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Literature summary for 3.4.23.1 extracted from

  • Galea, C.A.; Dalrymple, B.P.; Kuypers, R.; Blakeley, R.
    Modification of the substrate specificity of porcine pepsin for the enzymatic production of bovine hide gelatin (2000), Protein Sci., 9, 1947-1959.
    View publication on PubMedView publication on EuropePMC

Activating Compound

Activating Compound Comment Organism Structure
additional information recombinant pepsinogen is activated by lowering the pH to 3.5 at 37°C Sus scrofa

Application

Application Comment Organism
nutrition modification of the substrate specificity of porcine pepsin for the enzymatic production of bovine hide gelatin, The mutant enzyme F111T/L112F can potentially enhance the rate of solubilization of bovine hide collagen under conditions mild enough to maintain the triple helix structure and hence minimize the rate of subsequent denaturation and proteolytic cleavage Sus scrofa

Protein Variants

Protein Variants Comment Organism
E287M the ratio of turnover number to KM-value for KPILF(NO2)RL is 2.2fold higher than that of the wild-type enzyme, the ratio of turnover number to KM-value for KPIEF(NO2)RL is 1.3fold higher than that of the wild-type enzyme,the ratio of turnover number to KM-value for KPIQF(NO2)RL is 1.6fold higher than that of the wild-type enzyme, the ratio of turnover number to KM-value for KPIKF(NO2)RL is 60% of that of the wild-type enzyme, the ratio of turnover number to KM-value for KPPEF(NO2)RL is 90% of that of the wild-type enzyme Sus scrofa
F111T/L112F the ratio of turnover number to KM-value for KPILF(NO2)RL is 3.8fold higher than that of the wild-type enzyme, the ratio of turnover number to KM-value for KPIEF(NO2)RL is 1.9fold higher than that of the wild-type enzyme,the ratio of turnover number to KM-value for KPIQF(NO2)RL is 2.3fold higher than that of the wild-type enzyme, the ratio of turnover number to KM-value for KPIKF(NO2)RL is 1.7fold higher than that of the wild-type enzyme, the ratio of turnover number to KM-value for KPPEF(NO2)RL is 2.9fold higher than that of the wild-type enzyme. Mutant enzyme cleaves SGGYDLSFLPQPPQE at one site Leu-Ser, compared to three sites cleaved by the wild-type enzyme, and at a rate 23fold higher than that of the wild-type enzyme Sus scrofa
F111T/L112F/E287M the ratio of turnover number to KM-value for KPILF(NO2)RL is 5.8fold higher than that of the wild-type enzyme, the ratio of turnover number to KM-value for KPIEF(NO2)RL is 2.8fold higher than that of the wild-type enzyme,the ratio of turnover number to KM-value for KPIQF(NO2)RL is 2.8fold higher than that of the wild-type enzyme, the ratio of turnover number to KM-value for KPIKF(NO2)RL is 1.1fold higher than that of the wild-type enzyme, the ratio of turnover number to KM-value for KPPEF(NO2)RL is 3.7fold higher than that of the wild-type enzyme Sus scrofa
F111T/L112F/T222V/E287M the ratio of turnover number to KM-value for KPILF(NO2)RL is 3.5fold higher than that of the wild-type enzyme, the ratio of turnover number to KM-value for KPIEF(NO2)RL is 2.4fold higher than that of the wild-type enzyme,the ratio of turnover number to KM-value for KPIQF(NO2)RL is 4.4fold higher than that of the wild-type enzyme, the ratio of turnover number to KM-value for KPIKF(NO2)RL is 2.2fold higher than that of the wild-type enzyme, the ratio of turnover number to KM-value for KPPEF(NO2)RL is 5.1fold higher than that of the wild-type enzyme Sus scrofa
T222V the ratio of turnover number to KM-value for KPILF(NO2)RL is 2.5fold higher than that of the wild-type enzyme, the ratio of turnover number to KM-value for KPIEF(NO2)RL is 1.1fold higher than that of the wild-type enzyme,the ratio of turnover number to KM-value for KPIQF(NO2)RL is 1.4fold higher than that of the wild-type enzyme, the ratio of turnover number to KM-value for KPIKF(NO2)RL is equal to that of the wild-type enzyme, the ratio of turnover number to KM-value for KPPEF(NO2)RL is 1.9fold higher than that of the wild-type enzyme Sus scrofa
T222V/E287M the ratio of turnover number to KM-value for KPILF(NO2)RL is 4.1fold higher than that of the wild-type enzyme, the ratio of turnover number to KM-value for KPIEF(NO2)RL is 2.6fold higher than that of the wild-type enzyme,the ratio of turnover number to KM-value for KPIQF(NO2)RL is 2.1fold higher than that of the wild-type enzyme, the ratio of turnover number to KM-value for KPIKF(NO2)RL is 80% of that of the wild-type enzyme, the ratio of turnover number to KM-value for KPPEF(NO2)RL is 2.9fold higher than that of the wild-type enzyme. Mutant enzyme cleaves site Ser-Phe in SGGYDLSFLPQPPQE at a rate 20fold higher than the wild-type enzyme Sus scrofa

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0051
-
KPILF(NO2)RL pH 3.5, 25°C, mutant enzyme T222V Sus scrofa
0.0052
-
KPILF(NO2)RL pH 3.5, 25°C, mutant enzyme T222V/E287M Sus scrofa
0.0062
-
KPILF(NO2)RL pH 3.5, 25°C, mutant enzyme F111T/L112F/E287M Sus scrofa
0.0064
-
KPILF(NO2)RL pH 3.5, 25°C, mutant enzyme F111T/L112F/T222V/E287M Sus scrofa
0.0081
-
KPILF(NO2)RL pH 3.5, 25°C, wild-type enzyme Sus scrofa
0.0082
-
KPILF(NO2)RL pH 3.5, 25°C, mutant enzyme F111T/L112F Sus scrofa
0.0093
-
KPILF(NO2)RL pH 3.5, 25°C, mutant enzyme E287M Sus scrofa
0.011
-
KPIEF(NO2)RL pH 3.5, 25°C, mutant enzyme F111T/L112F/T222V/E287M Sus scrofa
0.011
-
KPIEF(NO2)RL pH 3.5, 25°C, mutant enzyme T222V/E287M Sus scrofa
0.013
-
KPPEF(NO2)RL pH 3.5, 25°C, mutant enzyme F111T/L112F/T222V/E287M Sus scrofa
0.015
-
KPIQF(NO2)RL pH 3.5, 25°C, mutant enzyme F111T/L112F/T222V/E287M Sus scrofa
0.018
-
KPIEF(NO2)RL pH 3.5, 25°C, mutant enzyme F111T/L112F/E287M Sus scrofa
0.019
-
KPIEF(NO2)RL pH 3.5, 25°C, mutant enzyme F111T/L112F Sus scrofa
0.02
-
KPIQF(NO2)RL pH 3.5, 25°C, mutant enzyme T222V Sus scrofa
0.02
-
KPIEF(NO2)RL pH 3.5, 25°C, mutant enzyme T222V Sus scrofa
0.024
-
KPIEF(NO2)RL pH 3.5, 25°C, mutant enzyme E287M Sus scrofa
0.024
-
KPPEF(NO2)RL pH 3.5, 25°C, mutant enzyme F111T/L112F Sus scrofa
0.024
-
KPPEF(NO2)RL pH 3.5, 25°C, mutant enzyme F111T/L112F/E287M Sus scrofa
0.027
-
KPPEF(NO2)RL pH 3.5, 25°C, mutant enzyme T222V/E287M Sus scrofa
0.03
-
KPIKF(NO2)RL pH 3.5, 25°C, mutant enzyme F111T/L112F/T222V/E287M Sus scrofa
0.034
-
KPIQF(NO2)RL pH 3.5, 25°C, mutant enzyme F111T/L112F Sus scrofa
0.034
-
KPIQF(NO2)RL pH 3.5, 25°C, mutant enzyme F111T/L112F/E287M Sus scrofa
0.035
-
KPIEF(NO2)RL pH 3.5, 25°C, wild-type enzyme Sus scrofa
0.036
-
KPIQF(NO2)RL pH 3.5, 25°C, mutant enzyme T222V/E287M Sus scrofa
0.042
-
KPPEF(NO2)RL pH 3.5, 25°C, mutant enzyme T222V Sus scrofa
0.046
-
KPIKF(NO2)RL pH 3.5, 25°C, mutant enzyme F111T/L112F Sus scrofa
0.046
-
KPIQF(NO2)RL pH 3.5, 25°C, wild-type enzyme Sus scrofa
0.05
-
KPIQF(NO2)RL pH 3.5, 25°C, mutant enzyme E287M Sus scrofa
0.053
-
KPPEF(NO2)RL pH 3.5, 25°C, wild-type enzyme Sus scrofa
0.074
-
KPPEF(NO2)RL pH 3.5, 25°C, mutant enzyme E287M Sus scrofa
0.075
-
KPIKF(NO2)RL pH 3.5, 25°C, mutant enzyme F111T/L112F/E287M Sus scrofa
0.079
-
KPIKF(NO2)RL pH 3.5, 25°C, wild-type enzyme Sus scrofa
0.085
-
KPIKF(NO2)RL pH 3.5, 25°C, mutant enzyme T222V Sus scrofa
0.134
-
KPIKF(NO2)RL pH 3.5, 25°C, mutant enzyme T222V/E287M Sus scrofa
0.16
-
KPIKF(NO2)RL pH 3.5, 25°C, mutant enzyme E287M Sus scrofa

Organism

Organism UniProt Comment Textmining
Sus scrofa
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
KPIEF(NO2)RL + H2O
-
Sus scrofa ?
-
?
KPIKF(NO2)RL + H2O
-
Sus scrofa ?
-
?
KPILF(NO2)RL + H2O
-
Sus scrofa ?
-
?
KPIQF(NO2)RL + H2O
-
Sus scrofa ?
-
?
KPPEF(NO2)RL + H2O
-
Sus scrofa ?
-
?
SGGYDLSFLPQPPQE + H2O predominant cleavage of the peptide corresponding to the carboxy-terminal telopeptide region of bovine type I collagen alpha1 chain at Asp-Leu, Leu-Ser and Phe-Leu and at a significant lower rate at Ser-Phe Sus scrofa ?
-
?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
additional information
-
additional information turnover numbers for loop mutant enzyme S238-M234 and Y274-T283 Sus scrofa
0.1
-
KPIQF(NO2)RL pH 3.5, 25°C, wild-type enzyme Sus scrofa
0.19
-
KPIQF(NO2)RL pH 3.5, 25°C, mutant enzyme T222V Sus scrofa
0.21
-
KPPEF(NO2)RL pH 3.5, 25°C, mutant enzyme F111T/L112F/E287M Sus scrofa
0.24
-
KPIQF(NO2)RL pH 3.5, 25°C, mutant enzyme F111T/L112F/E287M Sus scrofa
0.24
-
KPIEF(NO2)RL pH 3.5, 25°C, mutant enzyme F111T/L112F/E287M Sus scrofa
0.53
-
KPIQF(NO2)RL pH 3.5, 25°C, mutant enzyme F111T/L112F Sus scrofa
0.63
-
KPIKF(NO2)RL pH 3.5, 25°C, mutant enzyme F111T/L112F/E287M Sus scrofa
0.8
-
KPILF(NO2)RL pH 3.5, 25°C, mutant enzyme T222V/E287M Sus scrofa
2 3.7 KPIQF(NO2)RL pH 3.5, 25°C, mutant enzyme E287M Sus scrofa
2.8
-
KPIQF(NO2)RL pH 3.5, 25°C, mutant enzyme T222V/E287M Sus scrofa
7
-
KPPEF(NO2)RL pH 3.5, 25°C, mutant enzyme F111T/L112F/T222V/E287M Sus scrofa
8
-
KPILF(NO2)RL pH 3.5, 25°C, mutant enzyme F111T/L112F/E287M Sus scrofa
14
-
KPILF(NO2)RL pH 3.5, 25°C, wild-type enzyme Sus scrofa
22.1
-
KPILF(NO2)RL pH 3.5, 25°C, mutant enzyme T222V Sus scrofa
32.3
-
KPIKF(NO2)RL pH 3.5, 25°C, mutant enzyme F111T/L112F/T222V/E287M Sus scrofa
34.4
-
KPILF(NO2)RL pH 3.5, 25°C, mutant enzyme E287M Sus scrofa
35.6
-
KPILF(NO2)RL pH 3.5, 25°C, mutant enzyme T222V/E287M Sus scrofa
36.3
-
KPILF(NO2)RL pH 3.5, 25°C, mutant enzyme F111T/L112F/T222V/E287M Sus scrofa
38.8
-
KPIKF(NO2)RL pH 3.5, 25°C, mutant enzyme F111T/L112F Sus scrofa
38.9
-
KPIKF(NO2)RL pH 3.5, 25°C, wild-type enzyme Sus scrofa
40.5
-
KPIKF(NO2)RL pH 3.5, 25°C, mutant enzyme T222V Sus scrofa
41.4
-
KPIKF(NO2)RL pH 3.5, 25°C, mutant enzyme F111T/L112F/E287M Sus scrofa
41.5
-
KPIEF(NO2)RL pH 3.5, 25°C, mutant enzyme T222V Sus scrofa
44.2
-
KPIKF(NO2)RL pH 3.5, 25°C, mutant enzyme E287M Sus scrofa
47.3
-
KPPEF(NO2)RL pH 3.5, 25°C, wild-type enzyme Sus scrofa
47.9
-
KPIQF(NO2)RL pH 3.5, 25°C, wild-type enzyme Sus scrofa
49.7
-
KPIQF(NO2)RL pH 3.5, 25°C, mutant enzyme T222V Sus scrofa
52.3
-
KPIEF(NO2)RL pH 3.5, 25°C, mutant enzyme F111T/L112F/T222V/E287M Sus scrofa
53.1
-
KPILF(NO2)RL pH 3.5, 25°C, mutant enzyme F111T/L112F Sus scrofa
55.5
-
KPIKF(NO2)RL pH 3.5, 25°C, mutant enzyme T222V/E287M Sus scrofa
56.8
-
KPIEF(NO2)RL pH 3.5, 25°C, mutant enzyme T222V/E287M Sus scrofa
58.9
-
KPPEF(NO2)RL pH 3.5, 25°C, mutant enzyme F111T/L112F/T222V/E287M Sus scrofa
60.4
-
KPILF(NO2)RL pH 3.5, 25°C, mutant enzyme F111T/L112F/E287M Sus scrofa
60.7
-
KPIEF(NO2)RL pH 3.5, 25°C, mutant enzyme E287M Sus scrofa
62.3
-
KPPEF(NO2)RL pH 3.5, 25°C, mutant enzyme E287M Sus scrofa
62.3
-
KPPEF(NO2)RL pH 3.5, 25°C, mutant enzyme F111T/L112F Sus scrofa
68.9
-
KPIQF(NO2)RL pH 3.5, 25°C, mutant enzyme F111T/L112F/T222V/E287M Sus scrofa
68.9
-
KPIEF(NO2)RL pH 3.5, 25°C, wild-type enzyme Sus scrofa
70
-
KPPEF(NO2)RL pH 3.5, 25°C, mutant enzyme T222V/E287M Sus scrofa
71.4
-
KPPEF(NO2)RL pH 3.5, 25°C, mutant enzyme T222V Sus scrofa
72.5
-
KPIEF(NO2)RL pH 3.5, 25°C, mutant enzyme F111T/L112F Sus scrofa
77.4
-
KPIQF(NO2)RL pH 3.5, 25°C, mutant enzyme T222V/E287M Sus scrofa
79.8
-
KPPEF(NO2)RL pH 3.5, 25°C, mutant enzyme F111T/L112F/E287M Sus scrofa
82.2
-
KPIQF(NO2)RL pH 3.5, 25°C, mutant enzyme F111T/L112F Sus scrofa
85.2
-
KPIQF(NO2)RL pH 3.5, 25°C, mutant enzyme E287M Sus scrofa
97.7
-
KPIQF(NO2)RL pH 3.5, 25°C, mutant enzyme F111T/L112F/E287M Sus scrofa
97.8
-
KPIEF(NO2)RL pH 3.5, 25°C, mutant enzyme F111T/L112F/E287M Sus scrofa