Article
N-terminal truncations in the FhlA protein result in formate- and MoeA-independent expression of the hyc (formate hydrogenlyase) operon of Escherichia coli.
Microbiology (Reading, England) - 1 Nov 2001
Self W T, Hasona A, Shanmugam K T
Abstract excerpt
The formate hydrogenlyase complex of Escherichia coli catalyses the cleavage of formate to CO2 and H2 and consists of a molybdoenzyme formate dehydrogenase-H, hydrogenase 3 and intermediate electron carriers. The structural genes of this enzyme complex are activated by the FhlA protein in the presence of both formate and molybdate; ModE-Mo serves as a secondary activator. Mutational analysis of the FhlA protein...
Topics
- ATP-Binding Cassette Transporters
- Adenosine Triphosphatases
- Bacterial Proteins
- Binding Sites
- Enzyme Activation
- Escherichia coli
- Escherichia coli Proteins
- Formate Dehydrogenases
- Formates
- Hydrogenase
- Lac Operon
- Molybdenum
- Multienzyme Complexes