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Literature summary for 3.4.23.38 extracted from

  • Xiao, H.; Tanaka, T.; Ogawa, M.; Yada, R.Y.
    Expression and enzymatic characterization of the soluble recombinant plasmepsin I from Plasmodium falciparum (2007), Protein Eng. Des. Sel., 20, 625-633.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression and partial characterization of soluble recombinant PM I from Plasmodium falciparum in which a truncated form of PM I (Lys77P-Leu329) (P indicates a propart residues) is fused to thioredoxin in the pET32b(1) vector, Trx-tPM I and expressed in Escherichia coli Rosetta-gami B (DE3)pLysS. The soluble fusion protein is purified from cell culture using a combination of Ni21 affinity and gel filtration chromatography and is capable of autocatalytic activation at pH 4.0–5.5, which occurrs at Leu116P-Ser117P, seven residues upstream of the native cleavage site (Gly123P-Asn1) Plasmodium falciparum

Inhibitors

Inhibitors Comment Organism Structure
pepstatin A
-
Plasmodium falciparum

Organism

Organism UniProt Comment Textmining
Plasmodium falciparum
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
proteolytic modification expression and partial characterization of soluble recombinant PM I from Plasmodium falciparum in which a truncated form of PM I (Lys77P-Leu329) (P indicates a propart residues) is fused to thioredoxin in the pET32b(1) vector, Trx-tPM I and expressed in Escherichia coli Rosetta-gami B (DE3)pLysS. pLysS. The soluble fusion protein is purified from cell culture using a combination of Ni21 affinity and gel filtration chromatography and is capable of autocatalytic activation at pH 4.0–5.5, which occurrs at Leu116P–Ser117P, seven residues upstream of the native cleavage site (Gly123P-Asn1) Plasmodium falciparum

Purification (Commentary)

Purification (Comment) Organism
expression and partial characterization of soluble recombinant PM I from Plasmodium falciparum in which a truncated form of PM I (Lys77P–Leu329) (P indicates a propart residues) is fused to thioredoxin in the pET32b(1) vector, Trx-tPM I and expressed in Escherichia coli Rosetta-gami B (DE3)pLysS. pLysS. The soluble fusion protein is purified from cell culture using a combination of Ni21 affinity and gel filtration chromatography Plasmodium falciparum

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
EDANS-CO-CH2-CH2-CO-Ala-Leu-Glu-Arg-Met-Phe-Leu-Ser-Phe-Pro-Dap-(DABCYL)-OH + H2O
-
Plasmodium falciparum ?
-
?
human hemoglobin + H2O
-
Plasmodium falciparum ?
-
?

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
2.5 3 EDANS-CO-CH2-CH2-CO-Ala-Leu-Glu-Arg-Met-Phe-Leu-Ser-Phe-Pro-Dap-(DABCYL)-OH, and a second optimum at pH 4.5-5.5, mature fusion enzyme Plasmodium falciparum
2.8 4 human hemoglobin, mature fusion enzyme Plasmodium falciparum
4.5 5.5 EDANS-CO-CH2-CH2-CO-Ala-Leu-Glu-Arg-Met-Phe-Leu-Ser-Phe-Pro-Dap-(DABCYL)-OH, and a second optimum at pH 2.5-3.0, mature fusion enzyme Plasmodium falciparum

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.0000000117
-
pepstatin A pH 2.8, mature fusion protein Plasmodium falciparum
0.0000000699
-
pepstatin A pH 5.0, mature fusion protein Plasmodium falciparum