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Information on EC 2.1.1.157 - sarcosine/dimethylglycine N-methyltransferase and Organism(s) Halorhodospira halochloris and UniProt Accession Q9KJ21

for references in articles please use BRENDA:EC2.1.1.157
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EC Tree
IUBMB Comments
Cells of the oxygen-evolving halotolerant cyanobacterium Aphanocthece halophytica synthesize betaine from glycine by a three-step methylation process. The first enzyme, EC 2.1.1.156, glycine/sarcosine N-methyltransferase, 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 this enzyme. Both of these enzymes can catalyse the formation of N,N-dimethylglycine from sarcosine . The reactions are strongly inhibited by S-adenosyl-L-homocysteine.
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Halorhodospira halochloris
UNIPROT: Q9KJ21
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Word Map
The taxonomic range for the selected organisms is: Halorhodospira halochloris
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
sarcosine dimethylglycine n-methyltransferase, gsdmt, sarcosine dimethylglycine methyltransferase, glycine sarcosine methyltransferase, dimethylglycine methyltransferase, glycine sarcosine dimethylglycine methyltransferase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
sarcosine dimethylglycine methyltransferase
-
sarcosine dimethylglycine N-methyltransferase
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
S-adenosyl-L-methionine + sarcosine = S-adenosyl-L-homocysteine + N,N-dimethylglycine
show the reaction diagram
(1a)
S-adenosyl-L-methionine + N,N-dimethylglycine = S-adenosyl-L-homocysteine + betaine
show the reaction diagram
(1b)
2 S-adenosyl-L-methionine + sarcosine = 2 S-adenosyl-L-homocysteine + betaine
show the reaction diagram
(overall reaction)
SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:sarcosine(or N,N-dimethylglycine) N-methyltransferase [N,N-dimethylglycine(or betaine)-forming]
Cells of the oxygen-evolving halotolerant cyanobacterium Aphanocthece halophytica synthesize betaine from glycine by a three-step methylation process. The first enzyme, EC 2.1.1.156, glycine/sarcosine N-methyltransferase, 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 this enzyme. Both of these enzymes can catalyse the formation of N,N-dimethylglycine from sarcosine [3]. The reactions are strongly inhibited by S-adenosyl-L-homocysteine.
CAS REGISTRY NUMBER
COMMENTARY hide
294211-00-0
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
S-adenosyl-L-methionine + N,N-dimethylglycine
S-adenosyl-L-homocysteine + betaine
show the reaction diagram
S-adenosyl-L-methionine + sarcosine
S-adenosyl-L-homocysteine + N,N-dimethylglycine
show the reaction diagram
-
-
-
?
2 S-adenosyl-L-methionine + sarcosine
2 S-adenosyl-L-homocysteine + betaine
show the reaction diagram
(overall reaction)
-
-
?
S-adenosyl-L-methionine + N,N-dimethylglycine
S-adenosyl-L-homocysteine + betaine
show the reaction diagram
S-adenosyl-L-methionine + sarcosine
S-adenosyl-L-homocysteine + N,N-dimethylglycine
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
S-adenosyl-L-methionine + N,N-dimethylglycine
S-adenosyl-L-homocysteine + betaine
show the reaction diagram
-
-
-
?
S-adenosyl-L-methionine + sarcosine
S-adenosyl-L-homocysteine + N,N-dimethylglycine
show the reaction diagram
-
-
-
?
S-adenosyl-L-methionine + N,N-dimethylglycine
S-adenosyl-L-homocysteine + betaine
show the reaction diagram
-
-
-
-
?
S-adenosyl-L-methionine + sarcosine
S-adenosyl-L-homocysteine + N,N-dimethylglycine
show the reaction diagram
-
-
-
-
?
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
no requirement for Ca2+, Mg2+, EDTA, Mn2+, Co2+, or Zn2+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4-chloromercuribenzoate
-
recombinant enzyme: 23% inhibition at 1.33 mM, completely reversible by 5.3 mM DTT
betaine
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recombinant enzyme: poor inhibition, 71% inhibition at 2 M with sarcosine, and 69% inhibition at 2 M with dimethylglycine, partially reversible by salts KCl and NaCl, overview
KCl/NaCl
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recombinant enzyme: 32% inhibition at 0.33 M KCl and 0.66 M NaCl with sarcosine, and 25% inhibition at 0.33 M KCl and 0.66 M NaCl with dimethylglycine, decrease inhibition by betaine, overview
S-adenosyl-L-homocysteine
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recombinant enzyme: competitive product inhibition, 50% inhibition at 0.5 mM with glycine, and at 2.3 mM with sarcosine
additional information
-
no inhibition by N,N-dimethylglycine
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4.9
dimethylglycine
-
recombinant enzyme, pH 7.4, 37°C, with S-adenosyl-L-methionine
0.16 - 0.21
S-adenosyl-L-methionine
6.1
sarcosine
-
recombinant enzyme, pH 7.4, 37°C, with S-adenosyl-L-methionine
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.23
activity with sarcosine and S-adenosyl-L-methionine in crude cell extracts
2.6
activity with N,N-dimethylglycine and S-adenosyl-L-methionine in crude cell extracts
0.68
-
purified recombinant enzyme, substrate sarcosine
3.4
-
purified recombinant enzyme, substrate dimethylglycine
additional information
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.6
-
recombinant enzyme, with substrate dimethylglycine, triethanolamine buffer
8 - 9
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recombinant enzyme, with substrate sarcosine, pH-optimum depends on the buffer system
additional information
-
pH-optimum depends on the buffer system
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
SDMT_HALHR
279
0
32228
Swiss-Prot
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25000
-
gel filtration
32000
-
1 * 36000, recombinant enzyme, SDS-PAGE, 1 * 32000, about, amino acid sequence calculation
36000
-
1 * 36000, recombinant enzyme, SDS-PAGE, 1 * 32000, about, amino acid sequence calculation
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
-
1 * 36000, recombinant enzyme, SDS-PAGE, 1 * 32000, about, amino acid sequence calculation
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
formation of monoclinic crystals, diffracting to 2.15 A resolution, and orthorhombic crystals, diffracting to 1.8 A resolution
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme from Escherichia coli by ammonium sulfate fractionation, hydrophobic and anion exchange chromatography, and ultrafiltration to homogeneity
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
functional overexpression in Escherichia coli strain XL-1 Blue conferring betaine accumulation and increased salt tolerance when coexpressed with the glycine sarcosine methyltransferase, EC 2.1.1.156
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
agriculture
-
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
Manually annotated by BRENDA team
Nyyssola, A.; Kerovuo, J.; Kaukinen, P.; von Weymarn, N.; Reinikainen, T.
Extreme halophiles synthesize betaine from glycine by methylation
J. Biol. Chem.
275
22196-22201
2000
Actinopolyspora halophila, Halorhodospira halochloris, Halorhodospira halochloris (Q9KJ21)
Manually annotated by BRENDA team
Kallio, J.P.; Jaenis, J.; Nyyssoelae, A.; Hakulinen, N.; Rouvinen, J.
Preliminary X-ray analysis of twinned crystals of sarcosine dimethylglycine methyltransferase from Halorhodospira halochoris
Acta Crystallogr. Sect. F
65
805-808
2009
Halorhodospira halochloris (Q9KJ21)
Manually annotated by BRENDA team