Pepsin A from Sus scrofa (pig)

Enzyme Description

Extremophile
No
EC Number
3.4.23.1 β†—, 3.4.23.1 β†— (synthesis direction)

Sequence

Length: 326 amino acids
IGDEPLENYLDTEYFGTIGIGTPAQDFTVIFDTGSSNLWVPSVYCSSLACSDHNQFNPDDSSTFEATSQELSITYGTGSMTGILGYDTVQVGGISDTNQIFGLSETEPGSFLYYAPFDGILGLAYPSISASGATPVFDNLWDQGLVSQDLFSVYLSSNDDSGSVVLLGGIDSSYYTGSLNWVPVSVEGYWQITLDSITMDGETIACSGGCQAIVDTGTSLLTGPTSAIANIQSDIGASENSDGEMVISCSSIDSLPDIVFTINGVQYPLSPSAYILQDDDSCTSGFEGMDVPTSSGELWILGDVFIRQYYTVFDRANNKVGLAPVA
Marcelo Porto Bemquerer et al. (1994) β€” Pepsin-catalyzed peptide synthesis in organic media: studies with free and immobilized enzyme
International Journal of Peptide and Protein Research  Β· doi:10.1111/j.1399-3011.1994.tb00181.x β†—  Β· Activity + Stability - Product Formation
10 measurements
Database ID
UniProt: P00791 β†—
Sequence Annotation
Inferred - from protein name (first 59 UniProt residues cleaved)
Protein Source
Commercially purchased

Experimental Data (10 measurements)

10 measurements
Property Assay Solvent Solvent Volume Aqueous Reference Measured Value Units Solution pH Temperature Substrate(s) Product(s) Cofactor(s) Shaking Comments
Activity + Stability - Product Formation Reaction yield after incubation (72 hours at 38Β°C ) in the presence of organic solvent, measured by HPLC Butyl Acetate 95% 0 0 % 0.2 M Citrate buffer 6 38Β°C 0.08 mM Benzyloxycarbonyl-L-phenylalanine, 0.16 mM L-Phenylalanine methyl ester.HCl Z-Phe-L-Phenylalanine methyl ester β€” 250 rpm Classical aqueous control (in %) | Protease in synthesis mode/ deducted yield for control (protease then in hydrolysis mode)
Activity + Stability - Product Formation Reaction yield after incubation (72 hours at 38Β°C ) in the presence of organic solvent, measured by HPLC Diisopropyl Ether 95% 0 25 % 0.2 M Citrate buffer 6 38Β°C 0.08 mM Benzyloxycarbonyl-L-phenylalanine, 0.16 mM L-Phenylalanine methyl ester.HCl Z-Phe-L-Phenylalanine methyl ester β€” 250 rpm Classical aqueous control (in %) | Protease in synthesis mode/ deducted yield for control (protease then in hydrolysis mode)
Activity + Stability - Product Formation Reaction yield after incubation (72 hours at 38Β°C ) in the presence of organic solvent, measured by HPLC Benzene 95% 0 21 % 0.2 M Citrate buffer 6 38Β°C 0.08 mM Benzyloxycarbonyl-L-phenylalanine, 0.16 mM L-Phenylalanine methyl ester.HCl Z-Phe-L-Phenylalanine methyl ester β€” 250 rpm Classical aqueous control (in %) | Protease in synthesis mode/ deducted yield for control (protease then in hydrolysis mode)
Activity + Stability - Product Formation Reaction yield after incubation (72 hours at 38Β°C ) in the presence of organic solvent, measured by HPLC Toluene 95% 0 45 % 0.2 M Citrate buffer 6 38Β°C 0.08 mM Benzyloxycarbonyl-L-phenylalanine, 0.16 mM L-Phenylalanine methyl ester.HCl Z-Phe-L-Phenylalanine methyl ester β€” 250 rpm Classical aqueous control (in %) | Protease in synthesis mode/ deducted yield for control (protease then in hydrolysis mode)
Activity + Stability - Product Formation Reaction yield after incubation (72 hours at 38Β°C ) in the presence of organic solvent, measured by HPLC Carbon tetrachloride 95% 0 25 % 0.2 M Citrate buffer 6 38Β°C 0.08 mM Benzyloxycarbonyl-L-phenylalanine, 0.16 mM L-Phenylalanine methyl ester.HCl Z-Phe-L-Phenylalanine methyl ester β€” 250 rpm Classical aqueous control (in %) | Protease in synthesis mode/ deducted yield for control (protease then in hydrolysis mode)
Activity + Stability - Product Formation Reaction yield after incubation (72 hours at 38Β°C ) in the presence of organic solvent, measured by HPLC Cyclohexane 95% 0 58 % 0.2 M Citrate buffer 6 38Β°C 0.08 mM Benzyloxycarbonyl-L-phenylalanine, 0.16 mM L-Phenylalanine methyl ester.HCl Z-Phe-L-Phenylalanine methyl ester β€” 250 rpm Classical aqueous control (in %) | Protease in synthesis mode/ deducted yield for control (protease then in hydrolysis mode)
Activity + Stability - Product Formation Reaction yield after incubation (72 hours at 38Β°C ) in the presence of organic solvent, measured by HPLC n-Hexane 95% 0 70 % 0.2 M Citrate buffer 6 38Β°C 0.08 mM Benzyloxycarbonyl-L-phenylalanine, 0.16 mM L-Phenylalanine methyl ester.HCl Z-Phe-L-Phenylalanine methyl ester β€” 250 rpm Classical aqueous control (in %) | Protease in synthesis mode/ deducted yield for control (protease then in hydrolysis mode)
Activity + Stability - Product Formation Reaction yield after incubation (72 hours at 38Β°C ) in the presence of organic solvent, measured by HPLC n-Heptane 95% 0 69 % 0.2 M Citrate buffer 6 38Β°C 0.08 mM Benzyloxycarbonyl-L-phenylalanine, 0.16 mM L-Phenylalanine methyl ester.HCl Z-Phe-L-Phenylalanine methyl ester β€” 250 rpm Classical aqueous control (in %) | Protease in synthesis mode/ deducted yield for control (protease then in hydrolysis mode)
Activity + Stability - Product Formation Reaction yield after incubation (72 hours at 38Β°C ) in the presence of organic solvent, measured by HPLC n-Octane 95% 0 72 % 0.2 M Citrate buffer 6 38Β°C 0.08 mM Benzyloxycarbonyl-L-phenylalanine, 0.16 mM L-Phenylalanine methyl ester.HCl Z-Phe-L-Phenylalanine methyl ester β€” 250 rpm Classical aqueous control (in %) | Protease in synthesis mode/ deducted yield for control (protease then in hydrolysis mode)
Activity + Stability - Product Formation Reaction yield after incubation (72 hours at 38Β°C ) in the presence of organic solvent, measured by HPLC Isooctane 95% 0 70 % 0.2 M Citrate buffer 6 38Β°C 0.08 mM Benzyloxycarbonyl-L-phenylalanine, 0.16 mM L-Phenylalanine methyl ester.HCl Z-Phe-L-Phenylalanine methyl ester β€” 250 rpm Classical aqueous control (in %) | Protease in synthesis mode/ deducted yield for control (protease then in hydrolysis mode)

Visualization : Activity + Stability β€” Product Formation

Marcelo Porto Bemquerer et al. (1994)

One bar per measurement. Colour = solvent, shade = solvent volume.

T. Cardoso et al. (2009) β€” Acetonitrile-induced unfolding of porcine pepsin A
International Journal of Biological Macromolecules  Β· doi:10.1016/j.ijbiomac.2009.05.006 β†—  Β· Activity - Classical Stability - Tm
18 measurements

Structure

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