Disease relevance of endopeptidase

• After Coomassie Brilliant Blue (CBB) staining, 1200 spots were detected and 140 major spots were excised from the gel and subjected to in-gel digestion with Achromobacter protease I (lysyl endopeptidase) [1].

High impact information on endopeptidase

• This product, Bm-CPI-2, blocks conventional cysteine proteases such as papain, but also the aspariginyl endopeptidase involved in the Class II antigen processing pathway in human B cells [2].
• Metabolism of AF1 (KNEFIRF-NH2) in the nematode, Ascaris suum, by aminopeptidase, endopeptidase and deamidase enzymes [3].
• The endopeptidase resembled mammalian neprilysin (NEP, endopeptidase 24.11) in that the enzyme activity was inhibited by phosphoramidon and thiorphan and that it cleaved AF1 on the amino side of phenylalanine [3].
• We have previously identified in membranes of the locomotory muscle of Ascaris suum a phosphoramidon-sensitive endopeptidase which hydrolyses the neuropeptide AF1 (Lys-Asn-Glu-Phe-Ile-Arg-Phe-NH2) by cleavage of the Glu3-Phe4 bond (Sajid & Isaac, 1994) [4].
• The phosphoramidon-sensitive endopeptidase activity was detected on intact muscle cells prepared by collagenase treatment of the body wall musculature, indicating that endopeptidase is accessible to peptide molecules that interact with the cell surface [4].

Associations of endopeptidase with chemical compounds

• The endopeptidase had a neutral pH optimum and a significant proportion (45%) of the enzyme activity partitioned into the detergent-rich phase of Triton X-114, indicating that the enzyme is an integral membrane protein [4].
• Here, we identified a specific lactacystin-sensitive endopeptidase that cleaves the D: -Asp-containing protein and named it D: -aspartyl endopeptidase (DAEP) [5].

Other interactions of endopeptidase

• FIRF-NH2 and KNEFIRF were identified as three primary degradation products, resulting from the action of an endopeptidase, aminopeptidase and a deamidase, respectively [3].
• A peptide fraction from whole P. redivivus evoked an adipokinetic response in the locust, Schistocera gregaria which was dose dependent and was abolished by treatment with endopeptidase 24:11 but not by boiling or by incubation with leucine aminopeptidase [6].
• We have determined the properties of this neuropeptide-degrading enzyme of A. suum muscle using AKH-1 (pGlu-Leu-Asn-Phe-Thr-Pro-Asn-Trp-Gly-Thr-NH2) and [D-Ala2, Leu5]enkephalin as convenient endopeptidase substrates [4].

Analytical, diagnostic and therapeutic context of endopeptidase

• None of the aforementioned AF1 metabolites (2-20 microM) retained biological activity in this bioassay, indicating that the endopeptidase, aminopeptidase and deamidase have the potential to terminate the action of AF1 on locomotory muscle of A. suum [3].

References