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Literature summary extracted from

  • Elitas, M.
    Isoniazid killing of Mycobacterium smegmatis NADH pyrophosphatase mutant at single-cell level using microfluidics and time-lapse microscopy (2017), Sci. Rep., 7, 10770 .
    View publication on PubMedView publication on EuropePMC

Protein Variants

EC Number Protein Variants Comment Organism
3.6.1.22 additional information construction of the Mycobacterium smegmatis msm1946::Tn transposon mutant, single-cell analysis for isoniazid-treated mutant msm1946-NADH pyrophosphatase using microfluidics and automated time-lapse microscopy Mycolicibacterium smegmatis

Organism

EC Number Organism UniProt Comment Textmining
3.6.1.22 Mycolicibacterium smegmatis A0QTS4
-
-
3.6.1.22 Mycolicibacterium smegmatis ATCC 700084 A0QTS4
-
-
3.6.1.22 Mycolicibacterium smegmatis mc(2)155 A0QTS4
-
-

Synonyms

EC Number Synonyms Comment Organism
3.6.1.22 msm1946
-
 Mycolicibacterium smegmatis
3.6.1.22 MSMEG_1946
-
 Mycolicibacterium smegmatis
3.6.1.22 NADH pyrophosphatase
-
 Mycolicibacterium smegmatis
3.6.1.22 NudC
-
 Mycolicibacterium smegmatis

General Information

EC Number General Information Comment Organism
3.6.1.22 malfunction the msm1946-NADH pyrophosphatase mutant shows increased killing rate during exposure to isozianide and ethionamide (INH and ETH) as compared to wild-type. The msm1946::Tn transposon mutant grows indistinguishably from wild-type bacteria in standard 7H9 liquid medium. The ability of the mutant cells to form colonies on standard LB solid medium is also indistinguishable from wild-type cells. The impact of msm1946 disruption on drug-mediated killing is found to be specific to INH and ETH. Elevated levels of NADH in the msm1946::Tn mutant can contribute to enhanced formation of the INH-NAD adduct Mycolicibacterium smegmatis
3.6.1.22 additional information insights on isoniazid killing mechanism by microfluidics and automated time-lapse microscopy single-cell analysis, overview Mycolicibacterium smegmatis
3.6.1.22 physiological function mycobacterial NADH diphosphatase isoforms play an important role for the mechanism of isoniazid (INH) and ethionamide activation. INH has been one of the most effective and widely used antitubercular drugs, it is a pro-drug that is oxidatively activated in vivo by the katG-encoded mycobacterial catalase-peroxidase to generate covalently modified INH-NAD adduct. INH-NAD adduct inhibits InhA, an enoyl reductase that is a member of the type II dissociated fatty acid biosynthesis pathway. INH interferes with the biosynthesis of mycolic acids, the very long chain fatty acid components of the mycobacterial cell wall Mycolicibacterium smegmatis