EC Number |
Title |
Organism |
---|
4.1.99.26 | Bioinformatic evidence for a widely distributed, ribosomally produced electron carrier precursor, its maturation proteins, and its nicotinoprotein redox partners |
Mycobacterium tuberculosis |
4.1.99.26 | Bioinformatic evidence for a widely distributed, ribosomally produced electron carrier precursor, its maturation proteins, and its nicotinoprotein redox partners |
Mycobacterium tuberculosis H37Rv |
4.1.99.26 | Bioinformatic evidence for a widely distributed, ribosomally produced electron carrier precursor, its maturation proteins, and its nicotinoprotein redox partners |
Mycobacterium tuberculosis ATCC 25618 |
4.1.99.26 | Mechanistic elucidation of the mycofactocin-biosynthetic radical S-adenosylmethionine protein, MftC |
Mycobacterium ulcerans |
4.1.99.26 | Mechanistic elucidation of the mycofactocin-biosynthetic radical S-adenosylmethionine protein, MftC |
Mycobacterium ulcerans Agy99 |
4.1.99.26 | Occurrence, function, and biosynthesis of mycofactocin |
Mycobacterium sp. |
4.1.99.26 | Spectroscopic and electrochemical characterization of the mycofactocin biosynthetic protein, MftC, provides insight into its redox flipping mechanism |
Mycobacterium ulcerans |
4.1.99.26 | Spectroscopic and electrochemical characterization of the mycofactocin biosynthetic protein, MftC, provides insight into its redox flipping mechanism |
Mycobacterium ulcerans Agy99 |
4.1.99.26 | The creatininase homolog MftE from Mycobacterium smegmatis catalyzes a peptide cleavage reaction in the biosynthesis of a novel ribosomally synthesized post-translationally modified peptide (RiPP) |
Mycolicibacterium smegmatis |
4.1.99.26 | The creatininase homolog MftE from Mycobacterium smegmatis catalyzes a peptide cleavage reaction in the biosynthesis of a novel ribosomally synthesized post-translationally modified peptide (RiPP) |
Mycolicibacterium smegmatis ATCC 700084 |