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Methyltransferases involved in methanol conversion by Methanosarcina barkeri

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Abstract

2-(Methylthio)ethanesulfonate (CH3S-CoM) is formed as an intermediate in methanogenesis from methanol by cell-free extracts of Methanosarcina barkeri. The enzyme system involved in the methyltransfer from methanol to 2-mercaptoethanesulfonate (HS-CoM) was resolved into two enzyme fractions. One enzyme (methanol: 5-hydroxybenzimidazolylcobamide methyltransferase) appears to be a cobalamin-containing protein, which is oxygen sensitive. The other enzyme (Co-methyl-5-hydroxybenzimidazolylcobamide: HS-CoM methyltransferase) was purified. It is insensitive to oxygen and it transfers also the methylgroup from Co-methyl-5,6-dimethylbenzimidazolylcobamide to HS-CoM.

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Abbreviations

HS-CoM:

2-mercaptoethanesulfonic acid

CH3S-CoM:

2-(methylthio)ethanesulfonic acid

BrES:

2-bromoethanesulfonic acid

TES:

N-tris-(hydroxymethyl)-methyl-2-aminoethanesulfonic acid

HBI:

5-hydroxybenzimidazole; and

DMBI:

5,6-dimethylbenzimidazole, are α-ligands of cobalamins

B12r :

cob(II)alamin

B12s :

cob(I)alamin

MT1 :

methanol

B12-HBI:

methyltransferase

MT2 :

CH3-B12-HBI:HS-CoM methyltransferase

SDS:

sodium dodecyl sulfate

References

  • Blaylock BA (1968) Cobamide-dependent methanol-cyano-cob(I) alamin methyltransferase of Methanosarcina barkeri. Arch Biochem Biophys 124:314–324

    PubMed  Google Scholar 

  • Blaylock BA, Stadtman TC (1963) Biosynthesis of methane from the methyl moiety of methylcobalamin. Biochem Biophys Res Commun 11:34–38

    PubMed  Google Scholar 

  • Blaylock BA, Stadtman TC (1964) Enzymic formation of methylcobalamin in Methanosarcina barkeri extracts. Biochem Biophys Res Commun 17:475–480

    Google Scholar 

  • Blaylock BA, Stadtman TC (1966) Methane biosynthesis by Methanosarcina barkeri. Properties of the soluble enzyme system. Arch Biochem Biophys 116:138–152

    PubMed  Google Scholar 

  • Ellefson WI, Wolfe RS (1980) Role of component C in the methylreductase system of Methanobacterium. J Biol Chem 255:8388–8389

    PubMed  Google Scholar 

  • Hermans JMH, Hutten TJ, Drift C van der, Vogels GD (1980) Analysis of coenzyme M (2-mercaptoethanesulfonic acid) derivatives by isotachophoresis. Anal Biochem 106:363–366

    PubMed  Google Scholar 

  • Hutten TJ, Bongaerts HCM, Drift C van der, Vogels GD (1980) Acetate, methanol and carbon dioxide as substrates for growth of Methanosarcina barkeri. Antonie van Leeuwenhoek J Microbiol 46:601–610

    PubMed  Google Scholar 

  • Hutten TJ, Jong MH de, Peeters BPH, Drift C van der, Vogels GD (1981) Coenzyme M derivatives and their effects on methane formation from carbon dioxide and methanol by cell extracts of Methanosarcina barkeri. J Bacteriol 145:27–34

    PubMed  Google Scholar 

  • Keltjens JT, Whitman WB, Caerteling CG, Kooten AM van, Wolfe RS, Vogels GD (1982) Presence of coenzyme M derivatives in the prosthetic group (coenzyme MF430) of methylcoenzyme M reductase from Methanobacterium thermoautotrophicum. Biochem Biophys Res Commun 108:495–503

    PubMed  Google Scholar 

  • Laemmli UK (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature (London) 227:680–685

    Google Scholar 

  • McBride BC, Wolfe RS (1971) A new coenzyme of methyltransfer, coenzym M. Biochemistry 10:2317–2324

    PubMed  Google Scholar 

  • Pol A, Drift C van der, Vogels GD (1982) Corrinoids from Methanosarcina barkeri: Structure of the α-ligand. Biochem Biophys Res Commun 198:731–737

    Google Scholar 

  • Scherer P, Sahm H (1981) Effect of trace elements and vitamins on the growth of Methanosarcina barkeri. Acta Biotechnologica 1:57–65

    Google Scholar 

  • Sedmak JJ, Grossberg SE (1977) A rapid, sensitive, and versatile assay for protein using Coomassie Brilliant Blue G250. Anal Biochem 79:544–552

    PubMed  Google Scholar 

  • Shapiro S (1982) Do corrinoids function in the methanogenic dissimilation of methanol by Methanosarcina barkeri? Can J Microbiol 28:629–635

    Google Scholar 

  • Shapiro S, Wolfe RS (1980) Methyl-coenzyme M, an intermediate in methanogenic dissimilation of C1 compounds by Methanosarcina barkeri. J Bacteriol 141:728–734

    PubMed  Google Scholar 

  • Smith MR, Mah RA (1978) Growth and methanogenesis by Methanosarcina strain 227 on acetate and methanol. Appl Environ Microbiol 36:870–879

    PubMed  Google Scholar 

  • Taylor CD, Wolfe RS (1974a) Structure and methylation of coenzyme M. J Biol Chem 249:4879–4885

    PubMed  Google Scholar 

  • Taylor CD, Wolfe RS (1974b) A simplified assay for coenzyme M Resolution of methylcobalamin-coenzyme M methyltransferase and use of sodium borohydride. J Biol Chem 249:4886–4890

    PubMed  Google Scholar 

  • Van der Meijden P, Heythuysen HT, Sliepenbeek H, Houwen FP, Drift C van der, Vogels GD (1983) Activation and inactivation of methanol: 2-Mercaptoethanesulfonic acid methyltransferase from Methanosarcina barkeri. J Bacteriol 153:6–11

    PubMed  Google Scholar 

  • Vogels GD, Keltjens JT, Hutten TJ, Drift C van der (1982) Coenzymes of methanogenic bacteria. Zentbl Bakteriol Hyg, I. Abt Orig C 3:258–264

    Google Scholar 

  • Wolfe RS, Higgins IJ (1979) Biochemistry of methane — a study in contrasts. In: Quayle JR (ed) Microbial biochemistry. Interuational review of biochemistry. University Park Press, Baltimore, p 267

    Google Scholar 

  • Wood JM, Moura I, Moura JJG, Santos MH, Xavier AV, LeGall J, Scandellari M (1982) Role of vitamin B12 in methyl transfer for methane biosynthesis by Methanosarcina barkeri. Science 216:303–305

    PubMed  Google Scholar 

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van der Meijden, P., Heythuysen, H.J., Pouwels, A. et al. Methyltransferases involved in methanol conversion by Methanosarcina barkeri . Arch. Microbiol. 134, 238–242 (1983). https://doi.org/10.1007/BF00407765

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  • DOI: https://doi.org/10.1007/BF00407765

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