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Results 1 - 8 of 8
EC Number Metals/Ions Commentary Reference
Display the word mapDisplay the reaction diagram Show all sequences 1.13.12.19Fe2+ at the active site, enzyme acts as a bidentate ligand and it forms a complex with Fe2+. The Fe2+ is further coordinated to a tridentate Schiff base of 2-oxoglutarate and L-arginine, whose terminal carboxylate and guanidino groups are trapped by binding sites I and II on the enzyme, respectively 714008
Display the word mapDisplay the reaction diagram Show all sequences 1.13.12.19Fe2+ required, KM value 0.059 mM 715784
Display the word mapDisplay the reaction diagram Show all sequences 1.13.12.19Fe2+ dependent on, required for catalysis 741936, 742153
Display the word mapDisplay the reaction diagram Show all sequences 1.13.12.19Fe2+ non-heme Fe(II)-dependent ethylene-forming enzyme, the metal ion is hexa-coordinated 742750
Display the word mapDisplay the reaction diagram Show all sequences 1.13.12.19Fe2+ dependent on, required for catalysis. The overall metal-binding mode of PsEFE is relatively typical for 2OG oxygenases, with the metal coordinated by His189 (C terminus of DSBH II), Asp191 (loop linking DSBH II and III), and His268 (N-terminus of DSBH VII) 743692
Display the word mapDisplay the reaction diagram Show all sequences 1.13.12.19Fe2+ dependent on, residues H189, D191 and H268 are responsible for binding the Fe(II) ligand 744563
Display the word mapDisplay the reaction diagram Show all sequences 1.13.12.19Fe2+ the nonheme iron(II) oxygenase catalyzes the oxidative decarboxylation of 2-oxoglutarate to succinate and CO2 to generate a highly reactive iron species that hydroxylates a specific alkane C-H bond, in this case targeting L-arginine (Arg) for hydroxylation 764156
Display the word mapDisplay the reaction diagram Show all sequences 1.13.12.19Fe2+ Fe2+-dependent enzyme 764978, 765536
Results 1 - 8 of 8