ArticleScientific reports2017
Mycofactocin-associated mycobacterial dehydrogenases with non-exchangeable NAD cofactors.
Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 26 citations in OpenAlex.
- A Unique Insertion Loop Facilitates Tight NADInternational journal of molecular sciences · 2026Article
- Identification, functional characterization, and structural analysis of an atypical l-threonate 3-dehydrogenase.The Journal of biological chemistry · 2026Article
- Fitness and adaptive evolution of a Rhodococcus sp. harboring dioxin-catabolic plasmids.World journal of microbiology & biotechnology · 2025Article
- Rv0687 a Putative Short-Chain Dehydrogenase Is Required for In Vitro and In Vivo Survival ofInternational journal of molecular sciences · 2024Article
- Mechanism of Action of Ribosomally Synthesized and Post-Translationally Modified Peptides.Chemical reviews · 2022Review
- Article
- New developments in RiPP discovery, enzymology and engineering.Natural product reports · 2021Review
- MftD Catalyzes the Formation of a Biologically Active Redox Center in the Biosynthesis of the Ribosomally Synthesized and Post-translationally Modified Redox Cofactor Mycofactocin.Journal of the American Chemical Society · 2019Article
- Article
- Assessing the Flexibility of the Prochlorosin 2.8 Scaffold for Bioengineering Applications.ACS synthetic biology · 2019Article
- Occurrence, function, and biosynthesis of mycofactocin.Applied microbiology and biotechnology · 2019Review
- Spectroscopic and Electrochemical Characterization of the Mycofactocin Biosynthetic Protein, MftC, Provides Insight into Its Redox Flipping Mechanism.Biochemistry · 2019Article
- Mycofactocin Biosynthesis Proceeds through 3-Amino-5-[( p-hydroxyphenyl)methyl]-4,4-dimethyl-2-pyrrolidinone (AHDP); Direct Observation of MftE Specificity toward MftA.Biochemistry · 2018Article
- At the confluence of ribosomally synthesized peptide modification and radicalThe Journal of biological chemistry · 2017Review
- Mechanistic elucidation of the mycofactocin-biosynthetic radicalThe Journal of biological chemistry · 2017Article
Corrections and comments
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Authors and funding
13 authors at 3 institutions in 1 country.
Funding
Abstract
During human infection, Mycobacterium tuberculosis (Mtb) survives the normally bacteriocidal phagosome of macrophages. Mtb and related species may be able to combat this harsh acidic environment which contains reactive oxygen species due to the mycobacterial genomes encoding a large number of dehydrogenases. Typically, dehydrogenase cofactor binding sites are open to solvent, which allows NAD/NADH exchange to support multiple turnover. Interestingly, mycobacterial short chain dehydrogenases/reductases (SDRs) within family TIGR03971 contain an insertion at the NAD binding site. Here we present crystal structures of 9 mycobacterial SDRs in which the insertion buries the NAD cofactor except for a small portion of the nicotinamide ring. Line broadening and STD-NMR experiments did not show NAD or NADH exchange on the NMR timescale. STD-NMR demonstrated binding of the potential substrate carveol, the potential product carvone, the inhibitor tricyclazol, and an external redox partner 2,6-dichloroindophenol (DCIP). Therefore, these SDRs appear to contain a non-exchangeable NAD cofactor and may rely on an external redox partner, rather than cofactor exchange, for multiple turnover. Incidentally, these genes always appear in conjunction with the mftA gene, which encodes the short peptide MftA, and with other genes proposed to convert MftA into the external redox partner mycofactocin.
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