3.4.23.1: pepsin A
This is an abbreviated version!
For detailed information about pepsin A, go to the full flat file.
Word Map on EC 3.4.23.1
-
3.4.23.1
-
gastric
-
mucosa
-
porcine
-
ulcer
-
pylori
-
helicobacter
-
stomach
-
gastritis
-
proteinases
-
peptic
-
juice
-
chymosin
-
atrophic
-
zymogen
-
pepstatin
-
reflux
-
isozymogens
-
gastricsin
-
endoscopy
-
omeprazole
-
progastricsins
-
prosegment
-
fundic
-
pentagastrin
-
prochymosins
-
milk-clotting
-
medicine
-
synthesis
-
abomasum
-
hypergastrinaemia
-
nutrition
-
pylori-positive
-
analysis
-
food industry
- 3.4.23.1
- gastric
- mucosa
- porcine
- ulcer
- pylori
- helicobacter
- stomach
- gastritis
- proteinases
-
peptic
- juice
- chymosin
-
atrophic
- zymogen
- pepstatin
- reflux
-
isozymogens
- gastricsin
-
endoscopy
- omeprazole
- progastricsins
- prosegment
-
fundic
- pentagastrin
- prochymosins
-
milk-clotting
- medicine
- synthesis
- abomasum
-
hypergastrinaemia
- nutrition
-
pylori-positive
- analysis
- food industry
Reaction
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, P-III, pep/PAG-L, pepsin, pepsin 1, pepsin A, pepsin A1, pepsin A2, pepsin D, pepsin fortior, Pepsin I/II, pepsin R, pepsinogen A, pepsinogen/PAG-Like, pepsins A1, pepsins A2, PG1, PG1-1, PG2, PG2-2, shewasin A, shewasin D
ECTree
3.4.23.1 pepsin AAdvanced search results
results (
results (Substrates Products
Substrates Products on EC 3.4.23.1 - pepsin A
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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 30°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 30°C
-
-
?
2-chlorobenzaldehyde + 1-hydroxypropan-2-one
(3R,4S)-4-(2-chlorophenyl)-3,4-dihydroxybutan-2-one
-
in MeCN buffer, at 30°C
-
-
?
2-nitrobenzaldehyde + 1,3-dihydroxypropan-2-one
(3R,4S)-1,3,4-trihydroxy-4-(2-nitrophenyl)butan-2-one
-
in MeCN buffer, at 30°C
-
-
?
2-nitrobenzaldehyde + 1-hydroxypropan-2-one
(3R,4S)-3,4-dihydroxy-4-(2-nitrophenyl)butan-2-one
-
in MeCN buffer, at 30°C
-
-
?
2-nitrobenzaldehyde + 1-methoxypropan-2-one
(3R,4S)-4-hydroxy-3-methoxy-4-(2-nitrophenyl)butan-2-one
-
in MeCN buffer, at 30°C
-
-
?
2-nitrobenzaldehyde + cyclohexanone
(2S)-2-[(R)-hydroxy(2-nitrophenyl)methyl]cyclohexan-1-one
-
in MeCN buffer, at 30°C
-
-
?
2-nitrobenzaldehyde + cyclopentanone
(2S)-2-[(R)-hydroxy(2-nitrophenyl)methyl]cyclopentan-1-one
-
in MeCN buffer, at 30°C
-
-
?
3-bromobenzaldehyde + 1-hydroxypropan-2-one
(3R,4S)-4-(3-bromophenyl)-3,4-dihydroxybutan-2-one
-
in MeCN buffer, at 30°C
-
-
?
3-methylbutanal + 1-hydroxypropan-2-one
(3R,4S)-3,4-dihydroxy-6-methylheptan-2-one
-
in MeCN buffer, at 30°C
-
-
?
3-nitrobenzaldehyde + 1-hydroxypropan-2-one
(3R,4S)-3,4-dihydroxy-4-(3-nitrophenyl)butan-2-one
-
in MeCN buffer, at 30°C
-
-
?
3-nitrobenzaldehyde + cyclohexanone
(2S)-2-[(R)-hydroxy(3-nitrophenyl)methyl]cyclohexan-1-one
-
in MeCN buffer, at 30°C
-
-
?
4-(trifluoromethyl)benzaldehyde + 1-hydroxypropan-2-one
(3R,4S)-3,4-dihydroxy-4-[4-(trifluoromethyl)phenyl]butan-2-one
-
in MeCN buffer, at 30°C
-
-
?
4-bromobenzaldehyde + 1-hydroxypropan-2-one
(3R,4S)-4-(4-bromophenyl)-3,4-dihydroxybutan-2-one
-
in MeCN buffer, at 30°C
-
-
?
4-bromobenzaldehyde + propan-2-one
(4R)-4-(4-bromophenyl)-4-hydroxybutan-2-one
-
in MeCN buffer, at 30°C
-
-
?
4-chlorobenzaldehyde + 1-(benzyloxy)propan-2-one
(3R,4S)-3-(benzyloxy)-4-(4-chlorophenyl)-4-hydroxybutan-2-one
-
in MeCN buffer, at 30°C
-
-
?
4-chlorobenzaldehyde + 1-hydroxypropan-2-one
(3R,4S)-4-(4-chlorophenyl)-3,4-dihydroxybutan-2-one
-
in MeCN buffer, at 30°C
-
-
?
4-chlorobenzaldehyde + cyclohexanone
(2S)-2-[(R)-(4-chlorophenyl)(hydroxy)methyl]cyclohexan-1-one
-
in MeCN buffer, at 30°C
-
-
?
4-chlorobenzaldehyde + cyclopentanone
(2S)-2-[(R)-(4-chlorophenyl)(hydroxy)methyl]cyclopentan-1-one
-
in MeCN buffer, at 30°C
-
-
?
4-fluorobenzaldehyde + 1-hydroxypropan-2-one
(3R,4S)-4-(4-fluorophenyl)-3,4-dihydroxybutan-2-one
-
in MeCN buffer, at 30°C
-
-
?
4-formylbenzonitrile + 1-hydroxypropan-2-one
4-[(1S,2R)-1,2-dihydroxy-3-oxobutyl]benzonitrile
-
in MeCN buffer, at 30°C
-
-
?
4-methylbenzaldehyde + 1-hydroxypropan-2-one
(3R,4S)-3,4-dihydroxy-4-(4-methylphenyl)butan-2-one
-
in MeCN buffer, at 30°C
-
-
?
4-nitrobenzaldehyde + 1,3-dihydroxypropan-2-one
(3R,4S)-1,3,4-trihydroxy-4-(4-nitrophenyl)butan-2-one
-
in MeCN buffer, at 30°C
-
-
?
4-nitrobenzaldehyde + 1-(benzyloxy)propan-2-one
(3R,4S)-3-(benzyloxy)-4-hydroxy-4-(4-nitrophenyl)butan-2-one
-
in MeCN buffer, at 30°C
-
-
?
4-nitrobenzaldehyde + 1-hydroxypropan-2-one
(3R,4S)-3,4-dihydroxy-4-(4-nitrophenyl)butan-2-one
-
in MeCN buffer, at 30°C
-
-
?
4-nitrobenzaldehyde + 1-methoxypropan-2-one
(3R,4S)-4-hydroxy-3-methoxy-4-(4-nitrophenyl)butan-2-one
-
in MeCN buffer, at 30°C
-
-
?
4-nitrobenzaldehyde + cyclohexanone
(2S)-2-[(R)-hydroxy(4-nitrophenyl)methyl]cyclohexan-1-one
-
in MeCN buffer, at 30°C
-
-
?
4-nitrobenzaldehyde + cyclopentanone
(2S)-2-[(R)-hydroxy(4-nitrophenyl)methyl]cyclopentan-1-one
-
in MeCN buffer, at 30°C
-
-
?
4-nitrobenzaldehyde + oxan-4-one
(3S)-3-[(R)-hydroxy(4-nitrophenyl)methyl]oxan-4-one
-
in MeCN buffer, at 30°C
-
-
?
4-nitrobenzaldehyde + propan-2-one
(4R)-4-hydroxy-4-(4-nitrophenyl)butan-2-one
-
in MeCN buffer, at 30°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 30°C
-
-
?
4-nitrobenzaldehyde + thian-4-one
(3S)-3-[(R)-hydroxy(4-nitrophenyl)methyl]thian-4-one
-
in MeCN buffer, at 30°C
-
-
?
benzaldehyde + 1-hydroxypropan-2-one
(3R,4S)-3,4-dihydroxy-4-phenylbutan-2-one
-
in MeCN buffer, at 30°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 30°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 30°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 30°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 P1 site of substrate
-
-
?
additional information
?
-
-
pepsin A strongly prefers a hydrophobic/aromatic residue at P1 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 P1 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
-
-
?
