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Literature summary for 3.4.23.1 extracted from

  • Tanaka, T.; Yada, R.Y.
    N-terminal portion acts as an initiator of the inactivation of pepsin at neutral pH (2001), Protein Eng., 14, 669-674.
    View publication on PubMed
Search for more literature for 3.4.23.1

Protein Variants

Protein Variants Comment Organism
DELTA240-246/+GD inactivation rate at pH 7.0 is 86% of that of the wild-type value. The Km-value for KPAEFF(NO2)AL is 2fold higher than that of the wild-type enzyme. The KM-value for LSF(NO2)-Nle-AL as substrate is 79% of the wild-type value Sus scrofa
G2C/L167C the mutation reduces the inactivation rate at pH 7.0 by 1.8times compared to wild-type value. The Km-value for KPAEFF(NO2)AL is 2.35fold higher than that of the wild-type enzyme. The KM-value for LSF(NO2)-Nle-AL as substrate is 95% of the wild-type value Sus scrofa
G2S/D3Y the mutation reduces the inactivation rate at pH 7.0 by 1.4times compared to wild-type value. The Km-value for KPAEFF(NO2)AL is 2.2fold higher than that of the wild-type enzyme. The KM-value for LSF(NO2)-Nle-AL as substrate is 1.5fold higher than that of the wild-type enzyme Sus scrofa
G2S/D3Y/L10M/T12A/E13S the mutation reduces the inactivation rate at pH 7.0 by 5.8times. In presence of glycerol and sucrose, this mutant shows a very low rate of inactivation, the residual activity after 240 min is 50% of the initial activity compared to the wild-type which loses most of its activity in 60 min. The Km-value for KPAEFF(NO2)AL is 2.4fold higher than that of the wild-type enzyme. The KM-value for LSF(NO2)-Nle-AL as substrate is 1.5fold higher than that of the wild-type enzyme Sus scrofa
L10M/T12A/E13S the mutation reduces the inactivation rate at pH 7.0 by 1.5times compared to wild-type value. The Km-value for KPAEFF(NO2)AL is 1.9fold higher than that of the wild-type enzyme. The KM-value for LSF(NO2)-Nle-AL as substrate is 2.2fold higher than that of the wild-type enzyme Sus scrofa
S196R/D200G/E202K inactivation rate at pH 7.0 is 86% of that of the wild-type value Sus scrofa
S46K/D52N/N54K/Q55R/D60K inactivation rate at pH 7.0 is 91% of that of the wild-type value Sus scrofa
S46K/D52N/N54K/Q55R/D60K/S196R/D200G/E202K the mutation reduces the inactivation rate at pH 7.0 by 2.3times compared to wild-type value. Km-value for KPAEFF(NO2)AL is 1.7fold higher than that of the wild-type enzyme. The KM-value for LSF(NO2)-Nle-AL as substrate is 1.6fold higher than that of the wild-type enzyme Sus scrofa

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.015
-
 LSF(NO2)-Nle-AL pH 3.95, 37°C, mutant enzyme DELTA240-246/+GD Sus scrofa
0.018
-
 LSF(NO2)-Nle-AL pH 3.95, 37°C, mutant enzyme G2C/L167C Sus scrofa
0.019
-
 LSF(NO2)-Nle-AL pH 3.95, 37°C, wild-type enzyme Sus scrofa
0.028
-
 LSF(NO2)-Nle-AL pH 3.95, 37°C, mutant enzyme G2S/D3Y Sus scrofa
0.028
-
 LSF(NO2)-Nle-AL pH 3.95, 37°C, mutant enzyme G2S/D3Y/L10M/T12A/E13S Sus scrofa
0.031
-
 LSF(NO2)-Nle-AL pH 3.95, 37°C, mutant enzyme S46K/D52N/N54K/Q55R/D60K/S196R/D200G/E202K Sus scrofa
0.034
-
 KPAEFF(NO2)AL pH 3.95, 37°C, wild-type enzyme Sus scrofa
0.041
-
 LSF(NO2)-Nle-AL pH 3.95, 37°C, mutant enzyme L10M/T12A/E13S Sus scrofa
0.057
-
 KPAEFF(NO2)AL pH 3.95, 37°C, mutant enzyme S46K/D52N/N54K/Q55R/D60K/S196R/D200G/E202K Sus scrofa
0.065
-
 KPAEFF(NO2)AL pH 3.95, 37°C, mutant enzyme L10M/T12A/E13S Sus scrofa
0.07
-
 KPAEFF(NO2)AL pH 3.95, 37°C, mutant enzyme DELTA240-246/+GD Sus scrofa
0.075
-
 KPAEFF(NO2)AL pH 3.95, 37°C, mutant enzyme G2S/D3Y Sus scrofa
0.08
-
 KPAEFF(NO2)AL pH 3.95, 37°C, mutant enzyme G2C/L167C Sus scrofa
0.083
-
 KPAEFF(NO2)AL pH 3.95, 37°C, mutant enzyme G2S/D3Y/L10M/T12A/E13S Sus scrofa

Organism

Organism UniProt Comment Textmining
Sus scrofa
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
KPAEFF(NO2)AL + H2O
-
 Sus scrofa ?
-
 ?
LSF(NO2)-Nle-AL + H2O
-
 Sus scrofa ?
-
 ?

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
2.1
-
-
 Sus scrofa