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Literature summary for 3.4.23.20 extracted from

  • Blum, M.; Cunningham, A.; Bendiner, M.; Hofmann, T.
    Penicillopepsin, the aspartic proteinase from Penicillium janthinellum: substrate-binding effects and intermediates in transpeptidation reactions (1985), Biochem. Soc. Trans., 13, 1044-1046.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
Isovaleryl-Val-Val-statyl ethyl ester
-
Penicillium janthinellum
Isovaleryl-Val-Val-statyl-Ala ethyl ester
-
Penicillium janthinellum

Localization

Localization Comment Organism GeneOntology No. Textmining
extracellular secreted by mycelium during phase of sporulation Penicillium janthinellum
-
-

Organism

Organism UniProt Comment Textmining
Penicillium janthinellum
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Ac-(Ala)m-Lys-(NO2)Phe-(Ala)n amide + H2O
-
Penicillium janthinellum ?
-
?
additional information transpeptidation reaction of both the amino acid and the acyl transfer type Penicillium janthinellum ?
-
?
Trypsinogen + H2O
-
Penicillium janthinellum ?
-
?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
additional information
-
additional information effect of chain length of substrates and inhibitors of the turnover number Penicillium janthinellum