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Literature summary 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

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

Application

EC Number Application Comment Organism
3.4.23.1 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

EC Number Protein Variants Comment Organism
3.4.23.1 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
3.4.23.1 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
3.4.23.1 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
3.4.23.1 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
3.4.23.1 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
3.4.23.1 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]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.4.23.1 0.0051
-
 KPILF(NO2)RL pH 3.5, 25°C, mutant enzyme T222V Sus scrofa
3.4.23.1 0.0052
-
 KPILF(NO2)RL pH 3.5, 25°C, mutant enzyme T222V/E287M Sus scrofa
3.4.23.1 0.0062
-
 KPILF(NO2)RL pH 3.5, 25°C, mutant enzyme F111T/L112F/E287M Sus scrofa
3.4.23.1 0.0064
-
 KPILF(NO2)RL pH 3.5, 25°C, mutant enzyme F111T/L112F/T222V/E287M Sus scrofa
3.4.23.1 0.0081
-
 KPILF(NO2)RL pH 3.5, 25°C, wild-type enzyme Sus scrofa
3.4.23.1 0.0082
-
 KPILF(NO2)RL pH 3.5, 25°C, mutant enzyme F111T/L112F Sus scrofa
3.4.23.1 0.0093
-
 KPILF(NO2)RL pH 3.5, 25°C, mutant enzyme E287M Sus scrofa
3.4.23.1 0.011
-
 KPIEF(NO2)RL pH 3.5, 25°C, mutant enzyme F111T/L112F/T222V/E287M Sus scrofa
3.4.23.1 0.011
-
 KPIEF(NO2)RL pH 3.5, 25°C, mutant enzyme T222V/E287M Sus scrofa
3.4.23.1 0.013
-
 KPPEF(NO2)RL pH 3.5, 25°C, mutant enzyme F111T/L112F/T222V/E287M Sus scrofa
3.4.23.1 0.015
-
 KPIQF(NO2)RL pH 3.5, 25°C, mutant enzyme F111T/L112F/T222V/E287M Sus scrofa
3.4.23.1 0.018
-
 KPIEF(NO2)RL pH 3.5, 25°C, mutant enzyme F111T/L112F/E287M Sus scrofa
3.4.23.1 0.019
-
 KPIEF(NO2)RL pH 3.5, 25°C, mutant enzyme F111T/L112F Sus scrofa
3.4.23.1 0.02
-
 KPIQF(NO2)RL pH 3.5, 25°C, mutant enzyme T222V Sus scrofa
3.4.23.1 0.02
-
 KPIEF(NO2)RL pH 3.5, 25°C, mutant enzyme T222V Sus scrofa
3.4.23.1 0.024
-
 KPIEF(NO2)RL pH 3.5, 25°C, mutant enzyme E287M Sus scrofa
3.4.23.1 0.024
-
 KPPEF(NO2)RL pH 3.5, 25°C, mutant enzyme F111T/L112F Sus scrofa
3.4.23.1 0.024
-
 KPPEF(NO2)RL pH 3.5, 25°C, mutant enzyme F111T/L112F/E287M Sus scrofa
3.4.23.1 0.027
-
 KPPEF(NO2)RL pH 3.5, 25°C, mutant enzyme T222V/E287M Sus scrofa
3.4.23.1 0.03
-
 KPIKF(NO2)RL pH 3.5, 25°C, mutant enzyme F111T/L112F/T222V/E287M Sus scrofa
3.4.23.1 0.034
-
 KPIQF(NO2)RL pH 3.5, 25°C, mutant enzyme F111T/L112F Sus scrofa
3.4.23.1 0.034
-
 KPIQF(NO2)RL pH 3.5, 25°C, mutant enzyme F111T/L112F/E287M Sus scrofa
3.4.23.1 0.035
-
 KPIEF(NO2)RL pH 3.5, 25°C, wild-type enzyme Sus scrofa
3.4.23.1 0.036
-
 KPIQF(NO2)RL pH 3.5, 25°C, mutant enzyme T222V/E287M Sus scrofa
3.4.23.1 0.042
-
 KPPEF(NO2)RL pH 3.5, 25°C, mutant enzyme T222V Sus scrofa
3.4.23.1 0.046
-
 KPIKF(NO2)RL pH 3.5, 25°C, mutant enzyme F111T/L112F Sus scrofa
3.4.23.1 0.046
-
 KPIQF(NO2)RL pH 3.5, 25°C, wild-type enzyme Sus scrofa
3.4.23.1 0.05
-
 KPIQF(NO2)RL pH 3.5, 25°C, mutant enzyme E287M Sus scrofa
3.4.23.1 0.053
-
 KPPEF(NO2)RL pH 3.5, 25°C, wild-type enzyme Sus scrofa
3.4.23.1 0.074
-
 KPPEF(NO2)RL pH 3.5, 25°C, mutant enzyme E287M Sus scrofa
3.4.23.1 0.075
-
 KPIKF(NO2)RL pH 3.5, 25°C, mutant enzyme F111T/L112F/E287M Sus scrofa
3.4.23.1 0.079
-
 KPIKF(NO2)RL pH 3.5, 25°C, wild-type enzyme Sus scrofa
3.4.23.1 0.085
-
 KPIKF(NO2)RL pH 3.5, 25°C, mutant enzyme T222V Sus scrofa
3.4.23.1 0.134
-
 KPIKF(NO2)RL pH 3.5, 25°C, mutant enzyme T222V/E287M Sus scrofa
3.4.23.1 0.16
-
 KPIKF(NO2)RL pH 3.5, 25°C, mutant enzyme E287M Sus scrofa

Organism

EC Number Organism UniProt Comment Textmining
3.4.23.1 Sus scrofa
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.23.1 KPIEF(NO2)RL + H2O
-
 Sus scrofa ?
-
 ?
3.4.23.1 KPIKF(NO2)RL + H2O
-
 Sus scrofa ?
-
 ?
3.4.23.1 KPILF(NO2)RL + H2O
-
 Sus scrofa ?
-
 ?
3.4.23.1 KPIQF(NO2)RL + H2O
-
 Sus scrofa ?
-
 ?
3.4.23.1 KPPEF(NO2)RL + H2O
-
 Sus scrofa ?
-
 ?
3.4.23.1 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]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.4.23.1 additional information
-
 additional information turnover numbers for loop mutant enzyme S238-M234 and Y274-T283 Sus scrofa
3.4.23.1 0.1
-
 KPIQF(NO2)RL pH 3.5, 25°C, wild-type enzyme Sus scrofa
3.4.23.1 0.19
-
 KPIQF(NO2)RL pH 3.5, 25°C, mutant enzyme T222V Sus scrofa
3.4.23.1 0.21
-
 KPPEF(NO2)RL pH 3.5, 25°C, mutant enzyme F111T/L112F/E287M Sus scrofa
3.4.23.1 0.24
-
 KPIQF(NO2)RL pH 3.5, 25°C, mutant enzyme F111T/L112F/E287M Sus scrofa
3.4.23.1 0.24
-
 KPIEF(NO2)RL pH 3.5, 25°C, mutant enzyme F111T/L112F/E287M Sus scrofa
3.4.23.1 0.53
-
 KPIQF(NO2)RL pH 3.5, 25°C, mutant enzyme F111T/L112F Sus scrofa
3.4.23.1 0.63
-
 KPIKF(NO2)RL pH 3.5, 25°C, mutant enzyme F111T/L112F/E287M Sus scrofa
3.4.23.1 0.8
-
 KPILF(NO2)RL pH 3.5, 25°C, mutant enzyme T222V/E287M Sus scrofa
3.4.23.1 2 3.7 KPIQF(NO2)RL pH 3.5, 25°C, mutant enzyme E287M Sus scrofa
3.4.23.1 2.8
-
 KPIQF(NO2)RL pH 3.5, 25°C, mutant enzyme T222V/E287M Sus scrofa
3.4.23.1 7
-
 KPPEF(NO2)RL pH 3.5, 25°C, mutant enzyme F111T/L112F/T222V/E287M Sus scrofa
3.4.23.1 8
-
 KPILF(NO2)RL pH 3.5, 25°C, mutant enzyme F111T/L112F/E287M Sus scrofa
3.4.23.1 14
-
 KPILF(NO2)RL pH 3.5, 25°C, wild-type enzyme Sus scrofa
3.4.23.1 22.1
-
 KPILF(NO2)RL pH 3.5, 25°C, mutant enzyme T222V Sus scrofa
3.4.23.1 32.3
-
 KPIKF(NO2)RL pH 3.5, 25°C, mutant enzyme F111T/L112F/T222V/E287M Sus scrofa
3.4.23.1 34.4
-
 KPILF(NO2)RL pH 3.5, 25°C, mutant enzyme E287M Sus scrofa
3.4.23.1 35.6
-
 KPILF(NO2)RL pH 3.5, 25°C, mutant enzyme T222V/E287M Sus scrofa
3.4.23.1 36.3
-
 KPILF(NO2)RL pH 3.5, 25°C, mutant enzyme F111T/L112F/T222V/E287M Sus scrofa
3.4.23.1 38.8
-
 KPIKF(NO2)RL pH 3.5, 25°C, mutant enzyme F111T/L112F Sus scrofa
3.4.23.1 38.9
-
 KPIKF(NO2)RL pH 3.5, 25°C, wild-type enzyme Sus scrofa
3.4.23.1 40.5
-
 KPIKF(NO2)RL pH 3.5, 25°C, mutant enzyme T222V Sus scrofa
3.4.23.1 41.4
-
 KPIKF(NO2)RL pH 3.5, 25°C, mutant enzyme F111T/L112F/E287M Sus scrofa
3.4.23.1 41.5
-
 KPIEF(NO2)RL pH 3.5, 25°C, mutant enzyme T222V Sus scrofa
3.4.23.1 44.2
-
 KPIKF(NO2)RL pH 3.5, 25°C, mutant enzyme E287M Sus scrofa
3.4.23.1 47.3
-
 KPPEF(NO2)RL pH 3.5, 25°C, wild-type enzyme Sus scrofa
3.4.23.1 47.9
-
 KPIQF(NO2)RL pH 3.5, 25°C, wild-type enzyme Sus scrofa
3.4.23.1 49.7
-
 KPIQF(NO2)RL pH 3.5, 25°C, mutant enzyme T222V Sus scrofa
3.4.23.1 52.3
-
 KPIEF(NO2)RL pH 3.5, 25°C, mutant enzyme F111T/L112F/T222V/E287M Sus scrofa
3.4.23.1 53.1
-
 KPILF(NO2)RL pH 3.5, 25°C, mutant enzyme F111T/L112F Sus scrofa
3.4.23.1 55.5
-
 KPIKF(NO2)RL pH 3.5, 25°C, mutant enzyme T222V/E287M Sus scrofa
3.4.23.1 56.8
-
 KPIEF(NO2)RL pH 3.5, 25°C, mutant enzyme T222V/E287M Sus scrofa
3.4.23.1 58.9
-
 KPPEF(NO2)RL pH 3.5, 25°C, mutant enzyme F111T/L112F/T222V/E287M Sus scrofa
3.4.23.1 60.4
-
 KPILF(NO2)RL pH 3.5, 25°C, mutant enzyme F111T/L112F/E287M Sus scrofa
3.4.23.1 60.7
-
 KPIEF(NO2)RL pH 3.5, 25°C, mutant enzyme E287M Sus scrofa
3.4.23.1 62.3
-
 KPPEF(NO2)RL pH 3.5, 25°C, mutant enzyme E287M Sus scrofa
3.4.23.1 62.3
-
 KPPEF(NO2)RL pH 3.5, 25°C, mutant enzyme F111T/L112F Sus scrofa
3.4.23.1 68.9
-
 KPIQF(NO2)RL pH 3.5, 25°C, mutant enzyme F111T/L112F/T222V/E287M Sus scrofa
3.4.23.1 68.9
-
 KPIEF(NO2)RL pH 3.5, 25°C, wild-type enzyme Sus scrofa
3.4.23.1 70
-
 KPPEF(NO2)RL pH 3.5, 25°C, mutant enzyme T222V/E287M Sus scrofa
3.4.23.1 71.4
-
 KPPEF(NO2)RL pH 3.5, 25°C, mutant enzyme T222V Sus scrofa
3.4.23.1 72.5
-
 KPIEF(NO2)RL pH 3.5, 25°C, mutant enzyme F111T/L112F Sus scrofa
3.4.23.1 77.4
-
 KPIQF(NO2)RL pH 3.5, 25°C, mutant enzyme T222V/E287M Sus scrofa
3.4.23.1 79.8
-
 KPPEF(NO2)RL pH 3.5, 25°C, mutant enzyme F111T/L112F/E287M Sus scrofa
3.4.23.1 82.2
-
 KPIQF(NO2)RL pH 3.5, 25°C, mutant enzyme F111T/L112F Sus scrofa
3.4.23.1 85.2
-
 KPIQF(NO2)RL pH 3.5, 25°C, mutant enzyme E287M Sus scrofa
3.4.23.1 97.7
-
 KPIQF(NO2)RL pH 3.5, 25°C, mutant enzyme F111T/L112F/E287M Sus scrofa
3.4.23.1 97.8
-
 KPIEF(NO2)RL pH 3.5, 25°C, mutant enzyme F111T/L112F/E287M Sus scrofa