe33-/-Leu34, Thr108-/-Leu109, Leu136-/-Thr137
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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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-
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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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-
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?
Lys-Ala-Ile-Glu-Phe-Phe(NO2)-Arg-Leu + H2O
Lys-Ala-Ile-Glu-Phe + Phe(NO2)-Arg-Leu
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-
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?
Lys-Asp-Ile-Glu-Phe-Phe(NO2)-Arg-Leu + H2O
Lys-Asp-Ile-Glu-Phe + Phe(NO2)-Arg-Leu
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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-Ile-Phe-Phe(NO2)-Ala-Leu-Lys + H2O
Lys-Glu-Phe-Ile-Phe + Phe(NO2)-Ala-Leu-Lys
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?
Lys-Glu-Phe-Val-Lys-Phe(NO2)-Ala-Leu-Lys + H2O
Lys-Glu-Phe-Val-Lys + 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-Lys-Ile-Glu-Phe-Phe(NO2)-Arg-Leu + H2O
Lys-Lys-Ile-Glu-Phe + Phe(NO2)-Arg-Leu
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?
Lys-Phe-Ile-Glu-Phe-Phe(NO2)-Arg-Leu + H2O
Lys-Phe-Ile-Glu-Phe + Phe(NO2)-Arg-Leu
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?
Lys-Pro-Ala-Glu-Phe-Phe(NO2)-Arg-Leu + H2O
Lys-Pro-Ala-Glu-Phe + Phe(NO2)-Arg-Leu
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?
Lys-Pro-Asp-Glu-Phe-Phe(NO2)-Arg-Leu + H2O
Lys-Pro-Asp-Glu-Phe + Phe(NO2)-Arg-Leu
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?
Lys-Pro-Ile-Ala-Phe-Phe(NO2)-Arg-Leu + H2O
Lys-Pro-Ile-Ala-Phe + Phe(NO2)-Arg-Leu
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?
Lys-Pro-Ile-Asp-Phe-Phe(NO2)-Arg-Leu + H2O
Lys-Pro-Ile-Asp-Phe + Phe(NO2)-Arg-Leu
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?
Lys-Pro-Ile-Glu-Phe-NO2Phe-Arg-Leu + H2O
Lys-Pro-Ile-Glu-Phe + NO2Phe-Arg-Leu
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?
Lys-Pro-Ile-Glu-Phe-Phe(NO2)-Ala-Leu + H2O
Lys-Pro-Ile-Glu-Phe + Phe(NO2)-Ala-Leu
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?
Lys-Pro-Ile-Glu-Phe-Phe(NO2)-Arg-Arg + H2O
Lys-Pro-Ile-Glu-Phe + Phe(NO2)-Arg-Arg
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?
Lys-Pro-Ile-Glu-Phe-Phe(NO2)-Arg-Asp + H2O
Lys-Pro-Ile-Glu-Phe + Phe(NO2)-Arg-Asp
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?
Lys-Pro-Ile-Glu-Phe-Phe(NO2)-Arg-Ile + H2O
Lys-Pro-Ile-Glu-Phe + Phe(NO2)-Arg-Ile
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?
Lys-Pro-Ile-Glu-Phe-Phe(NO2)-Arg-Leu + H2O
Lys-Pro-Ile-Glu-Phe + Phe(NO2)-Arg-Leu
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?
Lys-Pro-Ile-Glu-Phe-Phe(NO2)-Arg-Ser + H2O
Lys-Pro-Ile-Glu-Phe + Phe(NO2)-Arg-Ser
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?
Lys-Pro-Ile-Glu-Phe-Phe(NO2)-Arg-Val + H2O
Lys-Pro-Ile-Glu-Phe + Phe(NO2)-Arg-Val
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?
Lys-Pro-Ile-Glu-Phe-Phe(NO2)-Glu-Leu + H2O
Lys-Pro-Ile-Glu-Phe + Phe(NO2)-Glu-Leu
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?
Lys-Pro-Ile-Glu-Phe-Phe(NO2)-Lys-Leu + H2O
Lys-Pro-Ile-Glu-Phe + Phe(NO2)-Lys-Leu
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?
Lys-Pro-Ile-Glu-Phe-Phe(NO2)-Ser-Leu + H2O
Lys-Pro-Ile-Glu-Phe + Phe(NO2)-Ser-Leu
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?
Lys-Pro-Ile-Glu-Phe-Phe(NO2)-Val-Leu + H2O
Lys-Pro-Ile-Glu-Phe + Phe(NO2)-Val-Leu
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?
Lys-Pro-Ile-Leu-Phe-Nph-Arg-Leu + H2O
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chromogenic peptide substrate
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?
Lys-Pro-Ile-Leu-Phe-Phe(NO2)-Arg-Leu + H2O
Lys-Pro-Ile-Leu-Phe + Phe(NO2)-Arg-Leu
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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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?
Lys-Pro-Ile-Nle-Phe-Phe(NO2)-Arg-Leu + H2O
Lys-Pro-Ile-Nle-Phe + Phe(NO2)-Arg-Leu
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?
Lys-Pro-Ile-Ser-Phe-Phe(NO2)-Arg-Leu + H2O
Lys-Pro-Ile-Ser-Phe + Phe(NO2)-Arg-Leu
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?
Lys-Pro-Ile-Val-Phe-Phe(NO2)-Arg-Leu + H2O
Lys-Pro-Ile-Val-Phe + Phe(NO2)-Arg-Leu
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?
Lys-Pro-Lys-Glu-Phe-Phe(NO2)-Arg-Leu + H2O
Lys-Pro-Lys-Glu-Phe + Phe(NO2)-Arg-Leu
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?
Lys-Pro-Phe-Glu-Phe-Phe(NO2)-Arg-Leu + H2O
Lys-Pro-Phe-Glu-Phe + Phe(NO2)-Arg-Leu
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?
Lys-Pro-Ser-Glu-Phe-Phe(NO2)-Arg-Leu + H2O
Lys-Pro-Ser-Glu-Phe + Phe(NO2)-Arg-Leu
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?
Lys-Ser-Ile-Glu-Phe-Phe(NO2)-Arg-Leu + H2O
Lys-Ser-Ile-Glu-Phe + Phe(NO2)-Arg-Leu
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?
p47phox-PX + H2O
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PX domain of p47phox, a cytosolic factor of the neutrophil NADPH oxydase is digested
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?
plasmepsin 2 + H2O
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PSM2 auto-cleavage after F112 is complete after 20 min in 10 mM citrate pH 4.5
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?
?
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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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quenched fluorescent peptide substrate
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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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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 + H2O
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the enzyme initiates degradation of hemoglobin by cleavage at the alpha-chain between Phe33 and Leu34
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?
Hemoglobin + H2O
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the enzyme participates in the hemoglobin digestive pathway
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?
Hemoglobin + H2O
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the enzyme is involved in degradation of the host cell hemoglobin within the acidic food vacuole of the parasite
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?
Hemoglobin + H2O
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pro-plasmepsin II is transported through the secretory system to cytostomal vacuoles and then is carried along with its substrate hemoglobin to the food vacuole where it is proteolytically processed to mature PMII
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?
Hemoglobin + H2O
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cleaves native hemoglobin and loosely folded alpha-chain
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Hemoglobin + H2O
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the enzyme participates in the hemoglobin digestive pathway
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?
spectrin + H2O
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recombinant plasmepsin II hydrolyzes native spectrin at pH 6.8
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?
spectrin + H2O
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the enzyme catalyzes the degradation of spectrin in the erythrocyte membrane cytoskeletron
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?
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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
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?
additional information
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multiple explicit-water molecular dynamics simulations of plasmepsin II, uncomplexed and with a hydroxypropylamine peptidomimetic inhibitor, indicate that protonation of Asp214 favours a stable active site structure
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?