Generation of formate by the formyltransferase/hydrolase complex (Fhc) from Methylobacterium extorquens AM1

@article{Pomper2002GenerationOF,
  title={Generation of formate by the formyltransferase/hydrolase complex (Fhc) from Methylobacterium extorquens AM1},
  author={B K Pomper and Olivier Saurel and Alain Milon and Julia A. Vorholt},
  journal={FEBS Letters},
  year={2002},
  volume={523}
}
Methylobacterium extorquens AM1 possesses a formyltransferase (Ftr) complex that is essential for growth in the presence of methanol and involved in formaldehyde oxidation to CO2. One of the subunits of the complex carries the catalytic site for transfer of the formyl group from tetrahydromethanopterin to methanofuran (MFR). We now found via nuclear magnetic resonance‐based studies that the Ftr complex also catalyzes the hydrolysis of formyl‐MFR and generates formate. The enzyme was therefore… Expand
Characterization of Two Methanopterin Biosynthesis Mutants of Methylobacterium extorquens AM1 by Use of a Tetrahydromethanopterin Bioassay
TLDR
Results provide the first biochemical evidence for H(4)MPT biosynthesis genes in bacteria. Expand
Purification of the Formate-Tetrahydrofolate Ligasefrom Methylobacterium extorquens AM1 and Demonstrationof Its Requirement for MethylotrophicGrowth
TLDR
The purification and characterization of FtfL from M. extorquens AM1 and the confirmation that this enzyme is encoded by an ftfL homolog identified previously through transposon mutagenesis suggest an alternative model for the role of the H(4)F pathway in this organism in which it functions to convert formate to methylene H( 4)F for assimilatory metabolism. Expand
The tungsten-containing formate dehydrogenase from Methylobacterium extorquens AM1: purification and properties.
TLDR
The beta-subunit of FDH1 contains putative motifs for binding FMN and NAD, as well as an iron-sulfur cluster binding motif, and appears to be a fusion protein related to NuoE-like subunits of known NADH-ubiquinone oxidoreductases. Expand
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. Expand
Structural diversity of the coenzyme methylofuran and identification of enzymes for the biosynthesis of its polyglutamate side chain
TLDR
Using gene deletions in combination with LC-MS analyses, three genes are identified that are essential for MYFR biosynthesis, and are renamed OrfY and Orf5 to MyfA and MyfB to highlight that these enzymes are specifically involved in MY FR biosynthesis. Expand
Molybdenum and tungsten-dependent formate dehydrogenases
TLDR
This review will highlight the present knowledge about the diverse physiological roles of FDH in prokaryotes, their modular structural organisation and active site structures and the mechanistic strategies followed to accomplish the formate oxidation. Expand
Methylofuran is a prosthetic group of the formyltransferase/hydrolase complex and shuttles one-carbon units between two active sites
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. Expand
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
Methylobacterium extorquens AM1 uses dedicated cofactors for one-carbon unit conversion. Based on the sequence identities of enzymes and activity determinations, a methanofuran (MFR) analog wasExpand
Novel Dephosphotetrahydromethanopterin Biosynthesis Genes Discovered via Mutagenesis in Methylobacterium extorquens AM1
TLDR
Methylobacterium extorquens AM1 was used to explore the genetics of dephosphotetrahydromethanopterin biosynthesis, and six strains with mutations in eight "archaeal-type" genes linked on the chromosome were found to be dH(4)MPT negative. Expand
Formaldehyde-Detoxifying Role of theTetrahydromethanopterin-Linked Pathway in MethylobacteriumextorquensAM1
TLDR
The role of the H(4)MPT pathway is defined as the primary formaldehyde oxidation and detoxification pathway in M. extorquens AM1 and null mutants were generated in genes previously thought to be essential, indicating that the H (4) Parliamentary pathway is not absolutely required during growth on multicarbon compounds. Expand
...
1
2
3
4
5
...

References

SHOWING 1-10 OF 23 REFERENCES
Characterization of the formyltransferase from Methylobacterium extorquens AM1.
TLDR
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. Expand
The NADP-dependent methylene tetrahydromethanopterin dehydrogenase in Methylobacterium extorquens AM1.
TLDR
The purification of this novel enzyme to apparent homogeneity identified to be the mtdA gene product catalyzed the dehydrogenation of methylene H4MPT with NADP+ rather than with NAD+, with a specific activity of approximately 400 U/mg of protein. Expand
Characterization of a second methylene tetrahydromethanopterin dehydrogenase from Methylobacterium extorquens AM1.
TLDR
It is reported that both MtdB and MtdA can be heterologously overproduced in Escherichia coli making these two enzymes readily available for structural analysis. Expand
[28] Tetrahydromethanopterin-specific enzymes from Methanopyrus kandleri
TLDR
This chapter describes the purification, assay, and properties of the five characterized H 4 MPT-specific enzymes from M. kandleri and provides a description of the isolation of the coenzymes required to assay these enzymes. Expand
Distribution of tetrahydromethanopterin-dependent enzymes in methylotrophic bacteria and phylogeny of methenyl tetrahydromethanopterin cyclohydrolases.
TLDR
H(4)MPT-dependent enzyme activities were detected in all of the methylotrophic and methanotrophic proteobacteria tested that assimilate formaldehyde by the serine or ribulose monophosphate pathway and in autotrophic Xanthobacter strains. Expand
Novel formaldehyde-activating enzyme in Methylobacterium extorquens AM1 required for growth on methanol.
TLDR
A previously unknown enzyme that efficiently catalyzes the removal of formaldehyde is found in the alpha-proteobacterium M. extorquens AM1 and predicted to be encoded by uncharacterized genes from archaea, indicating that this type of enzyme occurs outside the methylotrophic bacteria. Expand
C1 transfer enzymes and coenzymes linking methylotrophic bacteria and methanogenic Archaea.
TLDR
Methanogenic and sulfate-reducing Archaea are considered to have an energy metabolism involving C1 transfer coenzymes and enzymes unique for this group of strictly anaerobic microorganisms, and an aerobic methylotrophic bacterium was found to contain a cluster of genes that are predicted to encode some of these enzymes. Expand
The role of formylmethanofuran: tetrahydromethanopterin formyltransferase in methanogenesis from carbon dioxide.
TLDR
Reconstitution experiments established that the formyltransferase is an essential enzyme for the conversion of carbon dioxide to methane and substantiate the role of 5-formyl-H4MPT as an intermediate of methanogenesis. Expand
Re‐face stereospecificity of NADP dependent methylenetetrahydromethanopterin dehydrogenase from Methylobacterium extorquens AM1 as determined by NMR spectroscopy
TLDR
It was found that the pro-R hydrogen of methylene‐H4MPT is transferred by MtdA into the pro‐R position of NADPH. Expand
H2-forming methylenetetrahydromethanopterin dehydrogenase, a novel type of hydrogenase without iron-sulfur clusters in methanogenic archaea.
TLDR
Properties of the H2-forming methylenetetrahydromethanopterin dehydrogenase from Methanobacterium wolfei are described indicating that the enzyme from this methanogenic archaeon is very similar to the enzymes from M. thermoautotrophicum with respect both to molecular and catalytic properties. Expand
...
1
2
3
...