76AC42E3DFAFF7E2153A425D6C7752D7EAB10398C4E961AE625D5B07518CE6DE21DFC8F0F5CC8DA3AF5AA9A710A56E43

Is able to inhibit all four classes of proteinases by a unique 'trapping' mechanism. This protein has a peptide stretch, called the 'bait region' which contains specific cleavage sites for different proteinases. When a proteinase cleaves the bait region, a conformational change is induced in the protein which traps the proteinase. The entrapped enzyme remains active against low molecular weight substrates (activity against high molecular weight substrates is greatly reduced). Following cleavage in the bait region a thioester bond is hydrolyzed and mediates the covalent binding of the protein to the proteinase (By similarity).

Source:http://purl.uniprot.org/SHA-384/76AC42E3DFAFF7E2153A425D6C7752D7EAB10398C4E961AE625D5B07518CE6DE21DFC8F0F5CC8DA3AF5AA9A710A56E43

Statements in which the resource exists.
SubjectPredicateObjectContext
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http://purl.uniprot.org/SHA...rdfs:commentIs able to inhibit all four classes of proteinases by a unique 'trapping' mechanism. This protein has a peptide stretch, called the 'bait region' which contains specific cleavage sites for different proteinases. When a proteinase cleaves the bait region, a conformational change is induced in the protein which traps the proteinase. The entrapped enzyme remains active against low molecular weight substrates (activity against high molecular weight substrates is greatly reduced). Following cleavage in the bait region a thioester bond is hydrolyzed and mediates the covalent binding of the protein to the proteinase (By similarity).lld:uniprot
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uniprot-protein:Q63041uniprot:annotationhttp://purl.uniprot.org/SHA...lld:uniprot
http://linkedlifedata.com/r...rdf:subjecthttp://purl.uniprot.org/SHA...lld:uniprot
http://linkedlifedata.com/r...rdf:subjecthttp://purl.uniprot.org/SHA...lld:uniprot