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• W2035162646 abstract "The tphA1 II and tphA2 II A3 II genes of Comamonas sp. E6 perhaps code for the terephthalate (TPA) 1,2-dioxygenase (TPADO). To characterize E6 TPADO, these genes were expressed in a His-tagged form in Escherichia coli, and the recombinant proteins were purified. TPADO activity was reconstituted from TphA1II and TphA2IIA3II, indicating that TPADO consists of a reductase (TphA1II) and a terminal oxygenase component (TphA2II and TphA3II). TphA1II contains FAD, and the presence of a plant-type [2Fe-2S] cluster was suggested. These results indicate that TPADO is a class IB aromatic ring-hydroxylating dioxygenase. NADH and NADPH were effective as electron donors for TphA1II, but NADPH appeared to be the physiological electron donor, based on the kinetic parameters. TPADO showed activity only toward TPA, and Fe2+ was required for it. The Km values for TPA and the V max were determined to be 72±6 μm and 9.87±0.06 U/mg respectively." @default.
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• W2035162646 date "2008-09-23" @default.
• W2035162646 modified "2023-09-27" @default.
• W2035162646 title "Enzymatic Properties of Terephthalate 1,2-Dioxygenase of<i>Comamonas</i>sp. Strain E6" @default.
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• W2035162646 doi "https://doi.org/10.1271/bbb.80236" @default.
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