Identification of the Final Two Genes Functioning in Methanofuran Biosynthesis in Methanocaldococcus jannaschii

  title={Identification of the Final Two Genes Functioning in Methanofuran Biosynthesis in Methanocaldococcus jannaschii},
  author={Yu Kuo Wang and Huimin Xu and Michael K. Jones and Robert H. White},
  journal={Journal of Bacteriology},
  pages={2850 - 2858}
ABSTRACT All methanofuran structural variants contain a basic core structure of 4-[N-(γ-l-glutamyl)-p-(β-aminoethyl)phenoxymethyl]-(aminomethyl)furan (APMF-Glu) but have different side chains depending on the source organism. Recently, we identified four genes (MfnA, MfnB, MfnC, and MfnD) that are responsible for the biosynthesis of the methanofuran precursor γ-glutamyltyramine and 5-(aminomethyl)-3-furanmethanol-phosphate (F1-P) from tyrosine, glutamate, glyceraldehyde-3-P, and alanine in… 
The One-carbon Carrier Methylofuran from Methylobacterium extorquens AM1 Contains a Large Number of α- and γ-Linked Glutamic Acid Residues*
The structure of the cofactor, which was identified in cell extracts and further purified, was determined to consist of a polyglutamic acid side chain linked to a core structure similar to the one present in archaeal methanofuran variants.
Structure of Methylofuran in Methylobacterium extorquens AM 1 1 The One-carbon Carrier Methylofuran from Methylobacterium extorquens AM 1 Contains a Large Number of Alpha-and Gamma-linked Glutamic Acid Residues
The elucidation of the structure of the cofactor presented here sets the basis for further research on this cofactor, which is probably the largest cofactor known so far.
Industrial production, application, microbial biosynthesis and degradation of furanic compound, hydroxymethylfurfural (HMF)
Understanding the structure, function and catalytic mechanism of MfnB (4-(hydroxymethyl)-2-furancarboxyaldehyde-phosphate synthase) and hmfH (HMF oxidase) will provide important insights in enzyme engineering, which eventually will find industry applications in mass-production of biobased polymers and other bulk chemicals in future.
Genome-Scale Metabolic Modeling of Archaea Lends Insight into Diversity of Metabolic Function
It is shown how the metabolic models can be used to study the evolution of metabolism in archaea and the utility of GEMs to evolutionary studies, far beyond their original purpose of metabolic modeling.
Genome-wide gene expression and RNA half-life measurements allow predictions of regulation and metabolic behavior in Methanosarcina acetivorans
The results suggest that M. acetivorans employs extensive post-transcriptional regulation to optimize key metabolic steps, and more generally that degradation could play a much greater role in optimizing an organism’s metabolism than previously thought.
Interactive functional networks in microbiota
The aim of this thesis was to elucidate how various microbial communities work, with a focus on next generation sequencing data, and to discuss the relevant issues with modelling microbial communities, as well as overall scientific integrity in relationship with microbiome research.


Identification and characterization of a tyramine-glutamate ligase (MfnD) involved in methanofuran biosynthesis.
The identification of an ATP-grasp enzyme encoded by the gene Mefer_1180 in Methanocaldococcus fervens that catalyzes the ATP-dependent addition of one glutamate to tyramine via a γ-linked amide bond is reported, providing the first report describing the enzymology of the incorporation of the initial l-glutamate molecule into the methanofuran structure.
Identification of structurally diverse methanofuran coenzymes in methanococcales that are both N-formylated and N-acetylated.
This work uses liquid chromatography coupled with high-resolution mass spectrometry and a variety of biochemical methods to deduce the unique structures of MFs present in four different methanogen in the order Methanococcales, the first detailed characterization of the MF occurring in methanogens of this order.
β-Alanine Biosynthesis in Methanocaldococcus jannaschii
It was shown that the decarboxylation of aspartate was the only source of β-alanine in cell extracts of M. jannaschii, and the MJ0050 gene was demonstrated to complement the Escherichia coli panD deletion mutant cells, thus confirming the function of this gene in vivo.
Biosynthesis of the 5-(Aminomethyl)-3-furanmethanol moiety of methanofuran.
We have established the biosynthetic pathway and the associated genes for the biosynthesis of the 5-(aminomethyl)-3-furanmethanol (F1) moiety of methanofuran in the methanogenic archaeon
Mechanism of the Enzymatic Synthesis of 4-(Hydroxymethyl)-2- furancarboxaldehyde-phosphate (4-HFC-P) from Glyceraldehyde-3-phosphate Catalyzed by 4-HFC-P Synthase.
The biochemical characterization of the recombinantly expressed MfnB is described to understand its catalytic mechanism and structural analysis and molecular docking are predicted to predict the potential binding sites for two GA-3P molecules in the active site.
Structural diversity among methanofurans from different methanogenic bacteria
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  • Chemistry
    Journal of bacteriology
  • 1988
An examination of the methanofurans isolated from a wide range of methanogenic bacteria and from Archaeoglobus fulgidus has revealed at least five chromatographically distinct methanofurans. Bacteria
Characterization of the formyltransferase from Methylobacterium extorquens AM1.
The purification and characterization of formylmethanofuran-tetrahydromethanopterin formyltransferase (Ftr), which catalyzes the reversible formation of formymethan ofuran (formylMFR) and tetrahydromeethan helicopteropterin (H4MPT) from N5-formylH4 MPT and methanofuran (MFR), is described.
Enzymology of one-carbon metabolism in methanogenic pathways.
  • J. Ferry
  • Biology, Chemistry
    FEMS microbiology reviews
  • 1999
Recent progress on the enzymology of one-carbon reactions in these pathways has raised the level of understanding with regard to the physiology and molecular biology of methanogenesis and provided a foundation for future studies on the structure/function of these novel enzymes.