EC Number   |
Reaction |
Reference |
|---|
   3.4.21.B48 | specifically hydrolyzes Leu15-Tyr16 peptide bond in oxidized insulin B chain, additional cleavage at Phe25-Tyr26 at a considerably lower rate. Good cleavage of the Phe-I-(p-nitrophenylalanine) bond in synthetic peptides. The enzyme preferentially hydrolyzes peptides having an Ala or Pro residue at P2 position and prefers such charged amino acid residues as Glu or Arg at the P2' position. No cleavage: Asp-Pro-Ala-Lys-Phe-(p-nitrophenylalanine)-Arg-Leu |
mechanism, active site structure, the catalytic triad is formed by Glu78, Asp82, and Ser278, Ser278 forms direct hydrogen bonds with the side chain of Asn164 |
-, 664913 |
| 3.4.21.B48 | specifically hydrolyzes Leu15-Tyr16 peptide bond in oxidized insulin B chain, additional cleavage at Phe25-Tyr26 at a considerably lower rate. Good cleavage of the Phe-I-(p-nitrophenylalanine) bond in synthetic peptides. The enzyme preferentially hydrolyzes peptides having an Ala or Pro residue at P2 position and prefers such charged amino acid residues as Glu or Arg at the P2' position. No cleavage: Asp-Pro-Ala-Lys-Phe-(p-nitrophenylalanine)-Arg-Leu |
the catalytic triad is formed by Glu78, Asp82, and Ser278 |
-, 665094 |
| 3.4.21.B48 | Specifically hydrolyzes Leu15-Tyr16 peptide bond in oxidized insulin B-chain, additional cleavage at Phe25-Tyr26 at a considerably lower rate. Good cleavage of the Phe-/-(p-nitrophenylalanine) bond in synthetic peptides. The enzyme preferentially hydrolyzes peptides having an Ala or Pro residue at P2 position and prefers such charged amino acid residues as Glu or Arg at the P2' position. No cleavage: Asp-Pro-Ala-Lys-Phe-(p-nitrophenylalanine)-Arg-Leu |
- |
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