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Literature summary for 3.4.14.1 extracted from

  • Klemba, M.; Gluzman, I.; Goldberg, D.E.
    A Plasmodium falciparum dipeptidyl aminopeptidase I participates in vacuolar hemoglobin degradation (2004), J. Biol. Chem., 279, 43000-43007.
    View publication on PubMed
Search for more literature for 3.4.14.1

Localization

Localization Comment Organism GeneOntology No. Textmining
vacuole trafficking route for the enzyme through the parasitophorous vacuole to the food vacuole Plasmodium falciparum 5773
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Plasmodium falciparum dipeptidyl aminopeptidase I participates in vacuolar hemoglobin degradation, the enzyme is important for asexual proliferation ?
-
 ?

Organism

Organism UniProt Comment Textmining
Plasmodium falciparum
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
proteolytic modification the proenzyme has a MW of 77400 Da after signal peptide cleavage Plasmodium falciparum

Purification (Commentary)

Purification (Comment) Organism
-
 Plasmodium falciparum

Source Tissue

Source Tissue Comment Organism Textmining
bloodstream form
-
 Plasmodium falciparum
-
trophozoite
-
 Plasmodium falciparum
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Gly-Arg-7-amido-4-methylcoumarin + H2O
-
 Plasmodium falciparum Gly-Arg + 7-amino-4-methylcoumarin
-
 ?
additional information dipeptidyl aminopeptidase I participates in vacuolar hemoglobin degradation, the enzyme is important for asexual proliferation Plasmodium falciparum ?
-
 ?
Pro-Arg-7-amido-4-methylcoumarin + H2O
-
 Plasmodium falciparum Pro-Arg + 7-amino-4-methylcoumarin
-
 ?

Synonyms

Synonyms Comment Organism
dipeptidyl aminopeptidase I
-
 Plasmodium falciparum
DPAP1
-
 Plasmodium falciparum

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
5.5 6
-
 Plasmodium falciparum