2.1.1.20: glycine N-methyltransferase
This is an abbreviated version!
For detailed information about glycine N-methyltransferase, go to the full flat file.
Word Map on EC 2.1.1.20
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2.1.1.20
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s-adenosylmethionine
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s-adenosylhomocysteine
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homocysteine
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folate
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sarcosine
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adenosyltransferase
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cystathionine
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transmethylation
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adomet
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betaine-homocysteine
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remethylation
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beta-synthase
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one-carbon
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transsulfuration
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5-methyltetrahydrofolate
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medicine
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folate-dependent
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n-methylglycine
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s-methyltransferase
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glycine-n-methyltransferase
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guanidinoacetate
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folate-deficient
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pentaglutamate
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pah-binding
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adohcy
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diagnostics
- 2.1.1.20
- s-adenosylmethionine
- s-adenosylhomocysteine
- homocysteine
- folate
- sarcosine
-
adenosyltransferase
- cystathionine
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transmethylation
- adomet
-
betaine-homocysteine
-
remethylation
- beta-synthase
-
one-carbon
-
transsulfuration
- 5-methyltetrahydrofolate
- medicine
-
folate-dependent
- n-methylglycine
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s-methyltransferase
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glycine-n-methyltransferase
- guanidinoacetate
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folate-deficient
- pentaglutamate
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pah-binding
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adohcy
- diagnostics
Reaction
Synonyms
4S polycyclic aromatic hydrocarbon binding protein, glycine methyltransferase, glycine N-methyltransferase, glycine-N methyltransferase, GNMT, Gnmt gene product, methyltransferase, glycine, S-adenosyl-L-methionine:glycine methyltransferase
ECTree
2.1.1.20 glycine N-methyltransferaseAdvanced search results
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Cloned on EC 2.1.1.20 - glycine N-methyltransferase
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CLONED (Commentary) 
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
expression in Escherichia coli
full-length human GNMT is used as the bait in a yeast two-hybrid screen system with a human kidney cDNA library
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overview
PC-3 cells, LNCaP cells, HA22T/VGH cells and HEK-293A cells transfected with plasmid containing haplotype C
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when expressed in pTYB vector as a fusion protein with intein and the chitin binding domain, a cleavage of intein is found. The cleavage takes place at two sites near the N-terminus of intein and results in the appearance of an abnormal GNMT protein after one-column cleavage of the fusion protein, which can not be separated from normal GNMT. For this reason expression is done in the vector pET-17b. Expression of soluble protein in Escherichia coli at about 20-40 mg/L
wild-type and mutant enzymes H176N, L49P and N140S, expressed in Escherichia coli
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when expressed in pTYB vector as a fusion protein with intein and the chitin binding domain, a cleavage of intein is found. The cleavage takes place at two sites near the N-terminus of intein and results in the appearance of an abnormal GNMT protein after one-column cleavage of the fusion protein, which can not be separated from normal GNMT. For this reason expression is done in the vector pET-17b. Expression of soluble protein in Escherichia coli at about 20-40 mg/L
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when expressed in pTYB vector as a fusion protein with intein and the chitin binding domain, a cleavage of intein is found. The cleavage takes place at two sites near the N-terminus of intein and results in the appearance of an abnormal GNMT protein after one-column cleavage of the fusion protein, which can not be separated from normal GNMT. For this reason expression is done in the vector pET-17b. Expression of soluble protein in Escherichia coli at about 20-40 mg/L
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when expressed in pTYB vector as a fusion protein with intein and the chitin binding domain, a cleavage of intein is found. The cleavage takes place at two sites near the N-terminus of intein and results in the appearance of an abnormal GNMT protein after one-column cleavage of the fusion protein, which can not be separated from normal GNMT. For this reason expression is done in the vector pET-17b. Expression of soluble protein in Escherichia coli at about 20-40 mg/L
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