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Literature summary for 3.4.24.25 extracted from

  • Wilkes, S.H.; Prescott, J.M.
    Aeromonas neutral protease (1976), Methods Enzymol., 45, 404-415.
    View publication on PubMed

General Stability

General Stability Organism
Lyophilization and reconstitution results in approximately 20% loss of activity Vibrio proteolyticus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.5
-
Furylacryloyl-Gly-Leu-NH2
-
Vibrio proteolyticus

Metals/Ions

Metals/Ions Comment Organism Structure
Calcium contains 1.7 mol of calcium per mol of enzyme, after 48 h of dialysis, not essential for activity, Ca2+ likely plays a structural role Vibrio proteolyticus
Zinc essential for activity Vibrio proteolyticus
Zinc enzyme contains 1 mol of zinc per mol of enzyme Vibrio proteolyticus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
34800
-
Aeromonas proteolytica, sedimentation equilibrium, sedimentation velocity-diffusion experiments Vibrio proteolyticus
35000
-
1 * 35000 (about), Aeromonas proteolytica, sedimentation equilibrium in presence of guanidine-HCl Vibrio proteolyticus

Organism

Organism UniProt Comment Textmining
Vibrio proteolyticus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Vibrio proteolyticus

Source Tissue

Source Tissue Comment Organism Textmining
culture filtrate
-
Vibrio proteolyticus
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
-
Vibrio proteolyticus

Storage Stability

Storage Stability Organism
-20°C, Tricine or Tris buffer, stable for several years Vibrio proteolyticus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
casein + H2O
-
Vibrio proteolyticus ?
-
?
furylacryloyl-Gly-Leu-NH2 + H2O
-
Vibrio proteolyticus furylacryloyl-Gly + Leu-NH2
-
?
Gelatin + H2O
-
Vibrio proteolyticus ?
-
?
additional information preference for bonds of the type X-Phe, X-Leu, X-Tyr to which a hydrophobic residue contributes the amino group, and whereas it is essential that the NH2-terminal position of dipeptide substrates be blocked, the enzyme hydrolyzes substrates with free carboxyl groups Vibrio proteolyticus ?
-
?
Urea-denatured hemoglobin + H2O
-
Vibrio proteolyticus ?
-
?

Subunits

Subunits Comment Organism
monomer 1 * 35000 (about), Aeromonas proteolytica, sedimentation equilibrium in presence of guanidine-HCl Vibrio proteolyticus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
or 37°C, assay at Vibrio proteolyticus
37
-
or 25°C, assay at Vibrio proteolyticus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
-
Vibrio proteolyticus

pH Stability

pH Stability pH Stability Maximum Comment Organism
7 11 10°C, stable for more than 1 week Vibrio proteolyticus