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Enzyme Nomenclature
Information on EC 3.4.23.1 - pepsin A
for references in articles please use BRENDA:EC3.4.23.1
Word Map on EC 3.4.23.1
- 3.4.23.1
- gastric
- trypsin
- collagen
- ulcer
- stomach
- mucosa
- gastrointestinal
- juice
-
peptic
- porcine
- duodenal
- chymotrypsin
- reflux
-
pancreatin
- bile
- papain
- histamine
-
meal
- pentagastrin
- collagenase
-
cathepsins
-
hydrolysates
- hcl
-
hydrochloric
- fistula
- pepstatin
- lactoferrin
-
procollagens
-
vagal
-
gastroesophageal
-
fab\'2
- renin
- chymosin
-
antisecretory
- cimetidine
-
allergen
-
heartburn
-
h2-receptors
-
gastroprotective
- synthesis
-
pylorus
-
antacid
-
beta-lactoglobulin
-
fundic
-
ulcerogenic
-
antiulcer
- nutrition
-
gastroduodenal
- medicine
- alcalase
- analysis
- ranitidine
-
vagotomy
-
triple-helical
- food industry
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Specify your search results
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
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EC NUMBER 
COMMENTARY 
3.4.23.1
-
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RECOMMENDED NAME
GeneOntology No.
pepsin A
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Preferential cleavage: hydrophobic, preferably aromatic, residues in P1 and P1' positions. Cleaves Phe1-/-Val, Gln4-/-His, Glu13-/-Ala, Ala14-/-Leu, Leu15-/-Tyr, Tyr16-/-Leu, Gly23-/-Phe, Phe24-/-Phe and Phe25-/-Tyr bonds in the B chain of insulin
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
-
-
endopeptidase
-
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CAS REGISTRY NUMBER
COMMENTARY
9001-75-6
-
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
34993, 35005, 35010, 36729, 36730, 36734, 36738, 36739, 36742, 36743, 36745, 36751, 36752, 36753, 36756, 36760, 36761, 36764, 36769, 36770, 649688, 651321, 652620, 653313, 653708, 653827, 667408, 668029, 669014, 669817, 678165, 679555, 681064, 682500, 708952, 709708, 711237, 711286, 712213, 712220, 712877, 717384, 717394
-
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
benzyloxycarbonyl-His-Phe(NO2)-beta-phenyl-L-lactyl-O-methyl ester + H2O
benzyloxycarbonyl-His-Phe(NO2) + phenyl-L-lactyl-O-methyl ester
Cry1A(b) protein + H2O
?
-
from transgenic maize or from Bacillus thuringiensis
-
-
?
Mca-KKPAEFFALK-Dnp + H2O
Mca-KKPAEF + FFALK-Dnp
this peptide is preferentially cleaved at Phe-Phe, with a second minor cleavage occurring at Phe-Ala
-
-
?
Mca-KLHPEVLFVLEK-Dnp + H2O
Mca-KLHPEVL + FVLEK-Dnp
the preferred cleavage site is between Leu-Phe, a minor cleavage site is between Phe-Ala
-
-
?
metmyoglobin + H2O
?
-
-
treatment with pepsin at pH 4.0 results in lowering the (pseudo)peroxidase activity of metmyoglobin both at physiological pH and at meat pH, leading to strongly enhanced prooxidative effect of mildly proteolyzed metmyoglobin on lipid oxidation
-
?
oxidized insulin B chain + H2O
FVNQHLCGSHLVEAL + L-Tyr + LVCGERGFFYTPKA
two major cleavage sites are at Leu15-Tyr16 and Tyr16-Leu17
-
-
?
Pro-Thr-Glu-Phe-(p-nitro-Phe)-Arg-Leu-OH + H2O
Pro-Thr-Glu-Phe + (p-nitro-Phe)-Arg-Leu-OH
-
-
-
?
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
-
?
acetyl-L-phenylalanyl-L-diiodotyrosine + H2O
acetyl-L-phenylalanine + L-diiodotyrosine
-
low activity
-
-
?
acetyl-L-phenylalanyl-L-diiodotyrosine + H2O
acetyl-L-phenylalanine + L-diiodotyrosine
-
-
-
-
?
acetyl-L-phenylalanyl-L-diiodotyrosine + H2O
acetyl-L-phenylalanine + L-diiodotyrosine
-
-
-
-
?
acetyl-L-phenylalanyl-L-diiodotyrosine + H2O
acetyl-L-phenylalanine + L-diiodotyrosine
-
low activity
-
-
?
acetyl-L-phenylalanyl-L-diiodotyrosine + H2O
acetyl-L-phenylalanine + L-diiodotyrosine
-
-
-
-
?
acetyl-L-phenylalanyl-L-diiodotyrosine + H2O
acetyl-L-phenylalanine + L-diiodotyrosine
-
-
-
-
?
acetyl-L-phenylalanyl-L-diiodotyrosine + H2O
acetyl-L-phenylalanine + L-diiodotyrosine
-
-
-
-
?
benzyloxycarbonyl-His-Phe(NO2)-beta-phenyl-L-lactyl-O-methyl ester + H2O
benzyloxycarbonyl-His-Phe(NO2) + phenyl-L-lactyl-O-methyl ester
dogfish
-
-
-
-
?
benzyloxycarbonyl-His-Phe(NO2)-beta-phenyl-L-lactyl-O-methyl ester + H2O
benzyloxycarbonyl-His-Phe(NO2) + phenyl-L-lactyl-O-methyl ester
-
-
-
-
?
benzyloxycarbonyl-His-Phe(NO2)-beta-phenyl-L-lactyl-O-methyl ester + H2O
benzyloxycarbonyl-His-Phe(NO2) + phenyl-L-lactyl-O-methyl ester
salmon
-
-
-
-
?
benzyloxycarbonyl-His-Phe(NO2)-beta-phenyl-L-lactyl-O-methyl ester + H2O
benzyloxycarbonyl-His-Phe(NO2) + phenyl-L-lactyl-O-methyl ester
-
-
-
-
?
benzyloxycarbonyl-His-Phe(NO2)-beta-phenyl-L-lactyl-O-methyl ester + H2O
benzyloxycarbonyl-His-Phe(NO2) + phenyl-L-lactyl-O-methyl ester
shark
-
-
-
-
?
benzyloxycarbonyl-His-Phe(NO2)-beta-phenyl-L-lactyl-O-methyl ester + H2O
benzyloxycarbonyl-His-Phe(NO2) + phenyl-L-lactyl-O-methyl ester
-
-
-
-
?
Proteins + H2O
?
-
enzyme formed from pepsinogen A, agent of gastric digestion in mammals and birds
-
-
-
additional information
?
-
dogfish
-
absolute requirement for L-enantiomer in both the X and Y position of substrate
-
-
-
additional information
?
-
dogfish
-
condensation reaction: pH 4, high substrate concentrations, oligopeptides converted to polymeric products
-
-
-
additional information
?
-
-
absolute requirement for L-enantiomer in both the X and Y position of substrate
-
-
-
additional information
?
-
-
condensation reaction: pH 4, high substrate concentrations, oligopeptides converted to polymeric products
-
-
-
additional information
?
-
-
preference for hydrophobic and aromatic residues at P’1 site of substrate
-
-
-
additional information
?
-
-
pepsin A strongly prefers a hydrophobic/aromatic residue at P1’ in any type of peptide
-
-
-
additional information
?
-
the cleavage site of isoform PG1 to produce pepsin is clearly at the 41-42 bond of Phe-Ala
-
-
-
additional information
?
-
salmon
-
absolute requirement for L-enantiomer in both the X and Y position of substrate
-
-
-
additional information
?
-
salmon
-
condensation reaction: pH 4, high substrate concentrations, oligopeptides converted to polymeric products
-
-
-
additional information
?
-
-
absolute requirement for L-enantiomer in both the X and Y position of substrate
-
-
-
additional information
?
-
-
condensation reaction: pH 4, high substrate concentrations, oligopeptides converted to polymeric products
-
-
-
additional information
?
-
shark
-
absolute requirement for L-enantiomer in both the X and Y position of substrate
-
-
-
additional information
?
-
shark
-
condensation reaction: pH 4, high substrate concentrations, oligopeptides converted to polymeric products
-
-
-
additional information
?
-
Edans-Ile-His-Pro-Phe-His-Leu-Val-Ile-His-Thr-Lys-Dabcyl-Arg, Arg-Glu-Edans-Ser-Gln-Asn-Tyr-Pro-Ile-Val-Gln-Lys-Dabcyl-Arg, and Mca-Lys-Ser-Glu-Val-Asn-Leu-Asp-Ala-Glu-Phe-Lys-Dnp are not significantly processed by shewasin A
-
-
-
additional information
?
-
-
Edans-Ile-His-Pro-Phe-His-Leu-Val-Ile-His-Thr-Lys-Dabcyl-Arg, Arg-Glu-Edans-Ser-Gln-Asn-Tyr-Pro-Ile-Val-Gln-Lys-Dabcyl-Arg, and Mca-Lys-Ser-Glu-Val-Asn-Leu-Asp-Ala-Glu-Phe-Lys-Dnp are not significantly processed by shewasin A
-
-
-
additional information
?
-
-
preference for hydrophobic L-amino acid residues on both sides of X-Y bond in benzyloxycarbonyl-L-histidyl-X-Y-OR
-
-
-
additional information
?
-
-
absolute requirement for L-enantiomer in both the X and Y position of substrate
-
-
-
additional information
?
-
-
condensation reaction: pH 4, high substrate concentrations, oligopeptides converted to polymeric products
-
-
-
additional information
?
-
-
the active site of pepsin is formed in the intermediate conformation dominant at mildly acidic pH
-
?
additional information
?
-
-
detailed study on the interaction of porcine pepsin A with derivatives of aromatic amino acids immobilized via a carboxyl or amino group to Sepharose activated with divinyl sulfone
-
-
-
additional information
?
-
-
digestibility of maize and sorghum proteins without and after heat-treatment
-
-
-
additional information
?
-
-
solubilization of collagens from the skin of Priacanthus tayenus and Priacanthus macracanthus
-
-
?
additional information
?
-
-
pepsin A strongly prefers a hydrophobic/aromatic residue at P1’ in any type of peptide
-
-
-
additional information
?
-
-
solubilization of collagens from the skin of Priacanthus tayenus and Priacanthus macracanthus
-
-
?
additional information
?
-
no digestion of Phe-Gly-His-Phe-(p-nitro-Phe)-Ala-Phe-OMe
-
-
-
additional information
?
-
no digestion of Phe-Gly-His-Phe-(p-nitro-Phe)-Ala-Phe-OMe
-
-
-
additional information
?
-
-
no digestion of Phe-Gly-His-Phe-(p-nitro-Phe)-Ala-Phe-OMe
-
-
-
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
additional information
?
-
E2IKQ9
the cleavage site of isoform PG1 to produce pepsin is clearly at the 41-42 bond of Phe-Ala
-
-
-
Proteins + H2O
?
-
enzyme formed from pepsinogen A, agent of gastric digestion in mammals and birds
-
-
-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
alpha2-Macroglobulin
-
activity towards reduced and carboxymethylated ribonuclease A is significantly inhibited at pH 5.5, the activity towards a peptide substrate, oxidized insulin B-chain, is scarcely inhibited
-
imidazole
dogfish
-
hemoglobin hydrolysis inhibited, cleavage of small synthetic peptide and ester substrates enhanced
imidazole
-
hemoglobin hydrolysis inhibited, cleavage of small synthetic peptide and ester substrates enhanced
imidazole
salmon
-
hemoglobin hydrolysis inhibited, cleavage of small synthetic peptide and ester substrates enhanced
imidazole
-
hemoglobin hydrolysis inhibited, cleavage of small synthetic peptide and ester substrates enhanced
imidazole
shark
-
hemoglobin hydrolysis inhibited, cleavage of small synthetic peptide and ester substrates enhanced
imidazole
-
hemoglobin hydrolysis inhibited, cleavage of small synthetic peptide and ester substrates enhanced
KCN
dogfish
-
similar effect as with imidazole, hemoglobin hydrolysis inhibited, cleavage of small synthetic peptide and ester substrates enhanced
KCN
-
similar effect as with imidazole, hemoglobin hydrolysis inhibited, cleavage of small synthetic peptide and ester substrates enhanced
KCN
salmon
-
similar effect as with imidazole, hemoglobin hydrolysis inhibited, cleavage of small synthetic peptide and ester substrates enhanced
KCN
-
similar effect as with imidazole, hemoglobin hydrolysis inhibited, cleavage of small synthetic peptide and ester substrates enhanced
KCN
shark
-
similar effect as with imidazole, hemoglobin hydrolysis inhibited, cleavage of small synthetic peptide and ester substrates enhanced
KCN
-
similar effect as with imidazole, hemoglobin hydrolysis inhibited, cleavage of small synthetic peptide and ester substrates enhanced
Pepstatin
-
the intermediate conformation of the enzyme binds the active site inhibitor with a strength similar to that of the native conformation
pepstatin A
complete inhibition at a molar ratio of 1:20 (pepstatin A:pepsin)
pepstatin A
requires an inhibitor/enzyme ratio of 1:10 to reach about 50% inhibition; requires an inhibitor/enzyme ratio of 1:10 to reach about 60% inhibition
Tetranitromethane
dogfish
-
similar effect as with imidazole, haemoglobin hydrolysis inhibited, cleavage of small synthetic peptide and ester substrates enhanced
Tetranitromethane
-
similar effect as with imidazole, haemoglobin hydrolysis inhibited, cleavage of small synthetic peptide and ester substrates enhanced
Tetranitromethane
salmon
-
similar effect as with imidazole, haemoglobin hydrolysis inhibited, cleavage of small synthetic peptide and ester substrates enhanced
Tetranitromethane
-
similar effect as with imidazole, haemoglobin hydrolysis inhibited, cleavage of small synthetic peptide and ester substrates enhanced
Tetranitromethane
shark
-
similar effect as with imidazole, haemoglobin hydrolysis inhibited, cleavage of small synthetic peptide and ester substrates enhanced
Tetranitromethane
-
similar effect as with imidazole, haemoglobin hydrolysis inhibited, cleavage of small synthetic peptide and ester substrates enhanced
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
the pepsinogen isoform converts into the active form pepsin under pH 2.0
-
additional information
-
pepsinogen is converted into pepsin quickly at pH 2.0
-
additional information
-
recombinant pepsinogen is activated by lowering the pH to 3.5 at 37°C
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.055
hemoglobin
isoform pepsin 1, in 250 mM sodium acetate buffer (pH 3.0), at 37°C
-
0.12
hemoglobin
-
isoform pepsin 1, in 250 mM sodium acetate buffer (pH 3.0), at 37°C
-
0.057
KPAEFF(NO2)AL
-
pH 3.95, 37°C, mutant enzyme S46K/D52N/N54K/Q55R/D60K/S196R/D200G/E202K
0.011
KPIEF(NO2)RL
-
pH 3.5, 25°C, mutant enzyme F111T/L112F/T222V/E287M; pH 3.5, 25°C, mutant enzyme T222V/E287M
0.034
KPIQF(NO2)RL
-
pH 3.5, 25°C, mutant enzyme F111T/L112F; pH 3.5, 25°C, mutant enzyme F111T/L112F/E287M
0.024
KPPEF(NO2)RL
-
pH 3.5, 25°C, mutant enzyme F111T/L112F; pH 3.5, 25°C, mutant enzyme F111T/L112F/E287M
0.048
L-Lys-L-Pro-L-Ala-L-Glu-L-Phe-L-Phe(NO2)-L-Ala-L-Leu
-
unglycosylated mutant T77N, pH 2.0
0.049
L-Lys-L-Pro-L-Ala-L-Glu-L-Phe-L-Phe(NO2)-L-Ala-L-Leu
-
unglycosylated mutant S281N, pH 2.0
0.052
L-Lys-L-Pro-L-Ala-L-Glu-L-Phe-L-Phe(NO2)-L-Ala-L-Leu
-
glycosylated mutant T77N, pH 2.0
0.055
L-Lys-L-Pro-L-Ala-L-Glu-L-Phe-L-Phe(NO2)-L-Ala-L-Leu
-
unglycosylated mutant E244N/V246T, pH 2.0
0.064
L-Lys-L-Pro-L-Ala-L-Glu-L-Phe-L-Phe(NO2)-L-Ala-L-Leu
-
unglycosylated mutant S110N/L112T, pH 2.0
0.068
L-Lys-L-Pro-L-Ala-L-Glu-L-Phe-L-Phe(NO2)-L-Ala-L-Leu
-
glycosylated mutant E244N/V246T, pH 2.0
0.069
L-Lys-L-Pro-L-Ala-L-Glu-L-Phe-L-Phe(NO2)-L-Ala-L-Leu
-
glycosylated mutant S281N, pH 2.0
0.075
L-Lys-L-Pro-L-Ala-L-Glu-L-Phe-L-Phe(NO2)-L-Ala-L-Leu
-
glycosylated mutant S110N/L112T, pH 2.0
0.028
LSF(NO2)-Nle-AL
-
pH 3.95, 37°C, mutant enzyme G2S/D3Y; pH 3.95, 37°C, mutant enzyme G2S/D3Y/L10M/T12A/E13S
0.031
LSF(NO2)-Nle-AL
-
pH 3.95, 37°C, mutant enzyme S46K/D52N/N54K/Q55R/D60K/S196R/D200G/E202K
0.025
Pro-Thr-Glu-Phe-(p-nitro-Phe)-Arg-Leu-OH
37°C, acidic pH
0.074
Pro-Thr-Glu-Phe-(p-nitro-Phe)-Arg-Leu-OH
37°C, acidic pH
additional information
additional information
-
pH-dependence of Km-value of N-trifluoroacetyl aromatic amino acids
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
7.34
hemoglobin
isoform pepsin 1, in 250 mM sodium acetate buffer (pH 3.0), at 37°C
-
23.2
hemoglobin
-
isoform pepsin 1, in 250 mM sodium acetate buffer (pH 3.0), at 37°C
-
62.3
KPPEF(NO2)RL
-
pH 3.5, 25°C, mutant enzyme E287M; pH 3.5, 25°C, mutant enzyme F111T/L112F
16
L-Lys-L-Pro-L-Ala-L-Glu-L-Phe-L-Phe(NO2)-L-Ala-L-Leu
-
unglycosylated mutant S110N/L112T, pH 2.0
53
L-Lys-L-Pro-L-Ala-L-Glu-L-Phe-L-Phe(NO2)-L-Ala-L-Leu
-
glycosylated mutant T77N, pH 2.0
54
L-Lys-L-Pro-L-Ala-L-Glu-L-Phe-L-Phe(NO2)-L-Ala-L-Leu
-
glycosylated mutant S110N/L112T, pH 2.0
68.7
L-Lys-L-Pro-L-Ala-L-Glu-L-Phe-L-Phe(NO2)-L-Ala-L-Leu
-
glycosylated mutant S281N, pH 2.0
70.6
L-Lys-L-Pro-L-Ala-L-Glu-L-Phe-L-Phe(NO2)-L-Ala-L-Leu
-
glycosylated mutant E244N/V246T, pH 2.0
121
L-Lys-L-Pro-L-Ala-L-Glu-L-Phe-L-Phe(NO2)-L-Ala-L-Leu
-
unglycosylated mutant E244N/V246T, pH 2.0
127
L-Lys-L-Pro-L-Ala-L-Glu-L-Phe-L-Phe(NO2)-L-Ala-L-Leu
-
unglycosylated mutant S281N, pH 2.0
150.3
L-Lys-L-Pro-L-Ala-L-Glu-L-Phe-L-Phe(NO2)-L-Ala-L-Leu
-
unglycosylated mutant S110N/L112T, pH 2.0
154
L-Lys-L-Pro-L-Ala-L-Glu-L-Phe-L-Phe(NO2)-L-Ala-L-Leu
-
unglycosylated mutant T77N, pH 2.0
0.54
Pro-Thr-Glu-Phe-(p-nitro-Phe)-Arg-Leu-OH
37°C, acidic pH
3.32
Pro-Thr-Glu-Phe-(p-nitro-Phe)-Arg-Leu-OH
37°C, acidic pH
additional information
additional information
-
pH-dependence of turnover number of N-trifluoroacetyl aromatic amino acids
-
additional information
additional information
-
turnover numbers for loop mutant enzyme S238-M234 and Y274-T283
-
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2000
Lys-Pro-Ala-Glu-Phe-Phe(NO2)-Ala-Leu
-
pH not specified in the publication, temperature not specified in the publication
130
hemoglobin
isoform pepsin 1, in 250 mM sodium acetate buffer (pH 3.0), at 37°C
-
190
hemoglobin
-
isoform pepsin 1, in 250 mM sodium acetate buffer (pH 3.0), at 37°C
-
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
30.71 U/mg protein. One unit is defined as the amount causing an increase of 1.0 in absorbance at 280 nm per min
additional information
the specific activity of the crude extract and 7.9fold purified enzyme are 4.0 and 31.5 units/mg. One unit of pepsin activity is defined as an increase of absorbance of 1.0 at 280 nm during an incubation time of 30 min at pH 3.0 and 37°C
additional information
-
the specific activity of the crude extract and 8.4fold purified enzyme are 1.8 and 15.1 units/mg. One unit of pepsin activity is defined as an increase of absorbance of 1.0 at 280 nm during an incubation time of 30 min at pH 3.0 and 37°C
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
2.5
3.5
additional information
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.5 - 3.5
-
N,N-dimethylhemoglobin, pH 0.5: about 30% of maximum activity, pH 3.5: about 15% of maximum activity
0.5 - 5
-
N,N-dimethylcasein, pH 0.5: about 35% of maximum activity, pH 5.0: about 20% of maximum activity
1 - 3.5
1 - 4
pH 1.0: about 70% of maximal activity, pH 4.0: about 50% of maximal activity
1.5 - 4
-
pH 1.5: about 75% of maximum activity, pH 4.0: about 30% of maximum activity
1.5 - 4.5
2.5 - 4
-
pH 2.5: about 55% of maximal activity, pH 4.0: about 55% of maximal activity
3.5 - 5
50% activity is retained at pH 5.0 At pH 6.0, the enzyme shows no activity
additional information
1 - 3.5
pH 1.0: about 85% of maximal activity, pH 3.5: about 40% of maximal activity
1.5 - 4.5
-
pH 1.5: about 90% of maximum activity, pH 4.5: about 35% of maximum activity
1.5 - 4.5
-
pH 1.5: about 90% of maximum activity, pH 4.5: about 35% of maximum activity
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
42
42 - 50
maximum activity is observed at temperatures between 42 and 50°C, decreasing so drastically above 50°C that complete loss of activity is detected at 60°C
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20 - 55
-
20°C: about 40% of maximal activity, 55°C: about 60% of maximal activity
25 - 50
25°C: about 70% of maximal activity, 50°C: about 90% of maximal activity
25 - 60
25°C: about 50% of maximal activity, 60°C: about 10% of maximal activity
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
processing of sonic hedgehog in the normal stomach is hormonally regulated, acid-dependent, and mediated by the aspartic protease pepsin A. Parietal cell atrophy, a known preneoplastic lesion, correlates with loss of sonic hedgehog processing
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PDB
SCOP
CATH
UNIPROT
ORGANISM
Homo sapiens;
Sus scrofa;
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
32000
34000
35000
36000
43000
additional information
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
?
x * 30000, pepsin isoform P1, SDS-PAGE; x * 35000, pepsinogen isoform PG1, SDS-PAGE
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
proteolytic modification
side-chain modification
proteolytic modification
-
activation of pepsinogen to pepsin occurs between pH 1.0 and pH 4.0 for wild-type, between pH 1.0 and pH 6.0 for N-glycosylated mutants
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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
crystallization in presence of dimethyl sulfoxide. One dimethyl sulfoxide molecule occupies a site on the surface of enzyme interacting with two of its residues. In crystal structure, conformation of enzyme remains unchanged. In solution, dimethyl sulfoxide causes a slight change in secondary structure and complete loss of activity
-
hanging-drop vapour diffusion method, crystal structure of the complex between pepsin inhibitor-3 and the enzyme at 1.75 A and at 2.45 A resolution. In the enzyme-inhibitor complex, the N-terminal beta-strand of pepsin inhibitor-3 pairs with one strand of the active site flap (residues 70-82) of pepsin, thus forming an eight-stranded beta-sheet that spans the two proteins
-
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
2.2 - 5.9
-
45°C, pH 2.16: 7% loss of activity after 40 min, pH 5.93: 12% loss of activity after 40 min
36733
3 - 10
-
pepsin A is completely inactivated at pH 3.0-10.0 at 37°C after 30 days, the enzyme is unstable at pH 7.0 and above (irreversible inhibition)
717394
additional information
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
38.8
-
melting point of wild-type. For glycosylated mutants, melting point increases by 5-17 degrees
50
50
pH 5.3, half-life: 270 min; pH 5.3, half-life: 72 min
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ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
1,4-dioxane
-
incubation for 20 min at pH 2 and 25°C, the enzyme retains its activity in aqueous 1,4-dioxane with increasing organic solvent concentration up to 30%
acetonitrile
-
incubation for 20 min at pH 2 and 25°C, the enzyme retains its activity in aqueous acetonitrile with increasing organic solvent concentration up to 60%
Ethanol
-
incubation for 20 min at pH 2 and 25°C, the enzyme retains its activity in aqueous ethanol with increasing organic solvent concentration up to 60%
guanidine-HCl
-
pepsin A is stable up to 3.6 M and inactivated at 5 M guanidine-HCl
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
affinity chromatography of pepsin and pepsinogen using immobilized ligands derived from the specific substrate for this enzyme, optimum conditions of an interaction of the enzyme and its zymogen with immobilized ligands derived from the enzyme substrate: N-acetyl-L-Phe-3,5-diiodo-L-tyrosine
-
ammonium sulfate precipitation, DEAE-Sephacel column chromatography, and Sephacryl S-200 gel filtration
ammonium sulfate precipitation, DEAE-Sephacel gel filtration, and Sephacryl S-200 gel filtration
-
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
overexpression in Escherichia coli; overexpression in Escherichia coli
wild-type, D32E, D215E, and D32E/D215E thioredoxin-pepsinogen fusion proteins are expressed in Escherichia coli GI724
-
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
L291S
-
replacement of a pepsin A-specific residue by a chymosin-specific one. Decrease in hydrolysis of peptides with hydrophobic/aromatic residues at P’1 site, increase in hydrolysis of peptides with charged residues at P’1
L291S/L298Q
-
replacement of a pepsin A-specific residue by a chymosin-specific one. Decrease in hydrolysis of peptides with hydrophobic/aromatic residues at P’1 site, increase in hydrolysis of peptides with charged residues at P’1
L298Q
-
replacement of a pepsin A-specific residue by a chymosin-specific one. Decrease in hydrolysis of peptides with hydrophobic/aromatic residues at P’1 site, increase in hydrolysis of peptides with charged residues at P’1
M289D
-
replacement of a pepsin A-specific residue by a chymosin-specific one. Decrease in hydrolysis of peptides with hydrophobic/aromatic residues at P’1 site, increase in hydrolysis of peptides with charged residues at P’1
D37A
the mutant is completely inactive towards the fluorogenic substrate Mca-KKPAEFFALK-Dnp at pH 4.0
D215E
-
unlike wild-type, the mutant fusion protein is incapable of autocatalytic activation upon acidification of the medium, as determined by Western blot analysis. Mature mutant pepsin is obtained by processing fusion protein samples through an immobilized pepsin column. Tm-value of mutant enzyme is 65°C compared to 71°C for wild-type enzyme. The pH activity profiles of wild-type and mutant pepsin is similar. Mutant enzyme has a stronger affinity for the synthetic substrate KPAEFF(NO2)AL. Turnover number for mutant enzyme is significantly lower than that of the wild-type. kcat/Km is 1.9fold lower than wild-type value
D32E
-
unlike wild-type, the mutant fusion protein is incapable of autocatalytic activation upon acidification of the medium, as determined by Western blot analysis. Mature mutant pepsin is obtained by processing fusion protein samples through an immobilized pepsin column. Tm-value of mutant enzyme is 63°C compared to 71°C for wild-type enzyme. Pronounced decrease in activity below pH 2.5. Mutant enzyme has a stronger affinity for the synthetic substrate KPAEFF(NO2)AL. Turnover number for mutant enzyme is significantly lower than that of the wild-type. kcat/Km is 8.7fold lower than wild-type value
D32E/D215E
-
unlike wild-type, the mutant fusion protein is incapable of autocatalytic activation upon acidification of the medium, as determined by Western blot analysis. Mature mutant pepsin is obtained by processing fusion protein samples through an immobilized pepsin column. Tm-value of mutant enzyme is 63°C compared to 71°C for wild-type enzyme. The pH activity profiles of wild-type and mutant pepsin is similar. KM-value for KPAEFF(NO2)AL is not significantly different relative to wild-type. Turnover number for mutant enzyme is significantly lower than that of the wild-type. kcat/Km is fold lower than wild-type value. kcat/Km is 13.3fold lower than wild-type value
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
E244N/V246T
-
introduction of N-glycosylation site. Glycosylated mutant shows similar KM-value and substrate specificity as wild-type, but reduced catalytic efficiency
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
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
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
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
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
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
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
G76A
-
mutant enzyme with lower catalytic efficiency and is activated more slowly than the wild-type enzyme. The slower activation process is associated directly with altered proteolytic activity
G76S
-
mutant enzyme with lower catalytic efficiency and is activated more slowly than the wild-type enzyme. The slower activation process is associated directly with altered proteolytic activity
G76V
-
mutant enzyme with lower catalytic efficiency and is activated more slowly than the wild-type enzyme. The slower activation process is associated directly with altered proteolytic activity
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
S110N/L112T
-
introduction of N-glycosylation site. Glycosylated mutant shows similar KM-value and substrate specificity as wild-type, but reduced catalytic efficiency
S196R/D200G/E202K
-
inactivation rate at pH 7.0 is 86% of that of the wild-type value
S281N
-
introduction of N-glycosylation site. Glycosylated mutant shows similar KM-value and substrate specificity as wild-type, but reduced catalytic efficiency
S46K/D52N/N54K/Q55R/D60K
-
inactivation rate at pH 7.0 is 91% of that of the wild-type value
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
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
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
T77D/G78(S)S79
-
double mutant, differences in substrate specificity and catalytic activity
T77N
-
introduction of N-glycosylation site. Glycosylated mutant shows similar KM-value and substrate specificity as wild-type, but reduced catalytic efficiency
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Renatured/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
acid refolded pepsin has secondary and tertiary structures intermediate between the alkaline denatured and native forms but is thermodynamically stable relative to the native state. The acid refolded state of pepsin is dependent on the protein concentration during refolding. Both the secondary and tertiary structures of concentrated-refolded pepsin are native-like, in contrast to the intermediate nature of acid refolded pepsin, refolded under dilute concentration. Despite a native-like conformation, concentrated-refolded pepsin is more stable and has substantially reduced activity compared to that of the native state, suggesting that the protein is misfolded. It is proposed that the stable but misfolded, acid-refolded states are evidence that pepsin in its native conformation is metastable
-
renaturation of the supernatant containing pepsinogen A1 is achieved by a 200fold dilution of the denaturant in 100 mm Tris/HCl buffer (pH 8.0); renaturation of the supernatant containing pepsinogen A2 is achieved by a 200fold dilution of the denaturant in 100 mm Tris/HCl buffer (pH 8.0)
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
-
combined use of a theoretical model that relates electrophoretic behaviour of peptides to their sequence together with capillary electrophoresis-mass spectrometry to characterize the cleavage specificity of recombinant enzymes. Characterization of a protein lysate using recombinant and natural pepsin
food industry
-
treatment with pepsin at pH 4.0 results in lowering the (pseudo)peroxidase activity of metmyoglobin both at physiological pH and at meat pH, leading to strongly enhanced prooxidative effect of mildly proteolyzed metmyoglobin on lipid oxidation
medicine
nutrition
synthesis
-
comparison of hydrolysis kinetics of hemoglobin after immobilization of enzyme on aluminium oxide and on 2-ethanolamine-O-phosphate-modified acidic alumina. Modified alumina results in comparatively less adsorption of peptides and complete adsorption of heme
medicine
-
for elucidation and diagnosis of the allergic potential of egg white ovomucoid, the combination of digestibility studies by simulated gastric fluid and human IgE-binding experiments is useful
medicine
-
correlation of protein allergen digestion in simulated gastric fluid with that in actual gastric fluid. Digestion of peanut allergen Ara h 1 with pepsin and porcine gastric fluid results in virtually identical hydrolysis patterns
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
nutrition
-
treatment with pepsin at pH 4.0 results in lowering the (pseudo)peroxidase activity of metmyoglobin both at physiological pH and at meat pH, leading to strongly enhanced prooxidative effect of mildly proteolyzed metmyoglobin on lipid oxidation
nutrition
-
role for proteolysis in killing of bacteria. Addition of enzyme alone or in gastric juice at pH 3.5 reduces viability of suspensions of Escherichia coli 690 and K-12 by 100% after 100 min incubation. With Helicobacter pylori, viable counts decrease by 50% after 20 min
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LINKS TO OTHER DATABASES (specific for EC-Number 3.4.23.1)
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