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  • amino acid
  • Each amino acid in the triad performs a specific task in this process: The serine has an -OH group that is able to act as a nucleophile, attacking the carbonyl carbon of the scissile peptide bond of the substrate. (wikipedia.org)
  • cleavage
  • The determination of the cleavage sites in the oxidized B-chain of insulin showed specificity for hydrophobic residues at the P2 and P3 positions, indicating that RSIP is distinct from other previously characterized maize endopeptidases. (biochemj.org)
  • activity
  • Glucose starvation induced RSIP: after 4 days of starvation, RSIP was estimated to constitute 80% of total endopeptidase activity in the root tip. (biochemj.org)
  • protein
  • Only short protein residues are able to enter the active site of prolyl endopeptidase due to the distinct beta-propeller region that acts as a gating filter mechanism. (wikipedia.org)
  • type
  • Now included with EC 3.4.16.5, carboxypeptidase C EC 3.4.16.4: serine-type D-Ala-D-Ala carboxypeptidase EC 3.4.16.5: carboxypeptidase c EC 3.4.16.6: carboxypeptidase D EC 3.4.17.1: carboxypeptidase A EC 3.4.17.2: carboxypeptidase B EC 3.4.17.3: lysine carboxypeptidase EC 3.4.17.4: Gly-X carboxypeptidase EC 3.4.17.5: Deleted entry: aspartate carboxypeptidase EC 3.4.17.6: alanine carboxypeptidase EC 3.4.17.7: Transferred entry: acylmuramoyl-alanine carboxypeptidase. (wikipedia.org)