Substrate specificity of the protease that processes human interleukin-1 beta.

摘要: Abstract The substrate specificity of the protease which generates mature human interleukin-1 beta (IL-1 beta) from pro-interleukin-1 was investigated using synthetic peptide substrates and recombinant pro-IL-1 beta. requirement an L-aspartate in P-1 position confirmed together with need for a small hydrophobic residue P-1' (Gly or Ala). It shown that enzyme can tolerate conservative substitutions P-2 P-2' positions. We found little difference enzyme's ability to cleave denatured native beta, indicating tertiary structure recognition is not involved binding. did, however, require more than six amino acids cleavage occur. These results conclusively demonstrate unusual this protease.