EC Number   |
Substrates |
Organism |
Products |
Reversibility |
|---|
   3.4.21.B56 | alpha-casein + H2O |
alpha-casein is not cleaved as effectively as beta-casein. 1510-N probably cleaves the substrate specifically. The cleavage sites contain many hydrophobic and aromatic residues. The 1510-N protease possibly recognizes leucine at the cleavage site |
Pyrococcus horikoshii |
? |
- |
? |
| 3.4.21.B56 | beta-casein + H2O |
alpha-casein is not cleaved as effectively as beta-casein. 1510-N probably cleaves the substrate specifically. The cleavage sites contain many hydrophobic and aromatic residues. The 1510-N protease possibly recognizes leucine at the cleavage site |
Pyrococcus horikoshii |
? |
- |
? |
| 3.4.21.B56 | more |
1510-N is a serine protease with a catalytic residue, Ser-97 |
Pyrococcus horikoshii |
? |
- |
? |
| 3.4.21.B56 | more |
binding of the substrate to the catalytic site of 1510-N induces conformational changes in a region that includes loop L2 so that Lys138 approaches the catalytic Ser97 |
Pyrococcus horikoshii |
? |
- |
? |
| 3.4.21.B56 | more |
peptide substrate binding structure of the enzyme, detailed analysis and overview. The six central residues, VIVLML, of the peptide are hydrophobic and in a pseudopalindromic structure and therefore favorably fit into the hydrophobic active tunnel of the enzyme dimer, although the enzyme degrades the substrate at only one point. Binding of the substrate causes a large rotational and translational displacement between protomers and produces a tunnel suitable for binding the peptide. When the peptide binds, the flexible L2 loop of one protomer forms beta-strands, whereas that of the other protomer remains in a loop form, indicating that one protomer binds to the peptide more tightly than the other protomer. The Ala138 residues of the two protomers are located very close together, close positioning of the catalytic Ser97 and Lys138 residues may be induced by electrostatic repulsion of the two Lys138 side chains of the protomers |
Pyrococcus horikoshii |
? |
- |
? |
| 3.4.21.B56 | more |
binding of the substrate to the catalytic site of 1510-N induces conformational changes in a region that includes loop L2 so that Lys138 approaches the catalytic Ser97 |
Pyrococcus horikoshii OT-3 |
? |
- |
? |
| 3.4.21.B56 | p-stomatin PH1511 + H2O |
the N-terminal region of PH1510 (residues 16-236, i.e. 1510-N) is a serine protease with a catalytic Ser-Lys dyad (Ser97 and Lys138) and specifically cleaves the C-terminal hydrophobic region of the p-stomatin PH1511 |
Pyrococcus horikoshii |
? |
- |
? |
| 3.4.21.B56 | p-stomatin PH1511p + H2O |
the N-terminal region of PH1510p is a serine protease and specifically cleaves the C-terminal hydrophobic region of the p-stomatin PH1511p |
Pyrococcus horikoshii |
? |
- |
? |
| 3.4.21.B56 | stomatin-homolog PH1511 + H2O |
the N-terminal region of an open reading frame, PH1510 (residues 16236, designated as 1510-N) is a serine protease with a catalytic Ser-Lys dyad that specifically cleaves the C-terminal hydrophobic residues of a membrane protein, the stomatin-homolog PH1511 |
Pyrococcus horikoshii |
? |
- |
? |
| 3.4.21.B56 | stomatin-homolog PH1511 + H2O |
the N-terminal region of an open reading frame, PH1510 (residues 16236, designated as 1510-N) is a serine protease with a catalytic Ser-Lys dyad that specifically cleaves the C-terminal hydrophobic residues of a membrane protein, the stomatin-homolog PH1511 |
Pyrococcus horikoshii OT-3 |
? |
- |
? |
