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 | Comment | Organism | Structure |
---|---|---|---|
betaine | feedback inhibition | Methanohalophilus portucalensis | |
S-adenosyl-L-homocysteine | product inhibition | Methanohalophilus portucalensis |
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 | 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 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 | 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 | 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 (Comment) | Organism |
---|---|
recombinant MpGSMT from Escherichia coli strain BL21(DE3) by nickel affinity chromatography | Methanohalophilus portucalensis |
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 | Comment | Organism |
---|---|---|
dimer | 2 * 29040, sequence calculation, 2 * 35000, SDS-PAGE, quaternary structure analysis of MpGSMT by analytical ultracentrifugation | Methanohalophilus portucalensis |
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 Maximum [°C] | Comment | Organism |
---|---|---|---|
37 | - |
assay at | Methanohalophilus portucalensis |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.3 | - |
assay at | Methanohalophilus portucalensis |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
S-adenosyl-L-methionine | binding motifs and substrate binding sites from gsmt, overview | Methanohalophilus portucalensis |
Organism | Comment | pI Value Maximum | pI Value |
---|---|---|---|
Methanohalophilus portucalensis | sequence calculation | 7 | 4.5 |
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 |
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 | 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 |