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

@article{Allen2014IdentificationOS,
  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},
  journal={Biochemistry},
  year={2014},
  volume={53 39},
  pages={
          6199-210
        }
}
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

TLDR
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.

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TLDR
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.

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TLDR
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.

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TLDR
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*

TLDR
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

TLDR
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.

TLDR
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.

TLDR
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.

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