Reductive activation of the methyl-tetrahydromethanopterin: coenzyme M methyltransferase from Methanobacterium thermoautotrophicum strain ΔH

@article{Kengen2004ReductiveAO,
  title={Reductive activation of the methyl-tetrahydromethanopterin: coenzyme M methyltransferase from Methanobacterium thermoautotrophicum strain $\Delta$H},
  author={Serv{\'e} W.M. Kengen and J J Mosterd and Rob L. H. Nelissen and Jan T. Keltjens and Chris van der Drift and Godfried D. Vogels},
  journal={Archives of Microbiology},
  year={2004},
  volume={150},
  pages={405-412}
}
The enzymatic conversion of formaldehyde to CH3S-CoM in crude extracts of Methanobacterium thermoautotrophicum was used as a means to investigate the methyl-tetrahydromethanopterin: HS-CoM methyltransferase reaction. All components necessary for formaldehyde conversion were shown to be present in a soluble protein fraction. This soluble cell fraction still contained a major amount of corrinoids. Apart from tetrahydromethanopterin no other soluble cofactors were required for formaldehyde… Expand

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References

SHOWING 1-10 OF 42 REFERENCES
Activation of the methylreductase system from Methanobacterium bryantii by ATP
TLDR
Observations indicate that activation involves the modification of a protein or protein-bound cofactor of the methylreductase system, and that membrane proton gradients are not important in activation. Expand
Formation of methylcoenzyme M from formaldehyde by cell‐free extracts of Methanobacterium thermoautotrophicum. Evidence for the involvement of a corrinoid‐containing methyltransferase
The conversion of formaldehyde and coenzyme M to methyl-coenzyme M (CH3S-CoM) by cell-free extracts of Methanobacterium thermoautotrophicum requires the presence of catalytic amounts of ATP. OxygenExpand
Tetrahydromethanopterin methyltransferase, a component of the methane synthesizing complex of Methanobacterium thermoautotrophicum.
  • F. Sauer
  • Chemistry, Biology
  • Biochemical and biophysical research communications
  • 1986
TLDR
The demethylation of methyl-CoM, in the absence of methane synthesis, was dependent on the addition of H4MPT which suggests that the enzyme reaction is reversible. Expand
Coupling of carbon monoxide oxidation to CO2 and H2 with the phosphorylation of ADP in acetate-grown Methanosarcina barkeri.
TLDR
The results indicate that in acetate-grown M. barkeri the free-energy change associated with the formation of CO2 and H2 from CO andH2O can be used to drive the phosphorylation of ADP and that the coupling proceeds via a chemiosmotic mechanism. Expand
Methyl-coenzyme M, an intermediate in methanogenic dissimilation of C1 compounds by Methanosarcina barkeri
TLDR
Extracts of Methanosarcina barkeri possess a specific methyltransferase that catalyzes the transfer of the methyl group of methanol to 2-mercaptoethanesulfonic acid, which results in the formation of 2-(methylthio)ethanes sulfuronic acid. Expand
Methane formation from methyl-coenzyme M in a system containing methyl-coenzyme M reductase, component B and reduced cobalamin.
TLDR
It is concluded that in this assay system B-12s might serve as electron donor for the enzymatic reduction of methyl-CoM to methane. Expand
Methanol conversion in Eubacterium limosum
The conversion of methanol by cell-free extracts of the acetogenic bacterium Eubacterium limosum was studied. Incubation of mixed cell-free extracts of both E. limosum and Methanobacterium formicicumExpand
Presence of a trimethylamine: HS-coenzyme M methyltransferase in Methanosarcina barkeri
A trimethylamine:2-mercaptoethanesulfonate (HS-coenzyme M) methyltransferase has been shown to be present in trimethylamine-grown cells but not in methanol-grown cells of Methanosarcina barkeri. TheExpand
A simplified assay for coenzyme M (HSCH2CH2SO3). Resolution of methylcobalamin-coenzyme M methyltransferase and use of sodium borohydride.
TLDR
Evidence suggests that reduction by borohydride is chemical rather than enzyme directed, and may be used to determine the usual enzyme kinetic parameters. Expand
Do corrinoids function in the methanogenic dissimilation of methanol by Methanosarcina barkeri
TLDR
Results indicate that methylcobalamin-HS-CoM methyl-transferase is not involved in the biosynthesis of CH3-S- CoM or CH4 from CH3OH by M. barkeri. Expand
...
1
2
3
4
5
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