flavin-adenine-dinucleotide and terephthalic-acid

flavin-adenine-dinucleotide has been researched along with terephthalic-acid* in 1 studies

Other Studies

1 other study(ies) available for flavin-adenine-dinucleotide and terephthalic-acid

Article	Year
Enzymatic properties of terephthalate 1,2-dioxygenase of Comamonas sp. strain E6. Bioscience, biotechnology, and biochemistry, 2008, Volume: 72, Issue:9 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 TphA1 II and TphA2 II A3 II, indicating that TPADO consists of a reductase (TphA1 II) and a terminal oxygenase component (TphA2 II and TphA3 II). TphA1(II) 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 TphA1 II, 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 Vmax were determined to be 72+/-6 microM and 9.87+/-0.06 U/mg respectively. Topics: Comamonas; Dioxygenases; Electron Transport; Escherichia coli; Ferredoxin-NADP Reductase; Ferredoxins; Flavin-Adenine Dinucleotide; Hydrogen-Ion Concentration; Kinetics; Molecular Weight; NAD; NADP; Phthalic Acids; Recombinant Proteins; Substrate Specificity; Temperature	2008

Article

Year

Enzymatic properties of terephthalate 1,2-dioxygenase of Comamonas sp. strain E6.

Bioscience, biotechnology, and biochemistry, 2008, Volume: 72, Issue:9

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 TphA1 II and TphA2 II A3 II, indicating that TPADO consists of a reductase (TphA1 II) and a terminal oxygenase component (TphA2 II and TphA3 II). TphA1(II) 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 TphA1 II, 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 Vmax were determined to be 72+/-6 microM and 9.87+/-0.06 U/mg respectively.

Topics: Comamonas; Dioxygenases; Electron Transport; Escherichia coli; Ferredoxin-NADP Reductase; Ferredoxins; Flavin-Adenine Dinucleotide; Hydrogen-Ion Concentration; Kinetics; Molecular Weight; NAD; NADP; Phthalic Acids; Recombinant Proteins; Substrate Specificity; Temperature

2008