EC Number   |
General Information |
Reference |
|---|
  2.7.7.105 | evolution |
analysis of the evolution of the F420 biosynthesis enzymes (CofC, CofD, CofE, CofG and CofH) to understand the origin and distribution of the cofactor, phylogenetic analysis and tree, overview. F420 biosynthesis pathways evolved through bacterial-to-archaeal horizontal gene transfers |
-, 761327 |
| 2.7.7.105 | evolution |
structure comparisons of bacterial FbiD and archaeal CofC enzymes. Mtb-FbiD adopts the same MobA-like nucleoside triphosphate transferase family protein fold as CofC: central 7-stranded beta-sheet (six parallel strands and one antiparallel), with alpha-helices packed on either side. But Mtb-FbiD lacks the protruding hairpin that is important for dimer formation in CofC |
-, 757742 |
| 2.7.7.105 | metabolism |
archaeal guanylyltransferase CofC, along with its the bacterial homologue FbiD, accepts ohosphoenolpyruvate, rather than 2-phospho-L-lactate, as the substrate, leading to the formation of the intermediate dehydro-F420-0. The enzyme is involved in the F420-0 biosynthetic pathway, overview. Dehydro-F420-0 is a bona fide metabolic intermediate that can be converted to mature F420 by FbiB in an FMNH2-dependent fashion |
-, 757742 |
| 2.7.7.105 | metabolism |
the guanylyltransferase FbiD, along with its archaeal homologue CofC, accepts phosphoenolpyruvate, rather than 2-phospho-L-lactate, as the substrate, leading to the formation of the intermediate dehydro-F420-0. The C-terminal domain of FbiB then utilizes FMNH2 to reduce dehydro-F420-0, which produces mature F420 species when combined with the gamma-glutamyl ligase activity of the N-terminal domain. The enzyme is involved in the F420-0 biosynthetic pathway, overview. Dehydro-F420-0 is a bona fide metabolic intermediate that can be converted to mature F420 by FbiB in an FMNH2-dependent fashion |
-, 757742 |
| 2.7.7.105 | more |
docking of dehydro-F420-0 into the FMNH2-bound structure of FbiD. The methylene group of dehydro F420-0 is accommodated by a small hydrophobic pocket mostly comprised of P289 and M372 allowing it to be positioned above the N5 atom of FMNH2, in a plausible Michaelis complex for hydride transfer. The phosphoenolpyruvyl group of dehydro-F420-0 most likely samples conformations within this pocket where it can be reduced |
-, 757742 |
| 2.7.7.105 | physiological function |
archaeal guanylyltransferase CofC, along with its the bacterial homologue FbiD, accepts phosphoenolpyruvate, rather than 2-phospho-L-lactate, as the substrate, leading to the formation of the intermediate dehydro-F420-0 |
-, 757742 |
| 2.7.7.105 | physiological function |
guanylyltransferase FbiD accepts phosphoenolpyruvate, rather than 2-phospho-L-lactate, as the substrate, leading to the formation of the intermediate dehydro-F420-0. The C-terminal domain of gamma-glutamyl ligase FbiB then utilizes FMNH2 to reduce dehydro-F420-0, which produces mature F420 species when combined with the gamma-glutamyl ligase activity of the N-terminal domain. Expression of the FbiABCD cluster is sufficient to produce F420 in Escherichia coli |
-, 757742 |
| 2.7.7.105 | physiological function |
the guanylyltransferase FbiD, along with its archaeal homologue CofC, accepts phosphoenolpyruvate, rather than 2-phospho-L-lactate, as the substrate, leading to the formation of the intermediate dehydro-F420-0 |
-, 757742 |
