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Literature summary for 2.1.1.156 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 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

Inhibitors

Inhibitors Comment Organism Structure
betaine feedback inhibition Methanohalophilus portucalensis
S-adenosyl-L-homocysteine product inhibition Methanohalophilus portucalensis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.78
-
S-adenosyl-L-methionine pH 7.3, 37°C, recombinant enzyme, with sarcosine Methanohalophilus portucalensis
8.26
-
S-adenosyl-L-methionine pH 7.3, 37°C, recombinant enzyme, with glycine Methanohalophilus portucalensis
2320
-
glycine pH 7.3, 37°C, recombinant enzyme Methanohalophilus portucalensis
3020
-
sarcosine pH 7.3, 37°C, recombinant enzyme Methanohalophilus portucalensis

Metals/Ions

Metals/Ions Comment Organism Structure
K+ dramatic activating effects of sodium and potassium ions on the in vitro methyltransferase activities of MpGSMT Methanohalophilus portucalensis
additional information level of potassium and sodium ions may modulate the substrate binding activity of MpGSMT through the conformational change Methanohalophilus portucalensis
Na+ dramatic activating effects of sodium and potassium ions on the in vitro methyltransferase activities of MpGSMT Methanohalophilus portucalensis

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
29040
-
2 * 29040, sequence calculation, 2 * 35000, SDS-PAGE, quaternary structure analysis of MpGSMT by analytical ultracentrifugation Methanohalophilus portucalensis
35000
-
2 * 29040, sequence calculation, 2 * 35000, SDS-PAGE, quaternary structure analysis of MpGSMT by analytical ultracentrifugation 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. GSMT possesses glycine N-methyltransferase (GMT) and sarcosine N-methyltransferase (SMT) 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. GSMT possesses glycine N-methyltransferase (GMT) and sarcosine N-methyltransferase (SMT) activities ?
-
?
S-adenosyl-L-methionine + glycine Methanohalophilus portucalensis
-
S-adenosyl-L-homocysteine + sarcosine
-
?
S-adenosyl-L-methionine + glycine Methanohalophilus portucalensis FDF1
-
S-adenosyl-L-homocysteine + sarcosine
-
?
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 F6KV61 GSMT; the enzyme is encoded in the gene cluster of Mpgsmt-sdmt, gene Mpgsmt
-
Methanohalophilus portucalensis FDF1 F6KV61 GSMT; the enzyme is encoded in the gene cluster of Mpgsmt-sdmt, gene Mpgsmt
-

Purification (Commentary)

Purification (Comment) Organism
recombinant MpGSMT 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. GSMT possesses glycine N-methyltransferase (GMT) and sarcosine N-methyltransferase (SMT) activities Methanohalophilus portucalensis ?
-
?
additional information the enzyme from Methanohalophilus portucalensis possesses glycine N-methyltransferase (GMT) and sarcosine N-methyltransferase (SMT) 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. GSMT possesses glycine N-methyltransferase (GMT) and sarcosine N-methyltransferase (SMT) activities Methanohalophilus portucalensis FDF1 ?
-
?
additional information the enzyme from Methanohalophilus portucalensis possesses glycine N-methyltransferase (GMT) and sarcosine N-methyltransferase (SMT) activities Methanohalophilus portucalensis FDF1 ?
-
?
S-adenosyl-L-methionine + glycine
-
Methanohalophilus portucalensis S-adenosyl-L-homocysteine + sarcosine
-
?
S-adenosyl-L-methionine + glycine
-
Methanohalophilus portucalensis FDF1 S-adenosyl-L-homocysteine + sarcosine
-
?
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 * 29040, sequence calculation, 2 * 35000, SDS-PAGE, quaternary structure analysis of MpGSMT by analytical ultracentrifugation Methanohalophilus portucalensis

Synonyms

Synonyms Comment Organism
glycine sarcosine dimethylglycine methyltransferase
-
Methanohalophilus portucalensis
glycine sarcosine methyltransferase
-
Methanohalophilus portucalensis
GSDMT
-
Methanohalophilus portucalensis
GSMT
-
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 gsmt, overview Methanohalophilus portucalensis

pI Value

Organism Comment pI Value Maximum pI Value
Methanohalophilus portucalensis sequence calculation 7 4.5

IC50 Value

IC50 Value IC50 Value Maximum Comment Organism Inhibitor Structure
0.05
-
pH 7.3, 37°C, recombinant enzyme, with glycine Methanohalophilus portucalensis S-adenosyl-L-homocysteine
0.07
-
pH 7.3, 37°C, recombinant enzyme, with sarcosine 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
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