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Literature summary for 3.4.11.5 extracted from

  • Fuke, Y.; Matsuoka, G.
    The purification and characterization of prolyl aminopeptidase from Penicillium camemberti (1993), J. Dairy Sci., 76, 2478-2484.
No PubMed abstract available
Search for more literature for 3.4.11.5

Inhibitors

Inhibitors Comment Organism Structure
Fe2+
-
 Penicillium camemberti
Hg2+
-
 Penicillium camemberti

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.25
-
 Pro-p-nitroanilide
-
 Penicillium camemberti

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
66000
-
 ? * 66000, ? * 83000, SDS-PAGE Penicillium camemberti
83000
-
 ? * 66000, ? * 83000, SDS-PAGE Penicillium camemberti
270000
-
 gel filtration Penicillium camemberti

Organism

Organism UniProt Comment Textmining
Penicillium camemberti
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Penicillium camemberti

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
36880
-
-
 Penicillium camemberti

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Pro-p-nitroanilide + H2O
-
 Penicillium camemberti proline + p-nitroaniline
-
 ?

Subunits

Subunits Comment Organism
More ? * 66000, ? * 83000, SDS-PAGE Penicillium camemberti

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
45
-
-
 Penicillium camemberti

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7
-
-
 Penicillium camemberti