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.

Search for more literature for 2.1.1.157

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

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
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
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.
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.
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