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Literature summary for 3.4.24.33 extracted from

  • Noreau, J.; Drapeau, G.R.
    Isolation and properties of the protease from the wild-type and mutant strains of Pseudomonas fragi (1979), J. Bacteriol., 140, 911-916.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.4.24.33

Localization

Localization Comment Organism GeneOntology No. Textmining
extracellular
-
 Pseudomonas fragi
-
-

Organism

Organism UniProt Comment Textmining
Pseudomonas fragi
-
 mutant
-
Pseudomonas fragi
-
 obtained by growth of Pseudomonas fragi ATCC 4973 on elastin as sole C-source
-

Purification (Commentary)

Purification (Comment) Organism
-
 Pseudomonas fragi

Source Tissue

Source Tissue Comment Organism Textmining
culture supernatant
-
 Pseudomonas fragi
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
casein + H2O
-
 Pseudomonas fragi ?
-
 ?
Hemoglobin + H2O
-
 Pseudomonas fragi ?
-
 ?
Insulin B-chain + H2O oxidized with performic acid Pseudomonas fragi ?
-
 ?
Insulin B-chain + H2O cleavage sites: Leu6-Cys7, Leu15-Tyr16, Val18-Cys19, Phe24-Phe25 Pseudomonas fragi ?
-
 ?
additional information the wild-type protease has no well-delineated specificity, some preference for N-terminal side of hydrophilic residues, e.g. aminoethylcysteine, Ser, Thr, Gln and Gly Pseudomonas fragi ?
-
 ?

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 assay at Pseudomonas fragi