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

Advanced search results

Do not include text mining results

Include results (more...)

Include results (more...)

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]

Renatured

print visible entries

print all entries

Go back to the abbreviated version
of the Enzyme Summary Page.

Renatured on EC 3.4.23.1 - pepsin A

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.

top print hide Go to Renatured Search

Please wait a moment until the data is sorted. This message will disappear when the data is sorted.

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

Sus scrofa

-

678165

alkaline denatured pepsin

Sus scrofa

-

711237

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)

Trematomus bernacchii

Q6HA04, Q6HA05

679796

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)

Trematomus bernacchii

Q6HA04, Q6HA05

679796