| Literature DB >> 12706830 |
Murielle Wolff1, Myriam Seemann, Bernadette Tse Sum Bui, Yves Frapart, Denis Tritsch, Ana Garcia Estrabot, Manuel Rodríguez-Concepción, Albert Boronat, Andrée Marquet, Michel Rohmer.
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.Entities:
Mesh:
Substances:
Year: 2003 PMID: 12706830 DOI: 10.1016/s0014-5793(03)00317-x
Source DB: PubMed Journal: FEBS Lett ISSN: 0014-5793 Impact factor: 4.124