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Literature summary for 3.4.22.B69 extracted from

  • Pandey, K.C.; Barkan, D.T.; Sali, A.; Rosenthal, P.J.
    Regulatory elements within the prodomain of falcipain-2, a cysteine protease of the malaria parasite Plasmodium falciparum (2009), PLoS ONE, 4, e5694.
    View publication on PubMedView publication on EuropePMC
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Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
Hemoglobin + H2O Plasmodium falciparum
-
 ?
-
 ?
additional information Plasmodium falciparum the falcipain-2 prodomain efficiently inhibits falcipain-2, falcipain-2', berghepain-2, falcipain-3, cathepsin K, cathepsin L, cathepsin B, and cruzain, but it does not inhibit cathepsin C, pepsin, alpha-chymotrypsin, and collagenase ?
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 ?

Organism

Organism UniProt Comment Textmining
Plasmodium falciparum
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-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
benzyloxycarbonyl-Leu-Arg-7-amido-4-methylcoumarin + H2O
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 Plasmodium falciparum benzyloxycarbonyl-Leu-Arg + 7-amino-4-methylcoumarin
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 ?
Hemoglobin + H2O
-
 Plasmodium falciparum ?
-
 ?
additional information the falcipain-2 prodomain efficiently inhibits falcipain-2, falcipain-2', berghepain-2, falcipain-3, cathepsin K, cathepsin L, cathepsin B, and cruzain, but it does not inhibit cathepsin C, pepsin, alpha-chymotrypsin, and collagenase Plasmodium falciparum ?
-
 ?

Synonyms

Synonyms Comment Organism
falcipain-2
-
 Plasmodium falciparum

General Information

General Information Comment Organism
physiological function falcipain-2 plays a key role in Plasmodium falciparum hydrolysis of hemoglobin Plasmodium falciparum