Identification of structurally diverse methanofuran coenzymes in methanococcales that are both N-formylated and N-acetylated.

  title={Identification of structurally diverse methanofuran coenzymes in methanococcales that are both N-formylated and N-acetylated.},
  author={Kylie D. Allen and Robert H. White},
  volume={53 39},
Methanofuran (MF) is a coenzyme necessary for the first step of methanogenesis from CO2. The well-characterized MF core structure is 4-[N-(γ-l-glutamyl-γ-l-glutamyl)-p-(β-aminoethyl)phenoxymethyl]-2-(aminomethyl)furan (APMF-γ-Glu2). Three different MF structures that differ on the basis of the composition of their side chains have been determined previously. Here, we use liquid chromatography coupled with high-resolution mass spectrometry and a variety of biochemical methods to deduce the… 

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

The results show that MfnF catalyzes the formation of an ether bond during methanofuran biosynthesis, and further expands the functionality of this enzyme family, while MfnE is a promiscuous enzyme and its possible physiological role is to produce F1-PP.

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.

The one-carbon carrier methylofuran from Methylobacterium extorquens AM1 contains a large number of alpha- and gamma-linked glutamic acid residues

The structure of the cofactor, which is termed methylofuran, is determined to consist of a polyglutamic acid side chain linked to a core structure similar to the one present in archaeal methanofuran variants.

Methylofuran is a prosthetic group of the formyltransferase/hydrolase complex and shuttles one-carbon units between two active sites

The crystal structure of the formyltransferase/hydrolase complex from Methylorubrum extorquens demonstrates that the one-carbon carrier methylofuran tightly binds to the enzyme via its extended and branched polyglutamate chain.

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.

Archaeal pseudomurein and bacterial murein cell wall biosynthesis share a common evolutionary ancestry

Taxonomic distribution, gene cluster and phylogenetic analyses that confirm orthologues of 13 bacterial murein biosynthesis enzymes in pseudomurein-containing methanogens, most of which are distantly related to their bacterial counterparts, strongly indicate that muresin and pseudomuredin biosynthetic pathways share a common evolutionary history.

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.

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.



Structural diversity among methanofurans from different methanogenic bacteria

  • R. White
  • 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

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

CofE catalyzes the addition of two glutamates to F420-0 in F420 coenzyme biosynthesis in Methanococcus jannaschii.

The protein product of the Methanococcus jannaschii MJ0768 gene has been expressed in Escherichia coli, purified to homogeneity, and shown to catalyze the GTP-dependent addition of two l-glutamates

Molecular Insights into the Biosynthesis of the F420 Coenzyme*

The first crystal structures of CofD are reported, the free enzyme and two ternary complexes, with Fo and Pi or withfo and GDP, from Methanosarcina mazei, and provide significant molecular insights into the biosynthesis of the F420 coenzyme.

Biosynthesis of the 2-(aminomethyl)-4-(hydroxymethyl)furan subunit of methanofuran.

It was concluded that F1 is generated by the condensation of dihydroxyacetone phosphate with pyruvate after elimination of 2 mol of water and reduction of the carboxylic acid to an aldehyde and subsequent transamination would produce the phosphate ester of F1.

Structures of coenzyme F420 in Mycobacterium species

Peptidase treatment of F420 created F420 derivatives that may be useful for the assay of enzymes involved in F420 biosynthesis, which accounted for about 1–7% of the total deazaflavin in cells.

Structures of coenzyme F(420) in Mycobacterium species.

The structure of coenzyme F(420) in Mycobacterium smegmatis was examined using proton NMR, amino acid analysis, and HPLC, and peptidase treatment created F( 420) derivatives that may be useful for the assay of enzymes involved in F (420) biosynthesis.

Methanofuran (carbon dioxide reduction factor), a formyl carrier in methane production from carbon dioxide in Methanobacterium.

Formylmethanofuran was enzymically converted to 14CH4 in the presence of CH3-S-CoM [2-(methylthio)ethanesulfonic acid], hydrogen, and methanopterin, establishing the formyl moiety as an intermediate in methanogenesis.

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.