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Literature summary extracted from

  • Lai, S.J.; Lai, M.C.
    Characterization and regulation of the osmolyte betaine synthesizing enzymes GSMT and SDMT from halophilic methanogen Methanohalophilus portucalensis (2011), PLoS ONE, 6, e25090.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.1.1.156 gene Mpgsmt, DNA and amino acid sequence determination and analysis and sequence comparisons, phylogenetic analysis of GSMT, expression of complete gene cluster of Mpgsmt-sdmt in Escherichia coli strain BL21(DE3) and in strain MKH13 deficient in betaine transport, the recombinant enzyme is functional to synthesize and accumulate betaine and confers elevated survival ability in betaine transport deficient mutant strain MKH13 under high salt stress. The recombinantly expressed enzyme shows 10000fold lower catalytic efficiency compared with the enzyme isolated from the original cells Methanohalophilus portucalensis
2.1.1.157 gene Mpsdmt, DNA and amino acid sequence determination and analysis and sequence comparisons, phylogenetic analysis of SDMT, expression of complete gene cluster of Mpgsmt-sdmt in Escherichia coli strain BL21(DE3) and in strain MKH13 deficient in betaine transport, the recombinant enzyme is functional to synthesize and accumulate betaine and confers elevated survival ability in betaine transport deficient mutant strain MKH13 under high salt stress Methanohalophilus portucalensis

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.1.1.156 betaine feedback inhibition Methanohalophilus portucalensis
2.1.1.156 S-adenosyl-L-homocysteine product inhibition Methanohalophilus portucalensis
2.1.1.157 betaine does not affect the SMT activity, but represses the DMT activity by 35% at 2 M Methanohalophilus portucalensis
2.1.1.157 additional information both the SMT and DMT activities of SDMT from halophilic methanoarchaea are not inhibited by KCl or NaCl Methanohalophilus portucalensis
2.1.1.157 S-adenosyl-L-homocysteine product inhibition Methanohalophilus portucalensis

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.1.1.156 1.78
-
 S-adenosyl-L-methionine pH 7.3, 37°C, recombinant enzyme, with sarcosine Methanohalophilus portucalensis
2.1.1.156 8.26
-
 S-adenosyl-L-methionine pH 7.3, 37°C, recombinant enzyme, with glycine Methanohalophilus portucalensis
2.1.1.156 2320
-
 glycine pH 7.3, 37°C, recombinant enzyme Methanohalophilus portucalensis
2.1.1.156 3020
-
 sarcosine pH 7.3, 37°C, recombinant enzyme Methanohalophilus portucalensis
2.1.1.157 0.5
-
 S-adenosyl-L-methionine pH 7.3, 37°C, recombinant enzyme, with sarcosine Methanohalophilus portucalensis
2.1.1.157 0.79
-
 S-adenosyl-L-methionine pH 7.3, 37°C, recombinant enzyme, with N,N-dimethylglycine Methanohalophilus portucalensis
2.1.1.157 2.29
-
 sarcosine pH 7.3, 37°C, recombinant enzyme Methanohalophilus portucalensis
2.1.1.157 3.76
-
 N,N-dimethylglycine pH 7.3, 37°C, recombinant enzyme Methanohalophilus portucalensis

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.1.1.156 K+ dramatic activating effects of sodium and potassium ions on the in vitro methyltransferase activities of MpGSMT Methanohalophilus portucalensis
2.1.1.156 additional information level of potassium and sodium ions may modulate the substrate binding activity of MpGSMT through the conformational change Methanohalophilus portucalensis
2.1.1.156 Na+ dramatic activating effects of sodium and potassium ions on the in vitro methyltransferase activities of MpGSMT Methanohalophilus portucalensis
2.1.1.157 additional information no effect of Na+ and K+ on MpSDMT activity Methanohalophilus portucalensis

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.1.1.156 29040
-
 2 * 29040, sequence calculation, 2 * 35000, SDS-PAGE, quaternary structure analysis of MpGSMT by analytical ultracentrifugation Methanohalophilus portucalensis
2.1.1.156 35000
-
 2 * 29040, sequence calculation, 2 * 35000, SDS-PAGE, quaternary structure analysis of MpGSMT by analytical ultracentrifugation Methanohalophilus portucalensis
2.1.1.157 30690
-
 2 * 30690, sequence calculation, 2 * 38000, SDS-PAGE Methanohalophilus portucalensis
2.1.1.157 38000
-
 2 * 30690, sequence calculation, 2 * 38000, SDS-PAGE Methanohalophilus portucalensis

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.1.1.156 additional information Methanohalophilus portucalensis the broad substrate methyltransferase, glycine sarcosine dimethylglycine methyltransferase, GSDMT, purified from the halophilic methanoarchaeon Methanohalophilus portucalensis strain FDF1, has been shown to possess glycine N-methyltransferase (GMT), sarcosine N-methyltransferase (SMT) and dimethylglycine N-methyltransferase (DMT) activities. GSMT possesses glycine N-methyltransferase (GMT) and sarcosine N-methyltransferase (SMT) activities ?
-
 ?
2.1.1.156 additional information Methanohalophilus portucalensis FDF1 the broad substrate methyltransferase, glycine sarcosine dimethylglycine methyltransferase, GSDMT, purified from the halophilic methanoarchaeon Methanohalophilus portucalensis strain FDF1, has been shown to possess glycine N-methyltransferase (GMT), sarcosine N-methyltransferase (SMT) and dimethylglycine N-methyltransferase (DMT) activities. GSMT possesses glycine N-methyltransferase (GMT) and sarcosine N-methyltransferase (SMT) activities ?
-
 ?
2.1.1.156 S-adenosyl-L-methionine + glycine Methanohalophilus portucalensis
-
 S-adenosyl-L-homocysteine + sarcosine
-
 ?
2.1.1.156 S-adenosyl-L-methionine + glycine Methanohalophilus portucalensis FDF1
-
 S-adenosyl-L-homocysteine + sarcosine
-
 ?
2.1.1.156 S-adenosyl-L-methionine + sarcosine Methanohalophilus portucalensis
-
 S-adenosyl-L-homocysteine + N,N-dimethylglycine
-
 ?
2.1.1.156 S-adenosyl-L-methionine + sarcosine Methanohalophilus portucalensis FDF1
-
 S-adenosyl-L-homocysteine + N,N-dimethylglycine
-
 ?
2.1.1.157 additional information Methanohalophilus portucalensis the broad substrate methyltransferase, glycine sarcosine dimethylglycine methyltransferase, GSDMT, purified from the halophilic methanoarchaeon Methanohalophilus portucalensis strain FDF1, has been shown to possess glycine N-methyltransferase (GMT), sarcosine N-methyltransferase (SMT) and dimethylglycine N-methyltransferase (DMT) activities. SDMT possesses sarcosine N-methyltransferase (SMT) and dimethylglycine N-methyltransferase (DMT) activities ?
-
 ?
2.1.1.157 additional information Methanohalophilus portucalensis FDF1 the broad substrate methyltransferase, glycine sarcosine dimethylglycine methyltransferase, GSDMT, purified from the halophilic methanoarchaeon Methanohalophilus portucalensis strain FDF1, has been shown to possess glycine N-methyltransferase (GMT), sarcosine N-methyltransferase (SMT) and dimethylglycine N-methyltransferase (DMT) activities. SDMT possesses sarcosine N-methyltransferase (SMT) and dimethylglycine N-methyltransferase (DMT) activities ?
-
 ?
2.1.1.157 S-adenosyl-L-methionine + N,N-dimethylglycine Methanohalophilus portucalensis
-
 S-adenosyl-L-homocysteine + betaine
-
 ?
2.1.1.157 S-adenosyl-L-methionine + N,N-dimethylglycine Methanohalophilus portucalensis FDF1
-
 S-adenosyl-L-homocysteine + betaine
-
 ?
2.1.1.157 S-adenosyl-L-methionine + sarcosine Methanohalophilus portucalensis
-
 S-adenosyl-L-homocysteine + N,N-dimethylglycine
-
 ?
2.1.1.157 S-adenosyl-L-methionine + sarcosine Methanohalophilus portucalensis FDF1
-
 S-adenosyl-L-homocysteine + N,N-dimethylglycine
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.1.1.156 Methanohalophilus portucalensis F6KV61 GSMT; the enzyme is encoded in the gene cluster of Mpgsmt-sdmt, gene Mpgsmt
-
2.1.1.156 Methanohalophilus portucalensis FDF1 F6KV61 GSMT; the enzyme is encoded in the gene cluster of Mpgsmt-sdmt, gene Mpgsmt
-
2.1.1.157 Methanohalophilus portucalensis F6KV62 SDMT; the enzyme is encoded in the gene cluster of Mpgsmt-sdmt, gene Mpgsmt
-
2.1.1.157 Methanohalophilus portucalensis FDF1 F6KV62 SDMT; the enzyme is encoded in the gene cluster of Mpgsmt-sdmt, gene Mpgsmt
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.1.1.156 recombinant MpGSMT from Escherichia coli strain BL21(DE3) by nickel affinity chromatography Methanohalophilus portucalensis
2.1.1.157 recombinant MpSDMT from Escherichia coli strain BL21(DE3) by nickel affinity chromatography Methanohalophilus portucalensis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.1.1.156 additional information the broad substrate methyltransferase, glycine sarcosine dimethylglycine methyltransferase, GSDMT, purified from the halophilic methanoarchaeon Methanohalophilus portucalensis strain FDF1, has been shown to possess glycine N-methyltransferase (GMT), sarcosine N-methyltransferase (SMT) and dimethylglycine N-methyltransferase (DMT) activities. GSMT possesses glycine N-methyltransferase (GMT) and sarcosine N-methyltransferase (SMT) activities Methanohalophilus portucalensis ?
-
 ?
2.1.1.156 additional information the enzyme from Methanohalophilus portucalensis possesses glycine N-methyltransferase (GMT) and sarcosine N-methyltransferase (SMT) activities Methanohalophilus portucalensis ?
-
 ?
2.1.1.156 additional information the broad substrate methyltransferase, glycine sarcosine dimethylglycine methyltransferase, GSDMT, purified from the halophilic methanoarchaeon Methanohalophilus portucalensis strain FDF1, has been shown to possess glycine N-methyltransferase (GMT), sarcosine N-methyltransferase (SMT) and dimethylglycine N-methyltransferase (DMT) activities. GSMT possesses glycine N-methyltransferase (GMT) and sarcosine N-methyltransferase (SMT) activities Methanohalophilus portucalensis FDF1 ?
-
 ?
2.1.1.156 additional information the enzyme from Methanohalophilus portucalensis possesses glycine N-methyltransferase (GMT) and sarcosine N-methyltransferase (SMT) activities Methanohalophilus portucalensis FDF1 ?
-
 ?
2.1.1.156 S-adenosyl-L-methionine + glycine
-
 Methanohalophilus portucalensis S-adenosyl-L-homocysteine + sarcosine
-
 ?
2.1.1.156 S-adenosyl-L-methionine + glycine
-
 Methanohalophilus portucalensis FDF1 S-adenosyl-L-homocysteine + sarcosine
-
 ?
2.1.1.156 S-adenosyl-L-methionine + sarcosine
-
 Methanohalophilus portucalensis S-adenosyl-L-homocysteine + N,N-dimethylglycine
-
 ?
2.1.1.156 S-adenosyl-L-methionine + sarcosine
-
 Methanohalophilus portucalensis FDF1 S-adenosyl-L-homocysteine + N,N-dimethylglycine
-
 ?
2.1.1.157 additional information the broad substrate methyltransferase, glycine sarcosine dimethylglycine methyltransferase, GSDMT, purified from the halophilic methanoarchaeon Methanohalophilus portucalensis strain FDF1, has been shown to possess glycine N-methyltransferase (GMT), sarcosine N-methyltransferase (SMT) and dimethylglycine N-methyltransferase (DMT) activities. SDMT possesses sarcosine N-methyltransferase (SMT) and dimethylglycine N-methyltransferase (DMT) activities Methanohalophilus portucalensis ?
-
 ?
2.1.1.157 additional information the enzyme from Methanohalophilus portucalensis possesses sarcosine N-methyltransferase (SMT) and dimethylglycine N-methyltransferase (DMT) activities Methanohalophilus portucalensis ?
-
 ?
2.1.1.157 additional information the broad substrate methyltransferase, glycine sarcosine dimethylglycine methyltransferase, GSDMT, purified from the halophilic methanoarchaeon Methanohalophilus portucalensis strain FDF1, has been shown to possess glycine N-methyltransferase (GMT), sarcosine N-methyltransferase (SMT) and dimethylglycine N-methyltransferase (DMT) activities. SDMT possesses sarcosine N-methyltransferase (SMT) and dimethylglycine N-methyltransferase (DMT) activities Methanohalophilus portucalensis FDF1 ?
-
 ?
2.1.1.157 additional information the enzyme from Methanohalophilus portucalensis possesses sarcosine N-methyltransferase (SMT) and dimethylglycine N-methyltransferase (DMT) activities Methanohalophilus portucalensis FDF1 ?
-
 ?
2.1.1.157 S-adenosyl-L-methionine + N,N-dimethylglycine
-
 Methanohalophilus portucalensis S-adenosyl-L-homocysteine + betaine
-
 ?
2.1.1.157 S-adenosyl-L-methionine + N,N-dimethylglycine
-
 Methanohalophilus portucalensis FDF1 S-adenosyl-L-homocysteine + betaine
-
 ?
2.1.1.157 S-adenosyl-L-methionine + sarcosine
-
 Methanohalophilus portucalensis S-adenosyl-L-homocysteine + N,N-dimethylglycine
-
 ?
2.1.1.157 S-adenosyl-L-methionine + sarcosine
-
 Methanohalophilus portucalensis FDF1 S-adenosyl-L-homocysteine + N,N-dimethylglycine
-
 ?

Subunits

EC Number Subunits Comment Organism
2.1.1.156 dimer 2 * 29040, sequence calculation, 2 * 35000, SDS-PAGE, quaternary structure analysis of MpGSMT by analytical ultracentrifugation Methanohalophilus portucalensis
2.1.1.157 dimer 2 * 30690, sequence calculation, 2 * 38000, SDS-PAGE Methanohalophilus portucalensis

Synonyms

EC Number Synonyms Comment Organism
2.1.1.156 glycine sarcosine dimethylglycine methyltransferase
-
 Methanohalophilus portucalensis
2.1.1.156 glycine sarcosine methyltransferase
-
 Methanohalophilus portucalensis
2.1.1.156 GSDMT
-
 Methanohalophilus portucalensis
2.1.1.156 GSMT
-
 Methanohalophilus portucalensis
2.1.1.157 glycine sarcosine dimethylglycine methyltransferase
-
 Methanohalophilus portucalensis
2.1.1.157 GSDMT
-
 Methanohalophilus portucalensis
2.1.1.157 sarcosine dimethylglycine methyltransferase
-
 Methanohalophilus portucalensis
2.1.1.157 SDMT
-
 Methanohalophilus portucalensis

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.1.1.156 37
-
 assay at Methanohalophilus portucalensis
2.1.1.157 37
-
 assay at Methanohalophilus portucalensis

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.1.1.156 7.3
-
 assay at Methanohalophilus portucalensis
2.1.1.157 7.3
-
 assay at Methanohalophilus portucalensis

Cofactor

EC Number Cofactor Comment Organism Structure
2.1.1.156 S-adenosyl-L-methionine binding motifs and substrate binding sites from gsmt, overview Methanohalophilus portucalensis
2.1.1.157 S-adenosyl-L-methionine binding motifs and substrate binding sites from sdmt, overview Methanohalophilus portucalensis

pI Value

EC Number Organism Comment pI Value Maximum pI Value
2.1.1.156 Methanohalophilus portucalensis sequence calculation 7 4.5

IC50 Value

EC Number IC50 Value IC50 Value Maximum Comment Organism Inhibitor Structure
2.1.1.156 0.05
-
 pH 7.3, 37°C, recombinant enzyme, with glycine Methanohalophilus portucalensis S-adenosyl-L-homocysteine
2.1.1.156 0.07
-
 pH 7.3, 37°C, recombinant enzyme, with sarcosine Methanohalophilus portucalensis S-adenosyl-L-homocysteine
2.1.1.157 0.15
-
 pH 7.3, 37°C, recombinant enzyme, with sarcosine Methanohalophilus portucalensis S-adenosyl-L-homocysteine
2.1.1.157 0.4
-
 pH 7.3, 37°C, recombinant enzyme, with N,N-dimethylglycine Methanohalophilus portucalensis S-adenosyl-L-homocysteine

Expression

EC Number Organism Comment Expression
2.1.1.156 Methanohalophilus portucalensis betaine downregulates GSMT expression enhanced with increasing temperature, transcription unit and transcription level of Mpgsmt-sdmt is reduced under temperature stresses up to 37°C, but recovers at 45°C to the level at 20°C down
2.1.1.157 Methanohalophilus portucalensis betaine downregulates GSMT expression enhanced with increasing temperature, transcription unit and transcription level of Mpgsmt-sdmt is reduced under temperature stresses up to 37°C, but recovers at 45°C to the level at 20°C down

General Information

EC Number General Information Comment Organism
2.1.1.156 additional information conserved glycine- and sarcosine-binding residue Arg167, binding site structures, overview. The level of potassium and sodium ions may modulate the substrate binding activity of MpGSMT through the conformational change Methanohalophilus portucalensis
2.1.1.156 physiological function GSMT from a halophilic methanoarchaeon regulates betaine biosynthesis pathway by a distinct mechanism. GSMT catalyzes the first enzymatic step in synthesis of the osmolyte betaine in halophilic archaea, GSMT may also play a major role in coupling the salt-in and compatible solute (osmolyte) osmoadaptative strategies in halophilic methanogens for adapting to high salt environments Methanohalophilus portucalensis
2.1.1.157 additional information conserved glycine- and sarcosine-binding residue Arg167, binding site structures, overview. The level of potassium and sodium ions may modulate the substrate binding activity of MpGSMT through the conformational change Methanohalophilus portucalensis