Cloned (Comment) | Organism |
---|---|
overexpression in Escherichia coli | Archaeoglobus fulgidus |
Crystallization (Comment) | Organism |
---|---|
hanging-drop vapour diffusion method, crystal structure of the enzyme bound with coenzyme F420. The structure resolved to 1.65 A contains two domains: an N-terminal domain characteristic of a dinucleotide-binding Rossmann fold and a smaller C-terminal domain. The nicotinamide and the deazaflavin part of the two coenzymes are bound in the cleft between the domains such that the Si-faces of both face each other at a distance of 3.1 A, which is optimal for hydride transfer | Archaeoglobus fulgidus |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Archaeoglobus fulgidus | O29370 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
reduced coenzyme F420 + NADP+ | of the two substrates NADP+ has to bind first, the binding being associated with an induced fit. The stereochemical analysis of the hydrode transfer leads to the conclusion that the observed orientation of the Si-face of coenzyme F420 towards the Si-face of NADP+ allows only the transfer of the proS hydrogen at C5 to the proS position at C4 and vice versa | Archaeoglobus fulgidus | oxidized coenzyme F420 + NADPH + H+ | - |
? |
Synonyms | Comment | Organism |
---|---|---|
AF0892 | - |
Archaeoglobus fulgidus |
F420H2:NADP+ oxidoreductase | - |
Archaeoglobus fulgidus |
Fno | - |
Archaeoglobus fulgidus |