ArticleThe Journal of biological chemistry2013
The TP0796 lipoprotein of Treponema pallidum is a bimetal-dependent FAD pyrophosphatase with a potential role in flavin homeostasis.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed.
- Flavin transferase ApbE: From discovery to applications.The Journal of biological chemistry · 2025Review
- Research Advances in Clinical Strategies and Preclinical Models for Syphilis Relapse.Infection and drug resistance · 2025Review
- Biophysical and biochemical evidence for the role of acetate kinases (AckAs) in an acetogenic pathway in pathogenic spirochetes.PloS one · 2025Article
- Article
- Structural insights into the catalytic and inhibitory mechanisms of the flavin transferase FmnB inMedComm · 2022Article
- Inhibition of bacterial FMN transferase: A potential avenue for countering antimicrobial resistance.Protein science : a publication of the Protein Society · 2022Article
- AnInfection and immunity · 2021Article
- Article
- Conserved residue His-257 ofThe Journal of biological chemistry · 2019Article
- Functional insights from proteome-wide structural modeling of Treponema pallidum subspecies pallidum, the causative agent of syphilis.BMC structural biology · 2018Article
- The Membrane-Bound C Subunit of Reductive Dehalogenases: Topology Analysis and Reconstitution of the FMN-Binding Domain of PceC.Frontiers in microbiology · 2018Article
- Kinetic characterization of Vibrio cholerae ApbE: Substrate specificity and regulatory mechanisms.PloS one · 2017Article
- Treponema pallidum, the syphilis spirochete: making a living as a stealth pathogen.Nature reviews. Microbiology · 2016Review
- Efficient Sulfide Assimilation in Methanosarcina acetivorans Is Mediated by the MA1715 Protein.Journal of bacteriology · 2016Article
- Molecular insights into the enzymatic diversity of flavin-trafficking protein (Ftp; formerly ApbE) in flavoprotein biogenesis in the bacterial periplasm.MicrobiologyOpen · 2016Article
- The Tp0684 (MglB-2) Lipoprotein of Treponema pallidum: A Glucose-Binding Protein with Divergent Topology.PloS one · 2016Article
- Article
- Insights into the potential function and membrane organization of the TP0435 (Tp17) lipoprotein from Treponema pallidum derived from structural and biophysical analyses.Protein science : a publication of the Protein Society · 2015Article
- Alternative pyrimidine biosynthesis protein ApbE is a flavin transferase catalyzing covalent attachment of FMN to a threonine residue in bacterial flavoproteins.The Journal of biological chemistry · 2013Article
- The Treponema pallidum Outer Membrane.Current topics in microbiology and immunologyReview
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5 authors.
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Abstract
Treponema pallidum, an obligate parasite of humans and the causative agent of syphilis, has evolved the capacity to exploit host-derived metabolites for its survival. Flavin-containing compounds are essential cofactors that are required for metabolic processes in all living organisms, and riboflavin is a direct precursor of the cofactors FMN and FAD. Unlike many pathogenic bacteria, Treponema pallidum cannot synthesize riboflavin; we recently described a flavin-uptake mechanism composed of an ABC-type transporter. However, there is a paucity of information about flavin utilization in bacterial periplasms. Using a discovery-driven approach, we have identified the TP0796 lipoprotein as a previously uncharacterized Mg(2+)-dependent FAD pyrophosphatase within the ApbE superfamily. TP0796 probably plays a central role in flavin turnover by hydrolyzing exogenously acquired FAD, yielding AMP and FMN. Biochemical and structural investigations revealed that the enzyme has a unique bimetal Mg(2+) catalytic center. Furthermore, the pyrophosphatase activity is product-inhibited by AMP, indicating a possible role for this molecule in modulating FMN and FAD levels in the treponemal periplasm. The ApbE superfamily was previously thought to be involved in thiamine biosynthesis, but our characterization of TP0796 prompts a renaming of this superfamily as a periplasmic flavin-trafficking protein (Ftp). TP0796 is the first structurally and biochemically characterized FAD pyrophosphate enzyme in bacteria. This new paradigm for a bacterial flavin utilization pathway may prove to be useful for future inhibitor design.
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