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

  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},
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

Figures and Tables from this paper

Stimulation of the methyltetrahydromethanopterin: coenzyme M methyltransferase reaction in cell-free extracts of Methanobacterium thermoautotrophicum by the heterodisulfide of coenzyme M and 7-mercaptoheptanoylthreonine phosphate
The conversion of formaldehyde to methylcoenzyme M in cell-free extracts of Methanobacterium thermoautotrophicum was stimulated up to 10-fold by catalytic amounts of the heterodisulfide (CoM-S-S-HTP)Expand
N5-Methyltetrahydromethanopterin: coenzyme M methyltransferase in methanogenic archaebacteria is a membrane protein
A mechanism for the methyltransfer reaction and for the activation of the enzyme is proposed and proposed and is proposed for methanogenic archaebacteria. Expand
Demethylation and degradation of phenylmethylethers by the sulfide-methylating homoacetogenic bacterium strain TMBS 4
Biochemical studies on anaerobic phenylme-thylether cleavage by homoacetogenic bacteria have been hampered so far by the complexity of the reaction chain involving methyl transfer to acetyl-CoAExpand
Metabolism of methanogens
  • M. Blaut
  • Chemistry, Medicine
  • Antonie van Leeuwenhoek
  • 2004
The synthesis of cellular building blocks starts with the central anabolic intermediate acetyl-CoA which, in autotrophic methanogens, is synthesized from two molecules of CO2 in a linear pathway. Expand
Anaerobic acetate oxidation to CO2 by Desulfotomaculum acetoxidans
Desulfotomaculum acetoxidans oxidizes acetate to CO2 with sulfate. This organism metabolizes acetate via a pathway in which C1 units rather than tri- and dicarboxylic acids are intermediates. WeExpand
Reductive activation of the corrinoid-containing enzyme involved in methyl group transfer between methyl-tetrahydromethanopterin and coenzyme M inMethanosarcina barkeri
The conversion of methyl-tetrahydromethanopterin to methylcoenzyme M inMethanosarcina barkeri is catalyzed by two enzymes: an enzyme with a bound corrinoid, which becomes methylated during theExpand
Anaerobic acetate oxidation to CO2 by Desulfotomaculum acetoxidans
The presence of the enzyme activities required for the operation of the novel pathway to oxidize acetate to CO2 via an oxidative acetyl-CoA/carbon monoxide dehydrogenase pathway is reported here. Expand
Spectroscopic characterization and mechanistic investigation of P-methyl transfer by a radical SAM enzyme from the marine bacterium Shewanella denitrificans OS217.
The results suggest that SD_1168 catalyzes P-methylation using radical SAM-dependent chemistry with cobalamin as a coenzyme suggests that S. denitrificans produces a phosphinate natural product. Expand
Energy conservation under extreme energy limitation: the role of cytochromes and quinones in acetogenic bacteria
The literature on the characterization of cytochromes and quinones in acetogens are reviewed and a hypothesis that they may function in electron transport chains in addition to Rnf and Ech is presented. Expand
H2 as an energy source for mixotrophic acetogenesis from the reduction of CO2 and syringate by Acetobacterium woodii and Eubacterium limosum
Acetobacterium woodii and Eubacterium limosum were grown in a defined medium or suspended in buffer containing syringate as the sole organic carbon source to test whether H2 would supportExpand


Activation of the methylreductase system from Methanobacterium bryantii by ATP
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
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.
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
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.
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.
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
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