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Literature summary extracted from

  • Bryan, P.N.; Rollence, M.L.; Pantoliano, M.W.; Wood, J.; Finzel, B.C.; Gilliland, G.L.; Howard, A.J.; Poulos, T.L.
    Proteases of enhanced stability: characterization of a thermostable variant of subtilisin (1986), Proteins Struct. Funct. Genet., 1, 326-334.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.4.21.62 subtilisin 7150, mutagenized subtilisin with enhanced thermal stability Bacillus amyloliquefaciens

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.4.21.62 wild-type and thermostable mutant 7150 subtilisin at 1.8 A resolution Bacillus amyloliquefaciens

Organism

EC Number Organism UniProt Comment Textmining
3.4.21.62 Bacillus amyloliquefaciens
-
 wild-type and subtilisin 7150 (mutagenized subtilisin with enhanced thermal stability)
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.4.21.62
-
 Bacillus amyloliquefaciens

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.21.62 succinyl-Ala-Ala-Pro-Phe 4-nitroanilide + H2O
-
 Bacillus amyloliquefaciens succinyl-Ala-Ala-Pro-Phe + 4-nitroaniline
-
 ?

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.4.21.62 65
-
 pH 8.0, 10 mM CaCl2, half-life of wild-type enzyme: 59 min, half-life of mutant 7150 enzyme: 223 min Bacillus amyloliquefaciens