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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

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

pH Range

pH Range on EC 3.4.23.1 - pepsin A

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pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
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 - 3.5
-
highly active between pH 1.5-3.5
1.5 - 4
-
pH 1.5: about 75% of maximum activity, pH 4.0: about 30% of maximum activity
1.5 - 4.5
1.6 - 2.2
-
-
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
2.1 - 4.5
-
pH optimum for selective digestion of collagen telopeptides
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