Methanol: Coenzyme M Methyltransferase from Methanosarcina Barkeri
Open Access
- 1 October 1997
- journal article
- Published by Wiley in European Journal of Biochemistry
- Vol. 249 (1) , 280-285
- https://doi.org/10.1111/j.1432-1033.1997.t01-1-00280.x
Abstract
In Methanosarcina barkeri, methanogenesis from methanol is initiated by the formation of methyl‐coenzyme M from methanol and coenzyme M. This methyl transfer reaction is catalyzed by two enzymes, designated methyltransferases 1 (MT1) and 2 (MT2). Transferase MT1, which is composed of a 50‐kDa subunit, MtaB, and a 27‐kDa corrinoid‐harbouring subunit, MtaC, has been shown recently to catalyze the methylation of free cob(I)alamin with methanol [Sauer, K., Harms, U. & Thauer, R. K. (1997) Eur. J. Biochem. 243, 670–677]. We report here that this reaction is catalyzed by subunit MtaB overproduced in Escherichia coli. MtaB also catalyzed the formation of methanol from methylcobalamin and H2O, the hydrolysis being associated with a free‐energy change ΔG0′ of approximately +7.0 kJ/mol. MtaB was found to contain 1 mol zinc, and its activity to be zinc dependent (pKZn2+= 9.3). The zinc dependence of the MT2 (MtaA)‐catalyzed reaction is also described (pKZn2+= 9.6).Keywords
This publication has 25 references indexed in Scilit:
- Cobalamin-Dependent Methionine Synthase Is a Modular Protein with Distinct Regions for Binding Homocysteine, Methyltetrahydrofolate, Cobalamin, and AdenosylmethionineBiochemistry, 1997
- Methanol: Coenzyme M Methyltransferase from Methanosarcina BarkeriEuropean Journal of Biochemistry, 1997
- The Corrinoid‐Containing 23‐kDa Subunit MtrA of the Energy‐Conserving N5‐Methyltetrahydromethanopterin:coenzyme M Methyltransferase Complex from Methanobacterium ThermoautotrophicumEuropean Journal of Biochemistry, 1996
- Activation Mechanism of Methanol:5-Hydroxybenzimidazolylcobamide Methyltransferase fromPublished by Elsevier ,1996
- Methylcobalamin:Coenzyme M Methyltransferase Isoenzymes MtaA and MtbA from Methanosarcina barkeriEuropean Journal of Biochemistry, 1996
- Thermostable Aminoacylase fromBacillus stearothermophilus:Significance of the Metal Center for Catalysis and Protein StabilityBiological Chemistry Hoppe-Seyler, 1995
- Providing one-carbon units for biological methylations: mechanistic studies on serine hydroxymethyltransferase, methylenetetrahydrofolate reductase, and methyltetrahydrofolate-homocysteine methyltransferaseChemical Reviews, 1990
- Involvement of corrinoids in the methylation of coenzyme M (2-mercaptoethanesulfonic acid) by methanol and enzymes fromFEMS Microbiology Letters, 1983
- Involvement of corrinoids in the methylation of coenzyme M (2-mercaptoethanesulfonic acid) by methanol and enzymes fromMethanosarcina barkeriFEMS Microbiology Letters, 1983
- A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye bindingAnalytical Biochemistry, 1976