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Literature summary for 3.4.22.14 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

Inhibitors Comment Organism Structure
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
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
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

Organism UniProt Comment Textmining
Actinidia deliciosa
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
fruit
-
Actinidia deliciosa
-

Substrates and Products (Substrate)

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

Ki Value [mM]

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