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Literature summary extracted from

  • Wang, Q.; Yang, G.; Liu, Y.; Feng, Y.
    Discrimination of esterase and peptidase activities of acylaminoacyl peptidase from hyperthermophilic Aeropyrum pernix K1 by a single mutation (2006), J. Biol. Chem., 281, 18618-18625.
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
3.4.19.1 R526 I the ratio of kcat/Km for p-nitrophenyl caprylate to kcat/KM for N-acetyl-Leu-p-nitroanilide is 17.3fold higher than the wild-type ratio Aeropyrum pernix
3.4.19.1 R526A the ratio of kcat/Km for p-nitrophenyl caprylate to kcat/KM for N-acetyl-Leu-p-nitroanilide is 11.7fold higher than the wild-type ratio Aeropyrum pernix
3.4.19.1 R526E the ratio of kcat/Km for p-nitrophenyl caprylate to kcat/KM for N-acetyl-Leu-p-nitroanilide is 115.5fold higher than the wild-type ratio Aeropyrum pernix
3.4.19.1 R526K the ratio of kcat/Km for p-nitrophenyl caprylate to kcat/KM for N-acetyl-Leu-p-nitroanilide is 13.9fold higher than the wild-type ratio Aeropyrum pernix
3.4.19.1 R526L the ratio of kcat/Km for p-nitrophenyl caprylate to kcat/KM for N-acetyl-Leu-p-nitroanilide is 14.8fold higher than the wild-type ratio Aeropyrum pernix
3.4.19.1 R526V the ratio of kcat/Km for p-nitrophenyl caprylate to kcat/KM for N-acetyl-Leu-p-nitroanilide is 22.3fold higher than the wild-type ratio Aeropyrum pernix

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.4.19.1 0.4
-
 N-acetyl-Leu-p-nitroanilide 80°C, wild-type enzyme Aeropyrum pernix
3.4.19.1 1.3
-
 N-acetyl-Leu-p-nitroanilide 80°C, mutant enzyme R526L Aeropyrum pernix
3.4.19.1 1.7
-
 N-acetyl-Leu-p-nitroanilide 80°C, mutant enzyme R526V Aeropyrum pernix
3.4.19.1 2.1
-
 N-acetyl-Leu-p-nitroanilide 80°C, mutant enzyme R526I Aeropyrum pernix
3.4.19.1 4.3
-
 N-acetyl-Leu-p-nitroanilide 80°C, mutant enzyme R526A Aeropyrum pernix
3.4.19.1 5.8
-
 N-acetyl-Leu-p-nitroanilide 80°C, mutant enzyme R526E Aeropyrum pernix
3.4.19.1 10.5
-
 N-acetyl-Leu-p-nitroanilide 80°C, mutant enzyme R526K Aeropyrum pernix
3.4.19.1 35.7
-
 p-nitrophenyl caprylate 80°C, mutant enzyme R526V Aeropyrum pernix
3.4.19.1 38.2
-
 p-nitrophenyl caprylate 80°C, mutant enzyme R526K Aeropyrum pernix
3.4.19.1 38.2
-
 p-nitrophenyl caprylate 80°C, mutant enzyme R526L Aeropyrum pernix
3.4.19.1 40.1
-
 p-nitrophenyl caprylate 80°C, mutant enzyme R526I Aeropyrum pernix
3.4.19.1 41.6
-
 p-nitrophenyl caprylate 80°C, mutant enzyme R526A Aeropyrum pernix
3.4.19.1 43.3
-
 p-nitrophenyl caprylate 80°C, wild-type enzyme Aeropyrum pernix
3.4.19.1 114.6
-
 p-nitrophenyl caprylate 80°C, mutant enzyme R526E Aeropyrum pernix

Organism

EC Number Organism UniProt Comment Textmining
3.4.19.1 Aeropyrum pernix Q9YBQ2 K1
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.19.1 N-acetyl-Leu-p-nitroanilide + H2O esterase activity of wild-type enzyme with p-nitrophenyl caprylate as substrate is 7times higher than peptidase activity with N-acetyl-Leu-p-nitroanilide as substrate, 150fold higher for mutant enzyme R526V, peptidase activity for mutant R526E is abolished Aeropyrum pernix N-acetyl-Leu + p-nitroaniline
-
 ?
3.4.19.1 p-nitrophenyl caprylate + H2O esterase activity of wild-type enzyme with p-nitrophenyl caprylate as substrate is 7times higher than peptidase activity with N-acetyl-Leu-p-nitroanilide as substrate, 150fold higher for mutant enzyme R526V, peptidase activity for mutant R526E is abolished Aeropyrum pernix nitrophenol + caprylate
-
 ?

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.4.19.1 0.5
-
 N-acetyl-Leu-p-nitroanilide 80°C, mutant enzyme R526E Aeropyrum pernix
3.4.19.1 6.6
-
 p-nitrophenyl caprylate 80°C, wild-type enzyme Aeropyrum pernix
3.4.19.1 8.1
-
 p-nitrophenyl caprylate 80°C, mutant enzyme R526E Aeropyrum pernix
3.4.19.1 9.2
-
 N-acetyl-Leu-p-nitroanilide 80°C, mutant enzyme R526I Aeropyrum pernix
3.4.19.1 9.3
-
 N-acetyl-Leu-p-nitroanilide 80°C, wild-type enzyme Aeropyrum pernix
3.4.19.1 9.4
-
 p-nitrophenyl caprylate 80°C, mutant enzyme R526K Aeropyrum pernix
3.4.19.1 9.6
-
 p-nitrophenyl caprylate 80°C, mutant enzyme R526A Aeropyrum pernix
3.4.19.1 9.6
-
 N-acetyl-Leu-p-nitroanilide 80°C, mutant enzyme R526L Aeropyrum pernix
3.4.19.1 9.7
-
 N-acetyl-Leu-p-nitroanilide 80°C, mutant enzyme R526V Aeropyrum pernix
3.4.19.1 12.6
-
 N-acetyl-Leu-p-nitroanilide 80°C, mutant enzyme R526A Aeropyrum pernix
3.4.19.1 20.8
-
 p-nitrophenyl caprylate 80°C, mutant enzyme R526I Aeropyrum pernix
3.4.19.1 26.9
-
 N-acetyl-Leu-p-nitroanilide 80°C, mutant enzyme R526K Aeropyrum pernix
3.4.19.1 28.5
-
 p-nitrophenyl caprylate 80°C, mutant enzyme R526L Aeropyrum pernix
3.4.19.1 30.9
-
 p-nitrophenyl caprylate 80°C, mutant enzyme R526V Aeropyrum pernix