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Information on EC 3.4.23.1 - pepsin A
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3.4.23.1 pepsin ASpecify your search results
Word Map
- 3.4.23.1
- gastric
- mucosa
- porcine
- helicobacter
- ulcer
- stomach
- pylori
- gastritis
- juice
- proteinases
-
peptic
- pepstatin
- reflux
-
atrophic
- chymosin
- zymogen
-
endoscopy
- gastricsin
- omeprazole
-
isozymogens
- progastricsins
- prochymosins
-
fundic
- pentagastrin
-
milk-clotting
- prosegment
- abomasum
-
hypergastrinaemia
- synthesis
- analysis
-
pylori-positive
- medicine
- food industry
- nutrition
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Reaction Schemes
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
Synonyms
Aspartic proteinase, EC 3.4.4.1, elixir lactate of pepsin, fundus-pepsin, lactated pepsin, lactated pepsin elixir, P I, P-Ia, P-Ib, P-II, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
EC 3.4.4.1
-
-
formerly
-
elixir lactate of pepsin
-
-
-
-
fundus-pepsin
-
-
-
-
lactated pepsin
-
-
-
-
lactated pepsin elixir
-
-
-
-
P I
-
-
-
-
pepsin
pepsin 1
pepsin A
pepsin D
-
-
-
-
pepsin fortior
-
-
-
-
Pepsin I/II
-
-
-
-
pepsin R
-
-
-
-
PG1
pepsin
-
-
-
-
pepsin
-
-
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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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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
((7-methoxycoumarin-4-yl)acetyl)-Lys-Lys-Pro-Ala-Glu-Phe-Phe-Ala-Leu-Lys-(2,4-dinitrophenyl) + H2O
((7-methoxycoumarin-4-yl)acetyl)-Lys-Lys-Pro-Ala-Glu-Phe + Phe-Ala-Leu-Lys-(2,4-dinitrophenyl)
-
-
-
?
(R)-(+)-2,2-dimethyl-1,3-dioxolane-4-carbaldehyde + 1,3-dihydroxypropan-2-one
(3R,4R)-4-(2,2-dimethyl-1,3-dioxolan-4-yl)-1,3,4-trihydroxybutan-2-one
-
in MeCN buffer, at 30ĆĀ°C
-
-
?
2 pQLSK-(7-methoxycoumarin-4-yl)-GYDEKSTGISK-[Nepsilon-(2,4-dinitrophenyl)]-P-NH2 + 2 H2O
pQLSK-(7-methoxycoumarin-4-yl)-GYDEKSTG + ISK-[Nepsilon-(2,4-dinitrophenyl)]-P-NH2 + pQLSK-(7-methoxycoumarin-4-yl)-GY + DEKSTGISK-[Nepsilon-(2,4-dinitrophenyl)]-P-NH2
-
-
-
-
?
2,6-dichlorobenzaldehyde + 1-hydroxypropan-2-one
(3R,4S)-4-(2,6-dichlorophenyl)-3,4-dihydroxybutan-2-one
-
in MeCN buffer, at 30ĆĀ°C
-
-
?
2-chlorobenzaldehyde + 1-hydroxypropan-2-one
(3R,4S)-4-(2-chlorophenyl)-3,4-dihydroxybutan-2-one
-
in MeCN buffer, at 30ĆĀ°C
-
-
?
2-nitrobenzaldehyde + 1,3-dihydroxypropan-2-one
(3R,4S)-1,3,4-trihydroxy-4-(2-nitrophenyl)butan-2-one
-
in MeCN buffer, at 30ĆĀ°C
-
-
?
2-nitrobenzaldehyde + 1-hydroxypropan-2-one
(3R,4S)-3,4-dihydroxy-4-(2-nitrophenyl)butan-2-one
-
in MeCN buffer, at 30ĆĀ°C
-
-
?
2-nitrobenzaldehyde + 1-methoxypropan-2-one
(3R,4S)-4-hydroxy-3-methoxy-4-(2-nitrophenyl)butan-2-one
-
in MeCN buffer, at 30ĆĀ°C
-
-
?
2-nitrobenzaldehyde + cyclohexanone
(2S)-2-[(R)-hydroxy(2-nitrophenyl)methyl]cyclohexan-1-one
-
in MeCN buffer, at 30ĆĀ°C
-
-
?
2-nitrobenzaldehyde + cyclopentanone
(2S)-2-[(R)-hydroxy(2-nitrophenyl)methyl]cyclopentan-1-one
-
in MeCN buffer, at 30ĆĀ°C
-
-
?
3-bromobenzaldehyde + 1-hydroxypropan-2-one
(3R,4S)-4-(3-bromophenyl)-3,4-dihydroxybutan-2-one
-
in MeCN buffer, at 30ĆĀ°C
-
-
?
3-methylbutanal + 1-hydroxypropan-2-one
(3R,4S)-3,4-dihydroxy-6-methylheptan-2-one
-
in MeCN buffer, at 30ĆĀ°C
-
-
?
3-nitrobenzaldehyde + 1-hydroxypropan-2-one
(3R,4S)-3,4-dihydroxy-4-(3-nitrophenyl)butan-2-one
-
in MeCN buffer, at 30ĆĀ°C
-
-
?
3-nitrobenzaldehyde + cyclohexanone
(2S)-2-[(R)-hydroxy(3-nitrophenyl)methyl]cyclohexan-1-one
-
in MeCN buffer, at 30ĆĀ°C
-
-
?
4-(trifluoromethyl)benzaldehyde + 1-hydroxypropan-2-one
(3R,4S)-3,4-dihydroxy-4-[4-(trifluoromethyl)phenyl]butan-2-one
-
in MeCN buffer, at 30ĆĀ°C
-
-
?
4-bromobenzaldehyde + 1-hydroxypropan-2-one
(3R,4S)-4-(4-bromophenyl)-3,4-dihydroxybutan-2-one
-
in MeCN buffer, at 30ĆĀ°C
-
-
?
4-bromobenzaldehyde + propan-2-one
(4R)-4-(4-bromophenyl)-4-hydroxybutan-2-one
-
in MeCN buffer, at 30ĆĀ°C
-
-
?
4-chlorobenzaldehyde + 1-(benzyloxy)propan-2-one
(3R,4S)-3-(benzyloxy)-4-(4-chlorophenyl)-4-hydroxybutan-2-one
-
in MeCN buffer, at 30ĆĀ°C
-
-
?
4-chlorobenzaldehyde + 1-hydroxypropan-2-one
(3R,4S)-4-(4-chlorophenyl)-3,4-dihydroxybutan-2-one
-
in MeCN buffer, at 30ĆĀ°C
-
-
?
4-chlorobenzaldehyde + cyclohexanone
(2S)-2-[(R)-(4-chlorophenyl)(hydroxy)methyl]cyclohexan-1-one
-
in MeCN buffer, at 30ĆĀ°C
-
-
?
4-chlorobenzaldehyde + cyclopentanone
(2S)-2-[(R)-(4-chlorophenyl)(hydroxy)methyl]cyclopentan-1-one
-
in MeCN buffer, at 30ĆĀ°C
-
-
?
4-fluorobenzaldehyde + 1-hydroxypropan-2-one
(3R,4S)-4-(4-fluorophenyl)-3,4-dihydroxybutan-2-one
-
in MeCN buffer, at 30ĆĀ°C
-
-
?
4-formylbenzonitrile + 1-hydroxypropan-2-one
4-[(1S,2R)-1,2-dihydroxy-3-oxobutyl]benzonitrile
-
in MeCN buffer, at 30ĆĀ°C
-
-
?
4-methylbenzaldehyde + 1-hydroxypropan-2-one
(3R,4S)-3,4-dihydroxy-4-(4-methylphenyl)butan-2-one
-
in MeCN buffer, at 30ĆĀ°C
-
-
?
4-nitrobenzaldehyde + 1,3-dihydroxypropan-2-one
(3R,4S)-1,3,4-trihydroxy-4-(4-nitrophenyl)butan-2-one
-
in MeCN buffer, at 30ĆĀ°C
-
-
?
4-nitrobenzaldehyde + 1-(benzyloxy)propan-2-one
(3R,4S)-3-(benzyloxy)-4-hydroxy-4-(4-nitrophenyl)butan-2-one
-
in MeCN buffer, at 30ĆĀ°C
-
-
?
4-nitrobenzaldehyde + 1-hydroxypropan-2-one
(3R,4S)-3,4-dihydroxy-4-(4-nitrophenyl)butan-2-one
-
in MeCN buffer, at 30ĆĀ°C
-
-
?
4-nitrobenzaldehyde + 1-methoxypropan-2-one
(3R,4S)-4-hydroxy-3-methoxy-4-(4-nitrophenyl)butan-2-one
-
in MeCN buffer, at 30ĆĀ°C
-
-
?
4-nitrobenzaldehyde + cyclohexanone
(2S)-2-[(R)-hydroxy(4-nitrophenyl)methyl]cyclohexan-1-one
-
in MeCN buffer, at 30ĆĀ°C
-
-
?
4-nitrobenzaldehyde + cyclopentanone
(2S)-2-[(R)-hydroxy(4-nitrophenyl)methyl]cyclopentan-1-one
-
in MeCN buffer, at 30ĆĀ°C
-
-
?
4-nitrobenzaldehyde + oxan-4-one
(3S)-3-[(R)-hydroxy(4-nitrophenyl)methyl]oxan-4-one
-
in MeCN buffer, at 30ĆĀ°C
-
-
?
4-nitrobenzaldehyde + propan-2-one
(4R)-4-hydroxy-4-(4-nitrophenyl)butan-2-one
-
in MeCN buffer, at 30ĆĀ°C
-
-
?
4-nitrobenzaldehyde + tert-butyl 4-oxopiperidine-1-carboxylate
tert-butyl (3S)-3-[(R)-hydroxy(4-nitrophenyl)methyl]-4-oxopiperidine-1-carboxylate
-
in MeCN buffer, at 30ĆĀ°C
-
-
?
4-nitrobenzaldehyde + thian-4-one
(3S)-3-[(R)-hydroxy(4-nitrophenyl)methyl]thian-4-one
-
in MeCN buffer, at 30ĆĀ°C
-
-
?
benzaldehyde + 1-hydroxypropan-2-one
(3R,4S)-3,4-dihydroxy-4-phenylbutan-2-one
-
in MeCN buffer, at 30ĆĀ°C
-
-
?
benzyloxycarbonyl-Gly-Gly-Phe-Phe 3-(4-pyridyl)propyl ester + H2O
benzyloxycarbonyl-Gly-Gly-Phe + Phe 3-(4-pyridyl)propyl ester
-
-
-
-
?
benzyloxycarbonyl-Gly-Phe-Phe 3-(4-pyridyl)propyl ester + H2O
benzyloxycarbonyl-Gly-Phe + Phe 3-(4-pyridyl)propyl ester
-
-
-
-
?
benzyloxycarbonyl-His-Phe(NO2)-beta-phenyl-L-lactyl-O-methyl ester + H2O
benzyloxycarbonyl-His-Phe(NO2) + phenyl-L-lactyl-O-methyl ester
benzyloxycarbonyl-Phe-Phe 3-(4-pyridyl)propyl ester + H2O
benzyloxycarbonyl-Phe + Phe 3-(4-pyridyl)propyl ester
-
-
-
-
?
bovine type I collagen + H2O
?
-
pepsin cleaves type I collagen at various sites in the N-terminal and in the C-terminal telopeptides
-
-
?
bovine type I collagen alpha1 chain + H2O
pQLSYGY + pQLSYGYDEKSTG
-
the enzyme preferentially cleaves Tyr6-Asp7 and less preferentially Gly12-Ile13
-
-
?
cinnamaldehyde + 1,4-dithiane-2,5-diol
(2R)-2-phenyl-2,5-dihydrothiophene-3-carbaldehyde
-
asymmetric domino thia-Michael/aldol condensation in MeCN buffer, at 30ĆĀ°C
-
-
?
crude cheese whey + H2O
lactoferrin f(20-30) + beta-lactoglobulin f(14-22) + beta-lactoglobulin f(92-103) + ?
-
the porcine pepsin digests of crude cheese whey lead the production of the three peptides with antibacterial activity against Bacillus subtilis (lactoferrin f(20-30) and beta-lactoglobulin f(14-22)) and Escherichia coli (beta-lactoglobulin f(82-103))
-
-
?
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
-
?
naphthalene-1-carbaldehyde + 1-hydroxypropan-2-one
(3R,4S)-3,4-dihydroxy-4-(naphthalen-1-yl)butan-2-one
-
in MeCN buffer, at 30ĆĀ°C
-
-
?
oxidized insulin B chain + H2O
FVNQHLCGSHLVEAL + L-Tyr + LVCGERGFFYTPKA
two major cleavage sites are at Leu15-Tyr16 and Tyr16-Leu17
-
-
?
oxidized insulin B chain + H2O
FVNQHLCGSHLVEAL + YLVCGERGFFYTPKA
-
the cleavage specificities clarified with oxidized insulin B chain are restricted to a few bonds consisting of hydrophobic/aromatic residues, such as the Leu15-Tyr16, Phe24-Phe25 and Phe25-Tyr26 bonds
-
-
?
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
-
?
thiophene-2-carbaldehyde + 1-hydroxypropan-2-one
(3R,4R)-3,4-dihydroxy-4-(thiophen-2-yl)butan-2-one
-
in MeCN buffer, at 30ĆĀ°C
-
-
?
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
-
-
-
-
?
KPAEFIRL + H2O
KPAEF + IRL
best substrate for pepsin A1
-
-
?
KPAEFWRL + H2O
KPAEF + WRL
best substrate for pepsin A2
-
-
?
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 PĆ¢ĀĀ1 site of substrate
-
-
?
additional information
?
-
-
pepsin A strongly prefers a hydrophobic/aromatic residue at P1Ć¢ĀĀ in any type of peptide
-
-
?
additional information
?
-
-
amino acids set free by pepsin include tryptophan and phenylalanine. Aromatic amino acids are preferentially exposed and released by the enzyme
-
-
?
additional information
?
-
the cleavage site of isoform PG1 to produce pepsin is clearly at the 41-42 bond of Phe-Ala
-
-
?
additional information
?
-
the enzyme prefers both hydrophobic/aromatic residues and charged residues at the P'1 sites of substrates. Pepsin A1 does not prefer some hydrophobic residues such as Leu, Val, Ala and Met
-
-
?
additional information
?
-
the enzyme prefers both hydrophobic/aromatic residues and charged residues at the P'1 sites of substrates. Pepsin A1 does not prefer some hydrophobic residues such as Leu, Val, Ala and Met
-
-
?
additional information
?
-
-
the enzyme prefers both hydrophobic/aromatic residues and charged residues at the P'1 sites of substrates. Pepsin A1 does not prefer some hydrophobic residues such as Leu, Val, Ala and Met
-
-
?
additional information
?
-
the enzyme prefers both hydrophobic/aromatic residues and charged residues at the P'1 sites of substrates. Pepsin A2 does not prefer some hydrophobic residues such as Leu, Val, Ala and Met
-
-
?
additional information
?
-
the enzyme prefers both hydrophobic/aromatic residues and charged residues at the P'1 sites of substrates. Pepsin A2 does not prefer some hydrophobic residues such as Leu, Val, Ala and Met
-
-
?
additional information
?
-
-
the enzyme prefers both hydrophobic/aromatic residues and charged residues at the P'1 sites of substrates. Pepsin A2 does not prefer some hydrophobic residues such as Leu, Val, Ala and Met
-
-
?
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
?
-
no activity with ((7-methoxycoumarin-4-yl)acetyl)-Lys-Leu-His-Pro-Glu-Val-Leu-Phe-Val-Leu-Glu-Lys-(2,4-dinitrophenyl), Arg-Glu-(EDANS)-Ile-His-Pro-Phe-His-Leu-Val-Ile-His-Thr-Lys-(DABCYL)-Arg, ((7-methoxycoumarin-4-yl)acetyl)-Lys-Ser-Glu-Val-Asn-Leu-Asp-Ala-Glu-Phe-Lys-(2,4-dinitrophenyl), or ((7-methoxycoumarin-4-yl)acetyl)-Lys-Ala-Leu-Ile-Pro-Ser-Tyr-Lys-Trp-Ser-Lys-(2,4-dinitrophenyl)
-
-
?
additional information
?
-
-
no activity with ((7-methoxycoumarin-4-yl)acetyl)-Lys-Leu-His-Pro-Glu-Val-Leu-Phe-Val-Leu-Glu-Lys-(2,4-dinitrophenyl), Arg-Glu-(EDANS)-Ile-His-Pro-Phe-His-Leu-Val-Ile-His-Thr-Lys-(DABCYL)-Arg, ((7-methoxycoumarin-4-yl)acetyl)-Lys-Ser-Glu-Val-Asn-Leu-Asp-Ala-Glu-Phe-Lys-(2,4-dinitrophenyl), or ((7-methoxycoumarin-4-yl)acetyl)-Lys-Ala-Leu-Ile-Pro-Ser-Tyr-Lys-Trp-Ser-Lys-(2,4-dinitrophenyl)
-
-
?
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 P1Ć¢ĀĀ in any type of peptide
-
-
?
additional information
?
-
-
the enzyme prefers both hydrophobic/aromatic residues and charged residues at the P'1 sites of substrates. The enzyme prefers some hydrophobic residues such as Leu, Val, Ala and Met
-
-
?
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
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL 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
Proteins + H2O
?
-
enzyme formed from pepsinogen A, agent of gastric digestion in mammals and birds
-
-
?
additional information
?
-
the cleavage site of isoform PG1 to produce pepsin is clearly at the 41-42 bond of Phe-Ala
-
-
?
additional information
?
-
the enzyme prefers both hydrophobic/aromatic residues and charged residues at the P'1 sites of substrates. Pepsin A1 does not prefer some hydrophobic residues such as Leu, Val, Ala and Met
-
-
?
additional information
?
-
the enzyme prefers both hydrophobic/aromatic residues and charged residues at the P'1 sites of substrates. Pepsin A1 does not prefer some hydrophobic residues such as Leu, Val, Ala and Met
-
-
?
additional information
?
-
-
the enzyme prefers both hydrophobic/aromatic residues and charged residues at the P'1 sites of substrates. Pepsin A1 does not prefer some hydrophobic residues such as Leu, Val, Ala and Met
-
-
?
additional information
?
-
the enzyme prefers both hydrophobic/aromatic residues and charged residues at the P'1 sites of substrates. Pepsin A2 does not prefer some hydrophobic residues such as Leu, Val, Ala and Met
-
-
?
additional information
?
-
the enzyme prefers both hydrophobic/aromatic residues and charged residues at the P'1 sites of substrates. Pepsin A2 does not prefer some hydrophobic residues such as Leu, Val, Ala and Met
-
-
?
additional information
?
-
-
the enzyme prefers both hydrophobic/aromatic residues and charged residues at the P'1 sites of substrates. Pepsin A2 does not prefer some hydrophobic residues such as Leu, Val, Ala and Met
-
-
?
additional information
?
-
-
the enzyme prefers both hydrophobic/aromatic residues and charged residues at the P'1 sites of substrates. The enzyme prefers some hydrophobic residues such as Leu, Val, Ala and Met
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
acotiamide
-
the activity of pepsin decreases with the increasing concentration of acotiamide (0-0.02 mM)
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
additional information
-
not inhibited by EDTA, E-64, leupeptin, 4-(2-aminoethyl)benzenesulfonyl fluoride or aprotinin
-
additional information
not inhibited by Pefabloc, EDTA, E-64, amstatin, and dithiohtreitol
-
additional information
-
not inhibited by Pefabloc, EDTA, E-64, amstatin, and dithiohtreitol
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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 37ĆĀ°C
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00867
((7-methoxycoumarin-4-yl)acetyl)-Lys-Lys-Pro-Ala-Glu-Phe-Phe-Ala-Leu-Lys-(2,4-dinitrophenyl)
at pH 4.0 and 37ĆĀ°C
0.0000079
Acid-denatured hemoglobin
-
isoform P-III, at pH 2.0 and 37ĆĀ°C
-
0.000013
Acid-denatured hemoglobin
-
isoform P-II, at pH 2.0 and 37ĆĀ°C
-
0.000028
Acid-denatured hemoglobin
-
isoform P-I, at pH 2.0 and 37ĆĀ°C
-
0.4
benzyloxycarbonyl-Gly-Gly-Phe-Phe 3-(4-pyridyl)propyl ester
-
at pH 3.5 and 37ĆĀ°C
0.8
benzyloxycarbonyl-Gly-Gly-Phe-Phe 3-(4-pyridyl)propyl ester
-
at pH 2.0 and 37ĆĀ°C
0.4
benzyloxycarbonyl-Gly-Phe-Phe 3-(4-pyridyl)propyl ester
-
at pH 3.5 and 37ĆĀ°C
1.1
benzyloxycarbonyl-Gly-Phe-Phe 3-(4-pyridyl)propyl ester
-
at pH 2.0 and 37ĆĀ°C
0.04
benzyloxycarbonyl-Phe-Phe-OEt
-
at 43 mM ionic strength, at pH 5.5 and 37ĆĀ°C
0.055
hemoglobin
isoform pepsin 1, in 250 mM sodium acetate buffer (pH 3.0), at 37ĆĀ°C
-
0.12
hemoglobin
-
isoform pepsin 1, in 250 mM sodium acetate buffer (pH 3.0), at 37ĆĀ°C
-
0.057
KPAEFF(NO2)AL
-
pH 3.95, 37ĆĀ°C, mutant enzyme S46K/D52N/N54K/Q55R/D60K/S196R/D200G/E202K
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
0.031
LSF(NO2)-Nle-AL
-
pH 3.95, 37ĆĀ°C, mutant enzyme S46K/D52N/N54K/Q55R/D60K/S196R/D200G/E202K
0.071
Lys-Pro-Ala-Glu-Phe-Phe(p-NO2)-Ala-Leu
-
pH 2.1, 37ĆĀ°C, mutant enzyme G76V
0.085
Lys-Pro-Ala-Glu-Phe-Phe(p-NO2)-Ala-Leu
-
pH 2.1, 37ĆĀ°C, mutant enzyme G76S
0.098
Lys-Pro-Ala-Glu-Phe-Phe(p-NO2)-Ala-Leu
-
pH 2.1, 37ĆĀ°C, mutant enzyme G76A
0.025
Pro-Thr-Glu-Phe-(p-nitro-Phe)-Arg-Leu-OH
37ĆĀ°C, acidic pH
0.074
Pro-Thr-Glu-Phe-(p-nitro-Phe)-Arg-Leu-OH
37ĆĀ°C, acidic pH
additional information
additional information
-
pH-dependence of Km-value of N-trifluoroacetyl aromatic amino acids
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3.51
((7-methoxycoumarin-4-yl)acetyl)-Lys-Lys-Pro-Ala-Glu-Phe-Phe-Ala-Leu-Lys-(2,4-dinitrophenyl)
at pH 4.0 and 37ĆĀ°C
56.5
benzyloxycarbonyl-Gly-Gly-Phe-Phe 3-(4-pyridyl)propyl ester
-
at pH 2.0 and 37ĆĀ°C
71.8
benzyloxycarbonyl-Gly-Gly-Phe-Phe 3-(4-pyridyl)propyl ester
-
at pH 3.5 and 37ĆĀ°C
2.2
benzyloxycarbonyl-Gly-Phe-Phe 3-(4-pyridyl)propyl ester
-
at pH 2.0 and 37ĆĀ°C
3.1
benzyloxycarbonyl-Gly-Phe-Phe 3-(4-pyridyl)propyl ester
-
at pH 3.5 and 37ĆĀ°C
0.08
benzyloxycarbonyl-Phe-Phe-OEt
-
at 43 mM ionic strength, at pH 5.5 and 37ĆĀ°C
7.34
hemoglobin
isoform pepsin 1, in 250 mM sodium acetate buffer (pH 3.0), at 37ĆĀ°C
-
23.2
hemoglobin
-
isoform pepsin 1, in 250 mM sodium acetate buffer (pH 3.0), at 37ĆĀ°C
-
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
37ĆĀ°C, acidic pH
3.32
Pro-Thr-Glu-Phe-(p-nitro-Phe)-Arg-Leu-OH
37ĆĀ°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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
400
((7-methoxycoumarin-4-yl)acetyl)-Lys-Lys-Pro-Ala-Glu-Phe-Phe-Ala-Leu-Lys-(2,4-dinitrophenyl)
at pH 4.0 and 37ĆĀ°C
2000
Lys-Pro-Ala-Glu-Phe-Phe(NO2)-Ala-Leu
-
pH not specified in the publication, temperature not specified in the publication
2400000
Acid-denatured hemoglobin
-
isoform P-III, at pH 2.0 and 37ĆĀ°C
-
70.6
benzyloxycarbonyl-Gly-Gly-Phe-Phe 3-(4-pyridyl)propyl ester
-
at pH 2.0 and 37ĆĀ°C
180
benzyloxycarbonyl-Gly-Gly-Phe-Phe 3-(4-pyridyl)propyl ester
-
at pH 3.5 and 37ĆĀ°C
7.8
benzyloxycarbonyl-Gly-Phe-Phe 3-(4-pyridyl)propyl ester
-
at pH 3.5 and 37ĆĀ°C
2.65
benzyloxycarbonyl-Phe-Phe-OEt
-
at 43 mM ionic strength, at pH 5.5 and 37ĆĀ°C
130
hemoglobin
isoform pepsin 1, in 250 mM sodium acetate buffer (pH 3.0), at 37ĆĀ°C
-
190
hemoglobin
-
isoform pepsin 1, in 250 mM sodium acetate buffer (pH 3.0), at 37ĆĀ°C
-
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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IC50 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 37ĆĀ°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 37ĆĀ°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 - 6
-
trout pepsins exhibit the highest enzyme activity at pH 3.0 (isoform P-I) and 2.5 (isoforms P-II and P-III); P-I shows a broad optimum in the pH range from 1.5 to 4.0, while the optima for P-II and III are restricted to the pH range from 2.0 to 3.0.at pH 4.0. Isoform P-I retains 94% activity, while isoforms P-II 72 and P-III have 65% activity. All three isoforms show residual activity of about 20% at pH 6.0
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
-
with serum albumin as a substrate, the enzyme retains 70% of its activity at pH 4.0 and almost 40% at pH 5.0
2.5 - 4
-
pH 2.5: about 55% of maximal activity, pH 4.0: about 55% of maximal activity
3 - 5
maximum activity towards this substrate at pH values between pH 3.5 and 4.0, with a drastic decrease in activity of 50% and 70% at pH values 3.0 and 5.0, respectively
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
40
42
42 - 50
maximum activity is observed at temperatures between 42 and 50ĆĀ°C, decreasing so drastically above 50ĆĀ°C that complete loss of activity is detected at 60ĆĀ°C
50
40
-
the activity of pepsin isoform 1 is largely lost at higher than 50ĆĀ°C
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
10 - 40
maximum enzyme activity is detected between 30ĆĀ°C and 37ĆĀ°C. Above this temperature the activity abruptly decreases, with no detectable activity remaining at 50ĆĀ°C. At lower temperatures the activity decreases gradually, with the enzyme retaining 30% activity at 10ĆĀ°C
20 - 55
-
20ĆĀ°C: about 40% of maximal activity, 55ĆĀ°C: about 60% of maximal activity
25 - 50
25ĆĀ°C: about 70% of maximal activity, 50ĆĀ°C: about 90% of maximal activity
25 - 60
25ĆĀ°C: about 50% of maximal activity, 60ĆĀ°C: about 10% of maximal activity
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
brenda
-
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, 753031, 753326, 753632, 753846, 753865
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
-
secretions from the trachea, lung, nose, sinus, middle ear, and exhaled breath condensate
brenda
-
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
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
-
the enzyme responsible for protein digestion in the stomach
Show AA Sequence and Transmembrane Helices (145 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
32000
34000
35000
36000
43000
additional information