Tetrahydrofolate serves as a methyl acceptor in the demethylation of dimethylsulfoniopropionate in cell extracts of sulfate-reducing bacteria

被引：0
作者：
Jansen M. [1 ]
Hansen T.A. [1 ]
机构：
[1] Department of Microbiology, Groningen Biomol. Sci. Biotech. I., University of Groningen, NL-9751 NN Haren
来源：
Archives of Microbiology | 1997年 / 169卷 / 1期
关键词：
Desulfobacterium; Dimethylsulfoniopropionate; Methylthiopropionate; Methyltransferase; Sulfate-reducing bacteria; Tetrahydrofolate;
D O I：
10.1007/s002030050545
中图分类号：
学科分类号：
摘要：
Tetrahydrofolate was shown to function as a methyl acceptor in the anaerobic demethylation of dimethylsulfoniopropionate to methylthiopropionate in cell extracts of the sulfate-reducing bacterium strain WN. Dimethylsulfoniopropionate-dependent activities were 0.56 μmol methyltetrahydrofolate min-1 (mg protein)-1 and were higher than required to explain the growth rate of strain WN on dimethylsulfoniopropionate. The reaction did not require ATP or reductive activation by titanium(III)- nitrilotriacetic acid. Preincubation of the extract under air significantly decreased the activity (35% loss in 3 h). Three other dimethylsulfoniopropionate-demethylating sulfate reducers, Desulfobacterium niacini, Desulfobacterium vacuolatum, and Desulfobacterium strain PM4, had dimethylsulfoniopropionate:tetrahydrofolate methyltransferase activities of 0.16, 0.05, and 0.24 μmol min-1 (mg protein)-1, respectively. No methyltransferase activity to tetrahydrofolate was found with betaine as a substrate, not even in extracts of betaine-grown cells of these sulfate reducers. Dimethylsulfoniopropionate demethylation in cell extracts of strain WN was completely inhibited by 0.5 mM propyl iodide; in the light, the inhibition was far less strong, indicating involvement of a corrinoid- dependent methyltransferase.
引用
收藏
页码：84 / 87
页数：3
相关论文
共 25 条
  • [1] Berman M.H., Frazer A.C., Importance of tetrahydrofolate and ATP in the anaerobic O-demethylation reaction for phenylmethylethers, Appl Environ Microbiol, 58, pp. 925-931, (1992)
  • [2] Bradford M.M., A rapid and sensitive method for the quantilation of microgram quantities of protein utilizing the principle of protein-dye binding, Anal Biochem, 72, pp. 248-254, (1976)
  • [3] Brot N., Weissbach H., Enzymatic synthesis of methionine. Chemical alkylation of the enzyme-bound cobamide, J Biol Chem, 240, pp. 3064-3070, (1965)
  • [4] Chambers S.T., Kunin C.M., Miller D., Hamada A., Dimethylthetin can substitute for glycine betaine as an osmoprotectant molecule for Escherichia coli, J Bacteriol, 169, pp. 4845-4847, (1987)
  • [5] Catalogue of Strains 1993, (1993)
  • [6] Diaz M.R., Taylor B.F., Metabolism of methylated osmolytes by aerobic bacteria from Mono Lake, a moderately hypersaline, alkaline environment, FEMS Microbiol Ecol, 19, pp. 239-247, (1996)
  • [7] Garrow T.A., Purification, kinetic properties, and cDNA cloning of mammalian betaine-homocysteine methyltransferase, J Biol Chem, 271, pp. 22831-22838, (1996)
  • [8] Heijthuijsen J.H.F.G., Hansen T.A., Betaine fermentation and oxidation by marine Desulfuromonas strains, Appl Environ Microbiol, 55, pp. 965-969, (1989)
  • [9] Hensgens C.M.H., Vonck J., Van Beeumen J., Van Bruggen E.F.J., Hansen T.A., Purification and characterization of an oxygen-labile, NAD-dependent alcohol dehydrogenase from Desulfovibrio gigas, J Bacteriol, 175, pp. 2859-2863, (1993)
  • [10] Kengen S.W.M., Mosterd J.J., Nelissen R.L.H., Keltjens J.T., Van Der Drift C., Vogels G.D., Reductive activation of the methyltetrahydromethanopterin:coenzyme M methyltransferase from Methanobacterium thermoautotrophicum strain ΔH, Arch Microbiol, 150, pp. 405-412, (1988)
123