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dc.contributor.authorShin, JS-
dc.contributor.authorYu, MH-
dc.date.accessioned2024-01-21T10:42:18Z-
dc.date.available2024-01-21T10:42:18Z-
dc.date.created2021-09-04-
dc.date.issued2002-04-05-
dc.identifier.issn0021-9258-
dc.identifier.urihttps://pubs.kist.re.kr/handle/201004/139601-
dc.description.abstractSerpins (serine protease inhibitors) inhibit target proteases by forming a stable covalent complex in which the cleaved reactive site loop of the serpin is inserted into beta-sheet A of the serpin with concomitant translocation of the protease to the opposite of the initial binding site. Despite recent determination of the crystal structures of a Michaelis protease-serpin complex as well as a stable covalent complex, details on the kinetic mechanism remain unsolved mainly due to difficulties in measuring kinetic parameters of acylation, protease translo. cation, and deacylation steps. To address the problem, we applied a mathematical model developed on the basis of a suicide inhibition mechanism to the stopped-flow kinetics of fluorescence resonance energy transfer during complex formation between alpha(1)-antitrypsin, a prototype serpin, and proteases. Compared with the hydrolysis of a peptide substrate, acylation of the protease by alpha(1)-antitrypsin is facilitated, whereas deacylation of the acyl intermediate is strongly suppressed during the protease translocation. The results from nucleophile susceptibility of the acyl intermediate suggest strongly that the active site of the protease is already perturbed during translocation.-
dc.languageEnglish-
dc.publisherAMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC-
dc.subjectPLASMINOGEN-ACTIVATOR INHIBITOR-1-
dc.subjectSERPIN-PROTEINASE COMPLEX-
dc.subjectREACTIVE CENTER LOOP-
dc.subjectPORCINE PANCREATIC ELASTASE-
dc.subjectBETA-SHEET-A-
dc.subjectALPHA(1)-PROTEINASE INHIBITOR-
dc.subjectALPHA-1-PROTEINASE INHIBITOR-
dc.subjectNATIVE STRAIN-
dc.subjectCATHEPSIN-G-
dc.subjectINSERTION-
dc.titleKinetic dissection of alpha(1)-antitrypsin inhibition mechanism-
dc.typeArticle-
dc.identifier.doi10.1074/jbc.M111168200-
dc.description.journalClass1-
dc.identifier.bibliographicCitationJOURNAL OF BIOLOGICAL CHEMISTRY, v.277, no.14, pp.11629 - 11635-
dc.citation.titleJOURNAL OF BIOLOGICAL CHEMISTRY-
dc.citation.volume277-
dc.citation.number14-
dc.citation.startPage11629-
dc.citation.endPage11635-
dc.description.journalRegisteredClassscie-
dc.description.journalRegisteredClassscopus-
dc.identifier.wosid000174846400004-
dc.identifier.scopusid2-s2.0-0037023735-
dc.relation.journalWebOfScienceCategoryBiochemistry & Molecular Biology-
dc.relation.journalResearchAreaBiochemistry & Molecular Biology-
dc.type.docTypeArticle-
dc.subject.keywordPlusPLASMINOGEN-ACTIVATOR INHIBITOR-1-
dc.subject.keywordPlusSERPIN-PROTEINASE COMPLEX-
dc.subject.keywordPlusREACTIVE CENTER LOOP-
dc.subject.keywordPlusPORCINE PANCREATIC ELASTASE-
dc.subject.keywordPlusBETA-SHEET-A-
dc.subject.keywordPlusALPHA(1)-PROTEINASE INHIBITOR-
dc.subject.keywordPlusALPHA-1-PROTEINASE INHIBITOR-
dc.subject.keywordPlusNATIVE STRAIN-
dc.subject.keywordPlusCATHEPSIN-G-
dc.subject.keywordPlusINSERTION-
dc.subject.keywordAuthorα₁-antitrypsin-
dc.subject.keywordAuthorinhibition mechanism-
dc.subject.keywordAuthoracyl intermediate-
dc.subject.keywordAuthortranslocation-
dc.subject.keywordAuthorkinetic model-
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