EC Number   |
Title |
Organism |
|---|
  1.3.98.7 | Bioinformatic evidence for a widely distributed, ribosomally produced electron carrier precursor, its maturation proteins, and its nicotinoprotein redox partners |
Mycobacterium tuberculosis |
| 1.3.98.7 | Bioinformatic evidence for a widely distributed, ribosomally produced electron carrier precursor, its maturation proteins, and its nicotinoprotein redox partners |
Mycobacterium tuberculosis H37Rv |
| 1.3.98.7 | Mechanistic elucidation of the mycofactocin-biosynthetic radical S-adenosylmethionine protein, MftC |
Mycobacterium ulcerans |
| 1.3.98.7 | Mechanistic elucidation of the mycofactocin-biosynthetic radical S-adenosylmethionine protein, MftC |
Mycobacterium ulcerans Agy99 |
| 1.3.98.7 | Mycofactocin is associated with ethanol metabolism in mycobacteria |
Mycolicibacterium smegmatis |
| 1.3.98.7 | Mycofactocin is associated with ethanol metabolism in mycobacteria |
Mycolicibacterium smegmatis ATCC 700084 |
| 1.3.98.7 | Spectroscopic and electrochemical characterization of the mycofactocin biosynthetic protein, MftC, provides insight into its redox flipping mechanism |
Mycobacterium ulcerans |
| 1.3.98.7 | Spectroscopic and electrochemical characterization of the mycofactocin biosynthetic protein, MftC, provides insight into its redox flipping mechanism |
Mycobacterium ulcerans Agy99 |
| 1.3.98.7 | The radical S-adenosyl-L-methionine enzyme MftC catalyzes an oxidative decarboxylation of the C-terminus of the MftA peptide |
Mycolicibacterium smegmatis |
| 1.3.98.7 | The radical S-adenosyl-L-methionine enzyme MftC catalyzes an oxidative decarboxylation of the C-terminus of the MftA peptide |
Mycolicibacterium smegmatis ATCC 700084 |
