Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 1.3.8.17 extracted from

  • Bashiri, G.; Rehan, A.; Sreebhavan, S.; Baker, H.; Baker, E.; Squire, C.
    Elongation of the poly-gamma-glutamate tail of F420 requires both domains of the F420 gamma-glutamyl ligase (FbiB) of Mycobacterium tuberculosis (2016), J. Biol. Chem., 291, 6882-6894 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.3.8.17

Cloned(Commentary)

Cloned (Comment) Organism
-
 Mycobacterium tuberculosis

Crystallization (Commentary)

Crystallization (Comment) Organism
structures of the C-terminal domain of FbiB in apo-, F420-0-, and FMN-bound states, displaying distinct sites for F420-0 and FMN ligands that partially overlap Mycobacterium tuberculosis

Organism

Organism UniProt Comment Textmining
Mycobacterium tuberculosis P9WP79 cf. EC 6.3.2.31, EC 6.3.2.34
-
Mycobacterium tuberculosis H37Rv P9WP79 cf. EC 6.3.2.31, EC 6.3.2.34
-

General Information

General Information Comment Organism
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 Mycobacterium tuberculosis