4.5 Article

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

Journal

FEBS LETTERS
Volume 541, Issue 1-3, Pages 115-120

Publisher

WILEY
DOI: 10.1016/S0014-5793(03)00317-X

Keywords

dimethylallyl diphosphate; isopentenyl diphosphate; isoprenoid; LytB; 2-C-methyl-D-erythritol 4-phosphate pathway; (E)-4-hydroxy-3-methylbut-2-enyl diphosphate

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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. (C) 2003 Federation of European Biochemical Societies. Published by Elsevier Science B.V. All rights reserved.

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