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Information on EC 2.1.1.156 - glycine/sarcosine N-methyltransferase and Organism(s) Actinopolyspora halophila and UniProt Accession Q9KJ20

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EC Tree
     2 Transferases
         2.1 Transferring one-carbon groups
             2.1.1 Methyltransferases
                2.1.1.156 glycine/sarcosine N-methyltransferase
IUBMB 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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Actinopolyspora halophila
UNIPROT: Q9KJ20
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The taxonomic range for the selected organisms is: Actinopolyspora halophila
The expected taxonomic range for this enzyme is: Bacteria, Archaea
Synonyms
glycine sarcosine n-methyltransferase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycine sarcosine methyltransferase
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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 hide
294210-82-5
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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 + glycine
S-adenosyl-L-homocysteine + sarcosine
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 + glycine
S-adenosyl-L-homocysteine + sarcosine
show the reaction diagram
-
-
-
?
S-adenosyl-L-methionine + sarcosine
S-adenosyl-L-homocysteine + N,N-dimethylglycine
show the reaction diagram
-
-
-
?
additional information
?
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the enzyme catalyzes the first 2 steps of betaine synthesis from glycine in a 3-step process
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-
?
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.023
activity with glycine and S-adenosyl-L-methionine in crude cell extracts
0.34
activity with sarcosine and S-adenosyl-L-methionine in crude cell extracts
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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?
GSDMT_ACTHA
565
0
64719
Swiss-Prot
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
enzyme is instable during purification, activity is lost within 30 min
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination, the single gene encodes the glycine sarcosine methyltransferase as well as the sarcosine dimethylglycine methyltransferase, EC 2.1.1.157, the latter being probably a proteolytic processing product of the first, poor expression in Escherichia coli of the full length and the truncated enzyme
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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 (Q9KJ20), Halorhodospira halochloris, Halorhodospira halochloris (Q9KJ22)
Manually annotated by BRENDA team