3.4.23.1: pepsin A

This is an abbreviated version!
For detailed information about pepsin A, go to the full flat file.

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 Hydrolases

         3.4 Acting on peptide bonds (peptidases)

             3.4.23 Aspartic endopeptidases

                3.4.23.1 pepsin A

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Results	in table
3	Activating Compound
154	AA Sequence
10	Application
1	CAS Registry Number
11	Cloned(Commentary)
11	Crystallization (Commentary)
2972	Disease/ Diagnostics
1	General Information
3	General Stability
10	IC50 Value
151	Inhibitors
46	kcat/KM [mM/s]
5	Ki Value [mM]
145	KM Value [mM]
1	Localization
3	Metals/Ions
30	Molecular Weight [Da]
11	Natural Substrates/ Products (Substrates)
6	Organic Solvent Stability
124	Organism
23	PDB ID
51	pH Optimum
25	pH Range
24	pH Stability
11	pI Value
8	Posttranslational Modification
34	Protein Variants
40	Purification (Commentary)
1	Reaction
1	Reaction Type
121	Reference
4	Renatured (Commentary)
49	Source Tissue
10	Specific Activity [micromol/min/mg]
4	Storage Stability
235	Substrates and Products (Substrate)
25	Subunits
58	Synonyms
25	Temperature Optimum [°C]
7	Temperature Range [°C]
10	Temperature Stability [°C]
136	Turnover Number [1/s]

Application

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Application on EC 3.4.23.1 - pepsin A

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APPLICATION

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

analysis

Bos taurus

-

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

667196

food industry

2 entries

medicine

3 entries

nutrition

3 entries

synthesis

Sus scrofa

-

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

668029

food industry

Sus scrofa

-

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

669014

food industry

Sus scrofa

-

the porcine pepsin digests of cheese whey at a specific acidic pH have the potential to be used as natural food preservatives due to the presence 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))

754495

medicine

Sus scrofa

-

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

669034

medicine

Sus scrofa

-

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

668952

medicine

Homo sapiens

-

the enzyme is a biomarker of gastric reflux into the esophagus, airways, and lungs

752496

nutrition

Sus scrofa

-

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

653827

nutrition

Sus scrofa

-

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

669817

nutrition

Sus scrofa

-

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

669014