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Literature summary extracted from

  • Green, P.R.; Oliver, J.D.; Strickland, L.C.; Toerner, D.R.; Matsuzawa, H.; Ohta, T.
    Purification, crystallization and preliminary X-ray investigation of aqualysin I, a heat-stable serine protease (1993), Acta Crystallogr. Sect. D, D49, 349-352.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.4.21.111 hanging and sitting drop vapor diffusion method Thermus aquaticus

Organism

EC Number Organism UniProt Comment Textmining
3.4.21.111 Thermus aquaticus
-
 YT-1
-
3.4.21.111 Thermus aquaticus YT-1
-
 YT-1
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.4.21.111 homogeneity Thermus aquaticus

Source Tissue

EC Number Source Tissue Comment Organism Textmining

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
3.4.21.111 additional information
-
-
 Thermus aquaticus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.21.111 casein + H2O
-
 Thermus aquaticus ?
-
 ?
3.4.21.111 casein + H2O
-
 Thermus aquaticus YT-1 ?
-
 ?
3.4.21.111 N-benzyloxycarbonyl-L-leucyl-4-nitrophenyl ester + H2O
-
 Thermus aquaticus N-benzyloxycarbonyl-L-leucine + 4-nitrophenol
-
 ?
3.4.21.111 N-benzyloxycarbonyl-L-leucyl-4-nitrophenyl ester + H2O
-
 Thermus aquaticus YT-1 N-benzyloxycarbonyl-L-leucine + 4-nitrophenol
-
 ?

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.4.21.111 70 80
-
 Thermus aquaticus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.4.21.111 10 11.5
-
 Thermus aquaticus