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Pepsin exhibits a broad cleavage specificity. Pepsin will digest up to 20% of ingested amide bonds. [18] Residues in the P1 and P1' positions [19] are most important in determining cleavage probability. Generally, hydrophobic amino acids at P1 and P1' positions increase cleavage probability.
Preferential cleavage: hydrophobic, preferably aromatic, residues in P1 and P1' positions. Cleaves Phe 1-Val, Gln 4-His, Glu 13-Ala, Ala 14-Leu, Leu 15-Tyr, Tyr 16-Leu, Gly 23-Phe, Phe 24-Phe and Phe 25-Tyr bonds in the B chain of insulin. The enzyme is a predominant endopeptidase in the gastric juice of vertebrates. See also. Pepsin; References
Eqolosins prefer bulky amino acid residues at the P1 site and small amino acid residues at the P1′ site. [8] The substrate specificity of scytalidoglutamic peptidase is unique, particularly in the substrate preferences at the P3 (basic amino acid), P1′ (small amino acid) and P3′ (basic) positions. [9]
The particular geometry of the triad members are highly characteristic to their specific function: it was shown that the position of just four points of the triad characterize the function of the containing enzyme. [8] In the event of catalysis, an ordered mechanism occurs in which several intermediates are generated.
Hydrolyses various precursor proteins with Arg or Lys in P1, and commonly Arg or Lys also in P2. The P3 amino acid is usually non-polar, but otherwise additional basic amino acids are favourable in both non-prime and prime positions. This enzyme belongs to the peptidase family A1 of pepsin.
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