Premium
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
Author(s) -
Wolff Murielle,
Seemann Myriam,
Tse Sum Bui Bernadette,
Frapart Yves,
Tritsch Denis,
Estrabot Ana Garcia,
Rodrı́guez-Concepción Manuel,
Boronat Albert,
Marquet Andrée,
Rohmer Michel
Publication year - 2003
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(03)00317-x
Subject(s) - flavodoxin , chemistry , enzyme , reductase , biosynthesis , escherichia coli , nicotinamide adenine dinucleotide phosphate , biochemistry , stereochemistry , dehydrogenase , cofactor , nicotinamide adenine dinucleotide , nad+ kinase , ferredoxin , oxidase test , gene
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.