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Literature summary extracted from

  • Morimoto, K.; Furuta, E.; Hashimoto, H.; Inouye, K.
    Effects of high concentration of salts on the esterase activity and structure of a kiwifruit peptidase, actinidain (2006), J. Biochem., 139, 1065-1071.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.4.22.14 KCl minimal activity at 0.5-0.8 M, depending on substrate concentration. Minimal activity is 50-70% of the acitivity in absence of salt, with increase in KM-value and decrease in kcat-value. Slight reactivation above 0.8 M Actinidia deliciosa
3.4.22.14 LiCl minimal activity at 1.0-1.5 M, depending on substrate concentration. Minimal activity is 50-70% of the acitivity in absence of salt, with increase in KM-value and decrease in kcat-value. Slight reactivation above 1.5 M Actinidia deliciosa
3.4.22.14 NaCl minimal activity at 0.5-1.2 M, depending on substrate concentration. Minimal activity is 50-70% of the acitivity in absence of salt, with increase in KM-value and decrease in kcat-value. Slight reactivation above 1.2 M Actinidia deliciosa

Organism

EC Number Organism UniProt Comment Textmining
3.4.22.14 Actinidia deliciosa
-
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.4.22.14 fruit
-
 Actinidia deliciosa
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.22.14 Nalpha-benzyloxycarbonyl-L-Lys 4-nitrophenyl ester + H2O
-
 Actinidia deliciosa Nalpha-benzyloxycarbonyl-L-Lys + 4-nitrophenol
-
 ?

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
3.4.22.14 0.13
-
 LiCl 25°C, pH 6.5 Actinidia deliciosa
3.4.22.14 0.35
-
 KCl 25°C, pH 6.5 Actinidia deliciosa
3.4.22.14 0.43
-
 NaCl 25°C, pH 6.5 Actinidia deliciosa