{"@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/1361981471023684096.json","@type":"Article","productIdentifier":[{"identifier":{"@type":"DOI","@value":"10.1073/pnas.0337742100"}},{"identifier":{"@type":"URI","@value":"https://pnas.org/doi/pdf/10.1073/pnas.0337742100"}}],"dc:title":[{"@value":"The deoxyxylulose phosphate pathway of isoprenoid biosynthesis: Studies on the mechanisms of the reactions catalyzed by IspG and IspH protein"}],"description":[{"type":"abstract","notation":[{"@value":"<jats:p>\n            Earlier\n            <jats:italic>in vivo</jats:italic>\n            studies have shown that the sequential action of the IspG and IspH proteins is essential for the reductive transformation of 2\n            <jats:italic>C</jats:italic>\n            -methyl-\n            <jats:sc>d</jats:sc>\n            -erythritol 2,4-cyclodiphosphate into dimethylallyl diphosphate and isopentenyl diphosphate via 1-hydroxy-2-methyl-2-(\n            <jats:italic>E</jats:italic>\n            )-butenyl 4-diphosphate. A recombinant fusion protein comprising maltose binding protein and IspG protein domains was purified from a recombinant\n            <jats:italic>Escherichia coli</jats:italic>\n            strain. The purified protein failed to transform 2\n            <jats:italic>C</jats:italic>\n            -methyl-\n            <jats:sc>d</jats:sc>\n            -erythritol 2,4-cyclodiphosphate into 1-hydroxy-2-methyl-2-(\n            <jats:italic>E</jats:italic>\n            )-butenyl 4-diphosphate, but catalytic activity could be restored by the addition of crude cell extract from an\n            <jats:italic>ispG</jats:italic>\n            -deficient\n            <jats:italic>E. coli</jats:italic>\n            mutant. This indicates that auxiliary proteins are required, probably as shuttles for redox equivalents. On activation by photoreduced 10-methyl-5-deaza-isoalloxazine, the recombinant protein catalyzed the formation of 1-hydroxy-2-methyl-2-(\n            <jats:italic>E</jats:italic>\n            )-butenyl 4-diphosphate from 2\n            <jats:italic>C</jats:italic>\n            -methyl-\n            <jats:sc>d</jats:sc>\n            -erythritol 2,4-cyclodiphosphate at a rate of 1 nmol⋅min\n            <jats:sup>−1</jats:sup>\n            ⋅mg\n            <jats:sup>−1</jats:sup>\n            . Similarly, activation by photoreduced 10-methyl-5-deaza-isoalloxazine enabled purified IspH protein to catalyze the conversion of 1-hydroxy-2-methyl-2-(\n            <jats:italic>E</jats:italic>\n            )-butenyl 4-diphosphate into a 6:1 mixture of isopentenyl diphosphate and dimethylallyl diphosphate at a rate of 0.4 μmol⋅min\n            <jats:sup>−1</jats:sup>\n            ⋅mg\n            <jats:sup>−1</jats:sup>\n            . IspH protein could also be activated by a mixture of flavodoxin, flavodoxin reductase, and NADPH at a rate of 3 nmol⋅min\n            <jats:sup>−1</jats:sup>\n            ⋅mg\n            <jats:sup>−1</jats:sup>\n            . The striking similarities of IspG and IspH protein are discussed, and plausible mechanistic schemes are proposed for the two reactions.\n          </jats:p>"}]}],"creator":[{"@id":"https://cir.nii.ac.jp/crid/1380576138212885376","@type":"Researcher","foaf:name":[{"@value":"Felix Rohdich"}],"jpcoar:affiliationName":[{"@value":"Lehrstuhl für Organische Chemie und Biochemie, Technische Universität München, Lichtenbergstrasse 4, D-85747 Garching, Germany; and Laboratorium für Organische Chemie, Eidgenössische Technische Hochschule Zürich HCI, CH-8093 Zürich, Switzerland"}]},{"@id":"https://cir.nii.ac.jp/crid/1380576138212885378","@type":"Researcher","foaf:name":[{"@value":"Ferdinand Zepeck"}],"jpcoar:affiliationName":[{"@value":"Lehrstuhl für Organische Chemie und Biochemie, Technische Universität München, Lichtenbergstrasse 4, D-85747 Garching, Germany; and Laboratorium für Organische Chemie, Eidgenössische Technische Hochschule Zürich HCI, CH-8093 Zürich, Switzerland"}]},{"@id":"https://cir.nii.ac.jp/crid/1380576138212885505","@type":"Researcher","foaf:name":[{"@value":"Petra Adam"}],"jpcoar:affiliationName":[{"@value":"Lehrstuhl für Organische Chemie und Biochemie, Technische Universität München, Lichtenbergstrasse 4, D-85747 Garching, Germany; and Laboratorium für Organische Chemie, Eidgenössische Technische Hochschule Zürich HCI, CH-8093 Zürich, Switzerland"}]},{"@id":"https://cir.nii.ac.jp/crid/1380576138212885510","@type":"Researcher","foaf:name":[{"@value":"Stefan Hecht"}],"jpcoar:affiliationName":[{"@value":"Lehrstuhl für Organische Chemie und Biochemie, Technische Universität München, Lichtenbergstrasse 4, D-85747 Garching, Germany; and Laboratorium für Organische Chemie, Eidgenössische Technische Hochschule Zürich HCI, CH-8093 Zürich, Switzerland"}]},{"@id":"https://cir.nii.ac.jp/crid/1380576138212885509","@type":"Researcher","foaf:name":[{"@value":"Johannes Kaiser"}],"jpcoar:affiliationName":[{"@value":"Lehrstuhl für Organische Chemie und Biochemie, Technische Universität München, Lichtenbergstrasse 4, D-85747 Garching, Germany; and Laboratorium für Organische Chemie, Eidgenössische Technische Hochschule Zürich HCI, CH-8093 Zürich, Switzerland"}]},{"@id":"https://cir.nii.ac.jp/crid/1380576138212885379","@type":"Researcher","foaf:name":[{"@value":"Ralf Laupitz"}],"jpcoar:affiliationName":[{"@value":"Lehrstuhl für Organische Chemie und Biochemie, Technische Universität München, Lichtenbergstrasse 4, D-85747 Garching, Germany; and Laboratorium für Organische Chemie, Eidgenössische Technische Hochschule Zürich HCI, CH-8093 Zürich, Switzerland"}]},{"@id":"https://cir.nii.ac.jp/crid/1380576138212885506","@type":"Researcher","foaf:name":[{"@value":"Tobias Gräwert"}],"jpcoar:affiliationName":[{"@value":"Lehrstuhl für Organische Chemie und Biochemie, Technische Universität München, Lichtenbergstrasse 4, D-85747 Garching, Germany; and Laboratorium für Organische Chemie, Eidgenössische Technische Hochschule Zürich HCI, CH-8093 Zürich, Switzerland"}]},{"@id":"https://cir.nii.ac.jp/crid/1380576138212885504","@type":"Researcher","foaf:name":[{"@value":"Sabine Amslinger"}],"jpcoar:affiliationName":[{"@value":"Lehrstuhl für Organische Chemie und Biochemie, Technische Universität München, Lichtenbergstrasse 4, D-85747 Garching, Germany; and Laboratorium für Organische Chemie, Eidgenössische Technische Hochschule Zürich HCI, CH-8093 Zürich, Switzerland"}]},{"@id":"https://cir.nii.ac.jp/crid/1380576138212885507","@type":"Researcher","foaf:name":[{"@value":"Wolfgang Eisenreich"}],"jpcoar:affiliationName":[{"@value":"Lehrstuhl für Organische Chemie und Biochemie, Technische Universität München, Lichtenbergstrasse 4, D-85747 Garching, Germany; and Laboratorium für Organische Chemie, Eidgenössische Technische Hochschule Zürich HCI, CH-8093 Zürich, Switzerland"}]},{"@id":"https://cir.nii.ac.jp/crid/1380576138212885377","@type":"Researcher","foaf:name":[{"@value":"Adelbert Bacher"}],"jpcoar:affiliationName":[{"@value":"Lehrstuhl für Organische Chemie und Biochemie, Technische Universität München, Lichtenbergstrasse 4, D-85747 Garching, Germany; and Laboratorium für Organische Chemie, Eidgenössische Technische Hochschule Zürich HCI, CH-8093 Zürich, Switzerland"}]},{"@id":"https://cir.nii.ac.jp/crid/1380576138212885508","@type":"Researcher","foaf:name":[{"@value":"Duilio Arigoni"}],"jpcoar:affiliationName":[{"@value":"Lehrstuhl für Organische Chemie und Biochemie, Technische Universität München, Lichtenbergstrasse 4, D-85747 Garching, Germany; and Laboratorium für Organische Chemie, Eidgenössische Technische Hochschule Zürich HCI, CH-8093 Zürich, Switzerland"}]}],"publication":{"publicationIdentifier":[{"@type":"PISSN","@value":"00278424"},{"@type":"EISSN","@value":"10916490"}],"prism:publicationName":[{"@value":"Proceedings of the National Academy of Sciences"}],"dc:publisher":[{"@value":"Proceedings of the National Academy of Sciences"}],"prism:publicationDate":"2003-02-05","prism:volume":"100","prism:number":"4","prism:startingPage":"1586","prism:endingPage":"1591"},"reviewed":"false","url":[{"@id":"https://pnas.org/doi/pdf/10.1073/pnas.0337742100"}],"createdAt":"2003-02-18","modifiedAt":"2022-04-26","relatedProduct":[{"@id":"https://cir.nii.ac.jp/crid/1050845763735944704","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@language":"en","@value":"Impact of ligands and media on the structure and properties of biological and biomimetic iron-sulfur clusters"}]},{"@id":"https://cir.nii.ac.jp/crid/1390282679303560704","@type":"Article","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@language":"en","@value":"The genetic basis of foliar terpene yield: Implications for breeding and profitability of Australian essential oil crops"}]},{"@id":"https://cir.nii.ac.jp/crid/1524232504988427904","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@value":"Production of squalene by squalene synthases and their truncated mutants in Escherichia coli"}]}],"dataSourceIdentifier":[{"@type":"CROSSREF","@value":"10.1073/pnas.0337742100"},{"@type":"CROSSREF","@value":"10.5511/plantbiotechnology.14.1009a_references_DOI_QnZGx5JCDi26lJ9yGk3ZnXhGKrT"},{"@type":"CROSSREF","@value":"10.1016/j.ccr.2017.02.018_references_DOI_QnZGx5JCDi26lJ9yGk3ZnXhGKrT"},{"@type":"CROSSREF","@value":"10.1016/j.jbiosc.2014.07.013_references_DOI_QnZGx5JCDi26lJ9yGk3ZnXhGKrT"}]}