EC Number   |
General Information |
Reference |
|---|
   6.3.2.34 | physiological function |
both genes fbiA and fbiB are essential for normal coenzyme F420-5,6 production. fbiA and fbiB constitute an operon. Very low levels of fbiB mRNA are produced by the fbiA mutant |
-, 761374 |
| 6.3.2.34 | physiological function |
FbiB produces cofactor F420 with predominantly 5-7 L-glutamate residues in the poly-gamma-glutamate tail, reactions of EC 6.3.2.31 and 6.3.2.34. The N-terminal domain of FbiB is homologous to CofE with an annotated gamma-glutamyl ligase activity, whereas the C-terminal domain has sequence similarity to an FMN-dependent family of nitroreductase enzymes. Communication between the two domains is critical for full gamma-glutamyl ligase activity |
-, 745359 |
| 6.3.2.34 | physiological function |
in vitro, MtbFbiB synthesizes side chains containing up to seven glutamate residues if cofactor F420 is presented to the enzyme in a two-electron reduced state (F420H2). The polyglutamylation process requires the assistance of F420-dependent glucose-6-phosphate dehydrogenase (Fgd) which reduces F420 to F420H2. Starting with F420-0H2, the amino-terminal domain of FbiB may build F420-2H2, which is then transferred to the carboxy-terminal domain for further glutamylation. F420-2H2 modifies the carboxy-terminal domain structurally to accommodate longer glutamyl chains |
-, 761392 |
