{"@context":{"@vocab":"https://cir.nii.ac.jp/schema/1.0/","rdfs":"http://www.w3.org/2000/01/rdf-schema#","dc":"http://purl.org/dc/elements/1.1/","dcterms":"http://purl.org/dc/terms/","foaf":"http://xmlns.com/foaf/0.1/","prism":"http://prismstandard.org/namespaces/basic/2.0/","cinii":"http://ci.nii.ac.jp/ns/1.0/","datacite":"https://schema.datacite.org/meta/kernel-4/","ndl":"http://ndl.go.jp/dcndl/terms/","jpcoar":"https://github.com/JPCOAR/schema/blob/master/2.0/"},"@id":"https://cir.nii.ac.jp/crid/1390282679908327040.json","@type":"Article","productIdentifier":[{"identifier":{"@type":"DOI","@value":"10.1093/oxfordjournals.jbchem.a002874"}},{"identifier":{"@type":"COI","@value":"1:CAS:528:DC%2BD3MXjtlSju7c%3D"}},{"identifier":{"@type":"PMID","@value":"11226883"}},{"identifier":{"@type":"NDL_BIB_ID","@value":"5695466"}},{"identifier":{"@type":"URI","@value":"http://id.ndl.go.jp/bib/5695466"}},{"identifier":{"@type":"URI","@value":"https://ndlsearch.ndl.go.jp/books/R000000004-I5695466"}},{"identifier":{"@type":"URI","@value":"http://academic.oup.com/jb/article-pdf/129/3/429/2475946/129-3-429.pdf"}},{"identifier":{"@type":"NAID","@value":"130003534101"}},{"identifier":{"@type":"NAID","@value":"10007853844"}},{"identifier":{"@type":"URI","@value":"https://search.jamas.or.jp/link/ui/2001189233"}}],"resourceType":"学術雑誌論文(journal article)","dc:title":[{"@language":"en","@value":"Interactions of Human Matrix Metalloproteinase 7(Matrilysin) with the Inhibitors Thiorphan and R-94138."}],"dc:language":"en","description":[{"type":"abstract","notation":[{"@language":"en","@value":"The effects of the metalloproteinase inhibitors thiorphan and R-94138 on the matrilysincatalyzed hydrolysis of (7-methoxycoumarin-4-yl)acetyl-L-Pro-L-Leu-Gly-L-Leu-[<i>N</i><sup>3</sup>-(2, 4-dinitrophenyl)-L-2, 3-diamino-propionyl]-L-Ala-L-Arg-NH2 [MOCAc-PLGL(Dpa)AR] were examined. The inhibitor constants (<i>K</i><sub>i</sub>) of thiorphan and R-94138 for matrilysin at pH 7.5, 25°C were determined to be 11.2 and 7.65μM, respectively. From the temperature dependence of the <i>K</i><sub>i</sub> values at pH 7.5, the standard enthalpy change (Δ<i>H</i><sup>°</sup>) values for the binding of matrilysin with thiorphan and R-94138 were determined to be -(18.2±0.9) and (1.65±1.07) kJ•mol<sup>-1</sup>, respectively. The binding of matrilysin to thiorphan is exothermic and the free energy change in the complex formation depends mainly on the change in enthalpy, while the binding to R-94138 is endothermic and typically entropy-driven. Hydrophobic interactions are suggested to contribute significantly to the binding of matrilysin to R-94138 as well as to the substrate. The pH dependence of the <i>K</i><sub>i</sub> value suggests that at least two ionizing groups with p<i>K</i><sub>a</sub> values of 4.5 and 9.1-9.3 are involved in the binding. The matrilysin activity is regulated by ionizing groups with pK<sub>a</sub> values of 4.3 and 9.6. Both inhibition and hydrolysis are suggested to be controlled by the same residues in matrilysin, most likely Glu 198 and Tyr 219, respectively."}],"abstractLicenseFlag":"disallow"}],"creator":[{"@id":"https://cir.nii.ac.jp/crid/1410282679908327041","@type":"Researcher","personIdentifier":[{"@type":"NRID","@value":"9000253180875"},{"@type":"NRID","@value":"9000000667199"}],"foaf:name":[{"@language":"en","@value":"Oneda Hiroshi"}],"jpcoar:affiliationName":[{"@language":"en","@value":"Division of Applied Life Sciences, Graduate School of Agriculture, Kyoto University"}]},{"@id":"https://cir.nii.ac.jp/crid/1410282679908327040","@type":"Researcher","personIdentifier":[{"@type":"NRID","@value":"9000253180876"},{"@type":"NRID","@value":"9000000667201"}],"foaf:name":[{"@language":"en","@value":"Inouye Kuniyo"}],"jpcoar:affiliationName":[{"@language":"en","@value":"Division of Applied Life Sciences, Graduate School of Agriculture, Kyoto University"}]}],"publication":{"publicationIdentifier":[{"@type":"PISSN","@value":"0021924X"},{"@type":"EISSN","@value":"17562651"},{"@type":"NDL_BIB_ID","@value":"000000119499"},{"@type":"ISSN","@value":"0021924X"},{"@type":"LISSN","@value":"0021924X"},{"@type":"PISSN","@value":"https://id.crossref.org/issn/0021924X"},{"@type":"PISSN","@value":"http://id.crossref.org/issn/0021924X"},{"@type":"NCID","@value":"AA00694073"}],"prism:publicationName":[{"@language":"en","@value":"The Journal of Biochemistry"},{"@language":"en","@value":"J Biochem (Tokyo)"}],"dc:publisher":[{"@language":"en","@value":"The Japanese Biochemical Society"},{"@language":"ja","@value":"社団法人 日本生化学会"}],"prism:publicationDate":"2001","prism:volume":"129","prism:number":"3","prism:startingPage":"429","prism:endingPage":"435"},"reviewed":"false","url":[{"@id":"http://id.ndl.go.jp/bib/5695466"},{"@id":"https://ndlsearch.ndl.go.jp/books/R000000004-I5695466"},{"@id":"http://academic.oup.com/jb/article-pdf/129/3/429/2475946/129-3-429.pdf"},{"@id":"https://search.jamas.or.jp/link/ui/2001189233"}],"availableAt":"2001","foaf:topic":[{"@id":"https://cir.nii.ac.jp/all?q=inhibitor","dc:title":"inhibitor"},{"@id":"https://cir.nii.ac.jp/all?q=matrilysin","dc:title":"matrilysin"},{"@id":"https://cir.nii.ac.jp/all?q=matrix%20metalloproteinase","dc:title":"matrix metalloproteinase"},{"@id":"https://cir.nii.ac.jp/all?q=thermolysin","dc:title":"thermolysin"},{"@id":"https://cir.nii.ac.jp/all?q=thiorphan","dc:title":"thiorphan"}],"relatedProduct":[{"@id":"https://cir.nii.ac.jp/crid/1360855571486651776","@type":"Article","relationType":["cites"],"jpcoar:relatedTitle":[{"@value":"Metal and pH 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