Isoprenoid biosynthesis via the methylerythritol phosphate pathway: the (E)-4-hydroxy-3-methylbut-2-enyl diphosphate reductase (LytB/IspH) from Escherichia coli is a [4Fe-4S] protein |
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Authors: | Wolff Murielle Seemann Myriam Tse Sum Bui Bernadette Frapart Yves Tritsch Denis Garcia Estrabot Ana Rodríguez-Concepción Manuel Boronat Albert Marquet Andrée Rohmer Michel |
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Institution: | Université Louis Pasteur, UMR CNRS 7123, Institut Le Bel, Strasbourg, France. |
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Abstract: | The last enzyme (LytB) of the methylerythritol phosphate pathway for isoprenoid biosynthesis catalyzes the reduction of (E)-4-hydroxy-3-methylbut-2-enyl diphosphate into isopentenyl diphosphate and dimethylallyl diphosphate. This enzyme possesses a dioxygen-sensitive 4Fe-4S] cluster. This prosthetic group was characterized in the Escherichia coli enzyme by UV/visible and electron paramagnetic resonance spectroscopy after reconstitution of the purified protein. Enzymatic activity required the presence of a reducing system such as flavodoxin/flavodoxin reductase/reduced nicotinamide adenine dinucleotide phosphate or the photoreduced deazaflavin radical. |
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