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Literature summary for 3.4.22.25 extracted from

  • Huet, J.; Looze, Y.; Bartik, K.; Raussens, V.; Wintjens, R.; Boussard, P.
    Structural characterization of the papaya cysteine proteinases at low pH (2006), Biochem. Biophys. Res. Commun., 341, 620-626.
    View publication on PubMed
Search for more literature for 3.4.22.25

Application

Application Comment Organism
nutrition the enzyme needs to be protected from acid denaturation and proteolysis in the gut after oral administration to be effective as cysteine protease Carica papaya

Localization

Localization Comment Organism GeneOntology No. Textmining
extracellular latex Carica papaya
-
-

Organism

Organism UniProt Comment Textmining
Carica papaya
-
-
-

Purification (Commentary)

Purification (Comment) Organism
native enzyme from latex by ion exchange and adsorption chromatography, and gel filtration Carica papaya

Source Tissue

Source Tissue Comment Organism Textmining
latex
-
 Carica papaya
-

Synonyms

Synonyms Comment Organism
glycine endopeptidase
-
 Carica papaya

pH Stability

pH Stability pH Stability Maximum Comment Organism
additional information
-
 the enzyme undergoes a conformational transition at low pH and 37°C, that instantaneously and irreversibly converts the native form into molten globules, which are unstable and rapidly degraded by pepsin Carica papaya