ArticleThe Journal of biological chemistry2008
Molecular insights into the biosynthesis of the F420 coenzyme.
Article in The Journal of biological chemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 51 citations in OpenAlex.
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- Identification ofInfection and drug resistance · 2024Review
- Emergence of Canonical and Noncanonical Genomic Variants followingAntimicrobial agents and chemotherapy · 2023Article
- Multi-epitope chimeric vaccine designing and novel drug targets prioritization against multi-drug resistantFrontiers in microbiology · 2022Article
- Article
- Cofactor F420: an expanded view of its distribution, biosynthesis and roles in bacteria and archaea.FEMS microbiology reviews · 2021Article
- Open Issues for Protein Function Assignment inGenes · 2021Article
- A proposed carbon-utilization and virulence protein A, CuvA (Rv1422), from Mycobacterium tuberculosis H37Rv: crystallization, X-ray diffraction analysis and ligand binding.Acta crystallographica. Section F, Structural biology communications · 2020Article
- Article
- A revised biosynthetic pathway for the cofactor FNature communications · 2019Article
- YvcK, a protein required for cell wall integrity and optimal carbon source utilization, binds uridine diphosphate-sugars.Scientific reports · 2017Article
- Cofactor Tail Length Modulates Catalysis of Bacterial FFrontiers in microbiology · 2017Article
- The Listeria monocytogenes PASTA Kinase PrkA and Its Substrate YvcK Are Required for Cell Wall Homeostasis, Metabolism, and Virulence.PLoS pathogens · 2016Article
- Physiology, Biochemistry, and Applications of F420- and Fo-Dependent Redox Reactions.Microbiology and molecular biology reviews : MMBR · 2016Review
- Review article: inhibition of methanogenic archaea by statins as a targeted management strategy for constipation and related disorders.Alimentary pharmacology & therapeutics · 2016Review
- Mutations in genes for the F420 biosynthetic pathway and a nitroreductase enzyme are the primary resistance determinants in spontaneous in vitro-selected PA-824-resistant mutants of Mycobacterium tuberculosis.Antimicrobial agents and chemotherapy · 2015Article
- Mycobacterial gene cuvA is required for optimal nutrient utilization and virulence.Infection and immunity · 2014Article
- α-Galactosidase/sucrose kinase (AgaSK), a novel bifunctional enzyme from the human microbiome coupling galactosidase and kinase activities.The Journal of biological chemistry · 2011Article
- Genetic control of biosynthesis and transport of riboflavin and flavin nucleotides and construction of robust biotechnological producers.Microbiology and molecular biology reviews : MMBR · 2011Review
- More than 200 genes required for methane formation from H₂ and CO₂ and energy conservation are present in Methanothermobacter marburgensis and Methanothermobacter thermautotrophicus.Archaea (Vancouver, B.C.) · 2011Article
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Authors and funding
15 authors at 6 institutions in 2 countries.
Funding
Abstract
Coenzyme F(420), a hydride carrier, is found in Archaea and some bacteria and has crucial roles in methanogenesis, antibiotic biosynthesis, DNA repair, and activation of antitubercular compounds. CofD, 2-phospho-l-lactate transferase, catalyzes the last step in the biosynthesis of F(420)-0 (F(420) without polyglutamate), by transferring the lactyl phosphate moiety of lactyl(2)diphospho-(5')guanosine to 7,8-didemethyl-8-hydroxy-5-deazariboflavin ribitol (Fo). CofD is highly conserved among F(420)-producing organisms, and weak sequence homologs are also found in non-F(420)-producing organisms. This superfamily does not share any recognizable sequence conservation with other proteins. Here we report the first crystal structures of CofD, the free enzyme and two ternary complexes, with Fo and P(i) or with Fo and GDP, from Methanosarcina mazei. The active site is located at the C-terminal end of a Rossmann fold core, and three large insertions make significant contributions to the active site and dimer formation. The observed binding modes of Fo and GDP can explain known biochemical properties of CofD and are also supported by our binding assays. The structures provide significant molecular insights into the biosynthesis of the F(420) coenzyme. Large structural differences in the active site region of the non-F(420)-producing CofD homologs suggest that they catalyze a different biochemical reaction.
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