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3.4.23.2: pepsin B

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

Word Map on EC 3.4.23.2

Reaction

degradation of gelatin; little activity on hemoglobin. Specificity on B chain of insulin additional information restricted than that of pepsin A; does not cleave at Phe1-Val, Gln4-His or Gly23-Phe =

Synonyms

EC 3.4.4.2, gelatinase, More, parapepsin I, pepsin, Pepsina Suina TS

ECTree

     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.23 Aspartic endopeptidases
                3.4.23.2 pepsin B

Engineering

Engineering on EC 3.4.23.2 - pepsin B

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
F219S
mutant exhibits broad activity against various peptides, with retention of high activity against peptides with Gly at P2
Y13A
mutant shows new hydrolytic activity against several peptides, whereas the activity against peptides with Gly at P2 is decreased significantly. The newly obtained activity of the Tyr13Ala mutant is low
Y13A/F219S
mutant demonstrats general proteolytic activity, hydrolyzing various types of peptides very efficiently, although activity against peptides with Gly at P2 is decreased. The activity against typical peptides, such as KPAEFARL, KPAEFLRL, and KPGEFARL, is increased about 40times by the double mutation. The extent being much higher than that with single mutations
L287G
-
the mutation leads to a significant decrease in proteolytic activity. The mutant show an increase in the ratio of clotting activity to proteolytic activity compared to the wild type enzyme
T218A
-
the mutation leads to a significant decrease in proteolytic activity
T218S