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Literature summary for 2.1.1.157 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)

Cloned (Comment) Organism
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

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

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.5
-
S-adenosyl-L-methionine pH 7.3, 37°C, recombinant enzyme, with sarcosine Methanohalophilus portucalensis
0.79
-
S-adenosyl-L-methionine pH 7.3, 37°C, recombinant enzyme, with N,N-dimethylglycine Methanohalophilus portucalensis
2.29
-
sarcosine pH 7.3, 37°C, recombinant enzyme Methanohalophilus portucalensis
3.76
-
N,N-dimethylglycine pH 7.3, 37°C, recombinant enzyme Methanohalophilus portucalensis

Metals/Ions

Metals/Ions Comment Organism Structure
additional information no effect of Na+ and K+ on MpSDMT activity Methanohalophilus portucalensis

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
30690
-
2 * 30690, sequence calculation, 2 * 38000, SDS-PAGE Methanohalophilus portucalensis
38000
-
2 * 30690, sequence calculation, 2 * 38000, SDS-PAGE Methanohalophilus portucalensis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
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 ?
-
?
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 ?
-
?
S-adenosyl-L-methionine + N,N-dimethylglycine Methanohalophilus portucalensis
-
S-adenosyl-L-homocysteine + betaine
-
?
S-adenosyl-L-methionine + N,N-dimethylglycine Methanohalophilus portucalensis FDF1
-
S-adenosyl-L-homocysteine + betaine
-
?
S-adenosyl-L-methionine + sarcosine Methanohalophilus portucalensis
-
S-adenosyl-L-homocysteine + N,N-dimethylglycine
-
?
S-adenosyl-L-methionine + sarcosine Methanohalophilus portucalensis FDF1
-
S-adenosyl-L-homocysteine + N,N-dimethylglycine
-
?

Organism

Organism UniProt Comment Textmining
Methanohalophilus portucalensis F6KV62 SDMT; the enzyme is encoded in the gene cluster of Mpgsmt-sdmt, gene Mpgsmt
-
Methanohalophilus portucalensis FDF1 F6KV62 SDMT; the enzyme is encoded in the gene cluster of Mpgsmt-sdmt, gene Mpgsmt
-

Purification (Commentary)

Purification (Comment) Organism
recombinant MpSDMT from Escherichia coli strain BL21(DE3) by nickel affinity chromatography Methanohalophilus portucalensis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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 ?
-
?
additional information the enzyme from Methanohalophilus portucalensis possesses sarcosine N-methyltransferase (SMT) and dimethylglycine N-methyltransferase (DMT) activities Methanohalophilus portucalensis ?
-
?
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 ?
-
?
additional information the enzyme from Methanohalophilus portucalensis possesses sarcosine N-methyltransferase (SMT) and dimethylglycine N-methyltransferase (DMT) activities Methanohalophilus portucalensis FDF1 ?
-
?
S-adenosyl-L-methionine + N,N-dimethylglycine
-
Methanohalophilus portucalensis S-adenosyl-L-homocysteine + betaine
-
?
S-adenosyl-L-methionine + N,N-dimethylglycine
-
Methanohalophilus portucalensis FDF1 S-adenosyl-L-homocysteine + betaine
-
?
S-adenosyl-L-methionine + sarcosine
-
Methanohalophilus portucalensis S-adenosyl-L-homocysteine + N,N-dimethylglycine
-
?
S-adenosyl-L-methionine + sarcosine
-
Methanohalophilus portucalensis FDF1 S-adenosyl-L-homocysteine + N,N-dimethylglycine
-
?

Subunits

Subunits Comment Organism
dimer 2 * 30690, sequence calculation, 2 * 38000, SDS-PAGE Methanohalophilus portucalensis

Synonyms

Synonyms Comment Organism
glycine sarcosine dimethylglycine methyltransferase
-
Methanohalophilus portucalensis
GSDMT
-
Methanohalophilus portucalensis
sarcosine dimethylglycine methyltransferase
-
Methanohalophilus portucalensis
SDMT
-
Methanohalophilus portucalensis

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
assay at Methanohalophilus portucalensis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.3
-
assay at Methanohalophilus portucalensis

Cofactor

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

IC50 Value

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

Expression

Organism Comment Expression
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

General Information Comment Organism
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