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Information on EC 2.1.1.156 - glycine/sarcosine N-methyltransferase and Organism(s) Halorhodospira halochloris and UniProt Accession Q9KJ22
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2.1.1.156 glycine/sarcosine N-methyltransferaseIUBMB Comments
Cells of the oxygen-evolving halotolerant cyanobacterium Aphanocthece halophytica synthesize betaine from glycine by a three-step methylation process. This is the first enzyme and it leads to the formation of either sarcosine or N,N-dimethylglycine, which is further methylated to yield betaine (N,N,N-trimethylglycine) by the action of EC 2.1.1.157, sarcosine/dimethylglycine N-methyltransferase. Differs from EC 2.1.1.20, glycine N-methyltransferase, as it can further methylate the product of the first reaction. Acetate, dimethylglycine and S-adenosyl-L-homocysteine can inhibit the reaction .
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Word Map
- 2.1.1.156
-
halophilic
- betaine
-
methanohalophilus
- portucalensis
-
osmolyte
- s-adenosylhomocysteine
-
feedback-inhibited
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methanogen
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methanoarchaea
-
osmoprotectant
- methyltransferases
-
phosphorylation-mediated
- biotechnology
- agriculture
- nutrition
The taxonomic range for the selected organisms is: Halorhodospira halochloris
The expected taxonomic range for this enzyme is: Bacteria, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Archaea
Reaction Schemes
Synonyms
glycine sarcosine n-methyltransferase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
PATHWAY SOURCE
PATHWAYS
BRENDA
SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:glycine(or sarcosine) N-methyltransferase [sarcosine(or N,N-dimethylglycine)-forming]
Cells of the oxygen-evolving halotolerant cyanobacterium Aphanocthece halophytica synthesize betaine from glycine by a three-step methylation process. This is the first enzyme and it leads to the formation of either sarcosine or N,N-dimethylglycine, which is further methylated to yield betaine (N,N,N-trimethylglycine) by the action of EC 2.1.1.157, sarcosine/dimethylglycine N-methyltransferase. Differs from EC 2.1.1.20, glycine N-methyltransferase, as it can further methylate the product of the first reaction. Acetate, dimethylglycine and S-adenosyl-L-homocysteine can inhibit the reaction [3].
CAS REGISTRY NUMBER
COMMENTARY
294210-82-5
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
S-adenosyl-L-methionine + sarcosine
S-adenosyl-L-homocysteine + N,N-dimethylglycine
-
-
-
?
2 S-adenosyl-L-methionine + glycine
2 S-adenosyl-L-homocysteine + N,N-dimethylglycine
overall reaction
-
-
?
S-adenosyl-L-methionine + glycine
S-adenosyl-L-homocysteine + sarcosine
-
-
-
?
S-adenosyl-L-methionine + glycine
S-adenosyl-L-homocysteine + sarcosine
-
i.e. 2-methylglycine
-
?
S-adenosyl-L-methionine + glycine
S-adenosyl-L-homocysteine + sarcosine
-
-
-
?
S-adenosyl-L-methionine + glycine
S-adenosyl-L-homocysteine + sarcosine
-
-
i.e. 2-methylglycine
-
?
S-adenosyl-L-methionine + glycine
S-adenosyl-L-homocysteine + sarcosine
-
the recombinant enzyme from Escherichia coli is 3.3fold less active than the wild-type enzyme
i.e. 2-methylglycine
-
?
S-adenosyl-L-methionine + sarcosine
S-adenosyl-L-homocysteine + N,N-dimethylglycine
-
-
-
-
?
S-adenosyl-L-methionine + sarcosine
S-adenosyl-L-homocysteine + N,N-dimethylglycine
-
-
-
?
S-adenosyl-L-methionine + sarcosine
S-adenosyl-L-homocysteine + N,N-dimethylglycine
-
the recombinant enzyme from Escherichia coli is 2.5fold less active than the wild-type enzyme
-
-
?
additional information
?
-
-
the enzyme catalyzes the first 2 steps of betaine synthesis from glycine in a 3-step process
-
-
?
additional information
?
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the enzyme catalyzes the first 2 steps of betaine synthesis from glycine in a 3-step process
-
-
?
additional information
?
-
-
the enzyme has overlapping activities with the enzyme catalyzing the following reaction steps
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-
?
additional information
?
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the enzyme has overlapping activities with the enzyme catalyzing the following reaction steps
-
-
?
additional information
?
-
-
the enzyme catalyzes the first 2 steps of glycine betaine synthesis from glycine in a 3-step process, betaine is required for balancing osmotic pressure under high salt living conditions
-
-
?
additional information
?
-
-
the enzyme shows strict specificity for glycine and sarcosine as substrates, no activity with ethanolamine, monomethylethanolamine, nor several L-amino acid, overview
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-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
S-adenosyl-L-methionine + glycine
S-adenosyl-L-homocysteine + sarcosine
-
-
-
?
S-adenosyl-L-methionine + sarcosine
S-adenosyl-L-homocysteine + N,N-dimethylglycine
-
-
-
?
S-adenosyl-L-methionine + glycine
S-adenosyl-L-homocysteine + sarcosine
-
-
i.e. 2-methylglycine
-
?
S-adenosyl-L-methionine + sarcosine
S-adenosyl-L-homocysteine + N,N-dimethylglycine
-
-
-
-
?
additional information
?
-
-
the enzyme catalyzes the first 2 steps of betaine synthesis from glycine in a 3-step process
-
-
?
additional information
?
-
the enzyme catalyzes the first 2 steps of betaine synthesis from glycine in a 3-step process
-
-
?
additional information
?
-
-
the enzyme catalyzes the first 2 steps of glycine betaine synthesis from glycine in a 3-step process, betaine is required for balancing osmotic pressure under high salt living conditions
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
no requirement for Ca2+, Mg2+, EDTA, Mn2+, Co2+, or Zn2+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
4-chloromercuribenzoate
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recombinant enzyme: over 95% inhibition at 1.33 mM, completely reversible by 5.3 mM DTT
betaine
-
recombinant enzyme: poor inhibition, 60% inhibition at 2 M with glycine, and 70% inhibition at 2 M with sarcosine, synergistic with salts KCl and NaCl, overview
KCl/NaCl
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recombinant enzyme: synergistic with betaine, 80% inhibition at 0.33 M KCl and 0.66M NaCl with glycine, and 66% inhibition at 0.33 M KCl and 0.66 M NaCl with sarcosine, overview
N,N-dimethylglycine
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recombinant enzyme: poor competitive product inhibition, 50% inhibition at 38 mM with glycine, and at 49 mM with sarcosine
S-adenosyl-L-homocysteine
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recombinant enzyme: competitive product inhibition, 50% inhibition at 0.5 mM with glycine, and at 0.4 mM with sarcosine
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
betaine
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recombinant enzyme: 20% activation at 0.5 M with sarcosine, no activation with glycine
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
18
glycine
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recombinant enzyme, pH 7.4, 37°C, with S-adenosyl-L-methionine
2.3
sarcosine
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recombinant enzyme, pH 7.4, 37°C, with S-adenosyl-L-methionine
0.28
S-adenosyl-L-methionine
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recombinant enzyme, pH 7.4, 37°C, with sarcosine
0.42
S-adenosyl-L-methionine
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recombinant enzyme, pH 7.4, 37°C, with glycine
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.058
activity with glycine and S-adenosyl-L-methionine in crude cell extracts
0.19
activity with sarcosine and S-adenosyl-L-methionine, purified enzyme
0.23
activity with sarcosine and S-adenosyl-L-methionine in crude cell extracts
0.52
activity with glycine and S-adenosyl-L-methionine, purified enzyme
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
31000
-
1 * 42000, recombinant enzyme, SDS-PAGE, 1 * 31000, about, amino acid sequence calculation
42000
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1 * 42000, recombinant enzyme, SDS-PAGE, 1 * 31000, about, amino acid sequence calculation
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
-
1 * 42000, recombinant enzyme, SDS-PAGE, 1 * 31000, about, amino acid sequence calculation
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
by hydrophobic interaction chromatography, ammonium sulfate fractionation, gel filtration, ion exchange chromatography and ultrafiltration
recombinant enzyme from Escherichia coli by ammonium sulfate fractionation, hydrophobic and anion exchange chromatography, and ultrafiltration to homogeneity
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination, functional coexpression in Escherichia coli with sarcosine dimethylglycine methyltransferase, EC 2.1.1.157, conferring betaine accumulation and increased salt tolerance to the Escherichia coli cells
functional overexpression in Escherichia coli strain XL-1 Blue conferring betaine accumulation and increased salt tolerance when coexpressed with the sarcosine dimethylglycine methyltransferase, EC 2.1.1.157
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
agriculture
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enzyme can be used in betaine production for improvement of stress tolerance of commercially important microbes in agriculture and industry, and for nutritial improvement of transgenic crop plants, that do not produce betaine naturally
biotechnology
-
enzyme can be used in betaine production for improvement of stress tolerance of commercially important microbes in agriculture and industry, and for nutritial improvement of transgenic crop plants, that do not produce betaine naturally
nutrition
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enzyme can be used in betaine production for improvement of stress tolerance of commercially important microbes in agriculture and industry, and for nutritial improvement of transgenic crop plants, that do not produce betaine naturally
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Nyyssola, A.; Reinikainen, T.; Leisola, M.
Characterization of glycine sarcosine N-methyltransferase and sarcosine dimethylglycine N-methyltransferase
Appl. Environ. Microbiol.
67
2044-2050
2001
Halorhodospira halochloris
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