{"@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/1363388844910048256.json","@type":"Article","productIdentifier":[{"identifier":{"@type":"DOI","@value":"10.1128/jb.178.12.3539-3543.1996"}},{"identifier":{"@type":"URI","@value":"https://journals.asm.org/doi/pdf/10.1128/jb.178.12.3539-3543.1996"}}],"dc:title":[{"@value":"Purification and characterization of an oxygen-sensitive, reversible 3,4-dihydroxybenzoate decarboxylase from Clostridium hydroxybenzoicum"}],"description":[{"type":"abstract","notation":[{"@value":"<jats:p>A 3,4-dihydroxybenzoate decarboxylase (EC 4.1.1.63) from Clostridium hydroxybenzoicum JW/Z-1T was purified and partially characterized. The estimated molecular mass of the enzyme was 270 kDa. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis gave a single band of 57 kDa, suggesting that the enzyme consists of five identical subunits. The temperature and pH optima were 50 degrees C and pH 7.0, respectively. The Arrhenius energy for decarboxylation of 3,4-dihydroxybenzoate was 32.5 kJ . mol(-1) for the temperature range from 22 to 50 degrees C. The Km and kcat for 3,4-dihydroxybenzoate were 0.6 mM and 5.4 x 10(3) min(-1), respectively, at pH 7.0 and 25 degrees C. The enzyme optimally catalyzed the reverse reaction, that is, the carboxylation of catechol to 3,4-dihydroxybenzoate, at pH 7.0. The enzyme did not decarboxylate 2-hydroxybenzoate, 3-hydroxybenzoate, 4-hydroxybenzoate, 2,3-dihydroxybenzoate, 2,4-dihydroxybenzoate, 2,5-dihydroxybenzoate, 2,3,4-trihydroxybenzoate, 3,4,5-trihydroxybenzoate, 3-F-4-hydroxybenzoate, or vanillate. The decarboxylase activity was inhibited by 25 and 20%, respectively, by 2,3,4- and 3,4,5-trihydroxybenzoate. Thiamine PPi and pyridoxal 5'-phosphate did not stimulate and hydroxylamine and sodium borohydride did not inhibit the enzyme activity, indicating that the 3,4-dihydroxybenzoate decarboxylase is not a thiamine PPi-, pyridoxal 5'-phosphate-, or pyruvoyl-dependent enzyme.</jats:p>"}]}],"creator":[{"@id":"https://cir.nii.ac.jp/crid/1383388844910048256","@type":"Researcher","foaf:name":[{"@value":"Z He"}],"jpcoar:affiliationName":[{"@value":"Department of Microbiology, University of Georgia, Athens 30602-2605, USA."}]},{"@id":"https://cir.nii.ac.jp/crid/1383388844910048257","@type":"Researcher","foaf:name":[{"@value":"J Wiegel"}],"jpcoar:affiliationName":[{"@value":"Department of Microbiology, University of Georgia, Athens 30602-2605, USA."}]}],"publication":{"publicationIdentifier":[{"@type":"PISSN","@value":"00219193"},{"@type":"EISSN","@value":"10985530"}],"prism:publicationName":[{"@value":"Journal of Bacteriology"}],"dc:publisher":[{"@value":"American Society for Microbiology"}],"prism:publicationDate":"1996-06","prism:volume":"178","prism:number":"12","prism:startingPage":"3539","prism:endingPage":"3543"},"reviewed":"false","dc:rights":["https://journals.asm.org/non-commercial-tdm-license"],"url":[{"@id":"https://journals.asm.org/doi/pdf/10.1128/jb.178.12.3539-3543.1996"}],"createdAt":"2016-11-14","modifiedAt":"2021-07-29","relatedProduct":[{"@id":"https://cir.nii.ac.jp/crid/1360002219111523712","@type":"Article","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@value":"Production of <i>p</i>-Aminosalicylic Acid through Enzymatic Kolbe–Schmitt Reaction Catalyzed by Reversible Salicylic Acid Decarboxylase"}]},{"@id":"https://cir.nii.ac.jp/crid/1360290617458412544","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@value":"A Novel Gene Cluster Is Involved in the Degradation of Lignin-Derived Monoaromatics in Thermus oshimai JL-2"}]},{"@id":"https://cir.nii.ac.jp/crid/1360565165947367680","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@value":"Enhancement of protocatechuate decarboxylase activity for the effective production of muconate from lignin-related aromatic compounds"}]},{"@id":"https://cir.nii.ac.jp/crid/1360572184472200448","@type":"Article","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@value":"Expanding Substrate Specificity of Salicylate Decarboxylase by Site-directed Mutagenesis for Expansion of the Entrance Region Connecting to the Substrate Access Tunnel"}]},{"@id":"https://cir.nii.ac.jp/crid/1520010378552976000","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@value":"Recent progress in biocatalysis using supercritical carbon dioxide"}]},{"@id":"https://cir.nii.ac.jp/crid/1520291854855550208","@type":"Article","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@value":"Enzymatic Functionalization of Aromatic N-Heterocycles:Hydroxylation and Carboxylation"},{"@language":"ja-Kana","@value":"Enzymatic Functionalization of Aromatic N Heterocycles Hydroxylation and Carboxylation"}]},{"@id":"https://cir.nii.ac.jp/crid/1520573330010179328","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@value":"p-Aminosalicylic Acid Production by Enzymatic Kolbe-Schmitt Reaction Using Salicylic Acid Decarboxylases Improved through Site-Directed Mutagenesis"}]}],"dataSourceIdentifier":[{"@type":"CROSSREF","@value":"10.1128/jb.178.12.3539-3543.1996"},{"@type":"CROSSREF","@value":"10.1016/s1389-1723(00)88723-x_references_DOI_39KNnWXcDt6ly2UDf3nHiVpmyg8"},{"@type":"CROSSREF","@value":"10.1246/bcsj.20130006_references_DOI_39KNnWXcDt6ly2UDf3nHiVpmyg8"},{"@type":"CROSSREF","@value":"10.1128/aem.01589-20_references_DOI_39KNnWXcDt6ly2UDf3nHiVpmyg8"},{"@type":"CROSSREF","@value":"10.1016/j.jbiotec.2014.10.027_references_DOI_39KNnWXcDt6ly2UDf3nHiVpmyg8"},{"@type":"CROSSREF","@value":"10.1246/cl.180755_references_DOI_39KNnWXcDt6ly2UDf3nHiVpmyg8"},{"@type":"CROSSREF","@value":"10.1246/cl.2011.206_references_DOI_39KNnWXcDt6ly2UDf3nHiVpmyg8"},{"@type":"CROSSREF","@value":"10.1016/j.jbiosc.2012.10.002_references_DOI_39KNnWXcDt6ly2UDf3nHiVpmyg8"}]}