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Information on EC 2.1.1.20 - glycine N-methyltransferase
for references in articles please use BRENDA:EC2.1.1.20
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EC Tree 2 Transferases
2.1 Transferring one-carbon groups
2.1.1 Methyltransferases
2.1.1.20 glycine N-methyltransferase
IUBMB Comments
This enzyme is thought to play an important role in the regulation of methyl group metabolism in the liver and pancreas by regulating the ratio between S-adenosyl-L-methionine and S-adenosyl-L-homocysteine. It is inhibited by 5-methyltetrahydrofolate pentaglutamate . Sarcosine, which has no physiological role, is converted back into glycine by the action of EC 1.5.8.3, sarcosine dehydrogenase.
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
- 2.1.1.20
- s-adenosylmethionine
- s-adenosylhomocysteine
- homocysteine
- folate
- sarcosine
-
adenosyltransferase
- cystathionine
-
transmethylation
- adomet
-
betaine-homocysteine
-
remethylation
- beta-synthase
-
one-carbon
-
transsulfuration
- 5-methyltetrahydrofolate
- medicine
-
folate-dependent
- n-methylglycine
-
s-methyltransferase
-
glycine-n-methyltransferase
- guanidinoacetate
-
folate-deficient
- pentaglutamate
-
pah-binding
-
adohcy
- diagnostics
showSynonyms
gnmt, glycine n-methyltransferase, glycine methyltransferase, glycine-n methyltransferase, s-adenosyl-l-methionine:glycine n-methyltransferase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
glycine methyltransferase
glycine N-methyltransferase
GMT
GNMT
methyltransferase, glycine
-
-
-
-
S-adenosyl-L-methionine:glycine methyltransferase
-
-
-
-
TVD_RS00875
TvGMT
glycine methyltransferase
-
-
-
-
GNMT
-
-
-
-
GNMT
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
S-adenosyl-L-methionine + glycine = S-adenosyl-L-homocysteine + sarcosine
N-terminal acetylation or deprotonation is required for cooperative reaction mechanism
-
S-adenosyl-L-methionine + glycine = S-adenosyl-L-homocysteine + sarcosine
mechanism
S-adenosyl-L-methionine + glycine = S-adenosyl-L-homocysteine + sarcosine
overview mechanism
-
S-adenosyl-L-methionine + glycine = S-adenosyl-L-homocysteine + sarcosine
overview mechanism
-
S-adenosyl-L-methionine + glycine = S-adenosyl-L-homocysteine + sarcosine
overview mechanism
-
S-adenosyl-L-methionine + glycine = S-adenosyl-L-homocysteine + sarcosine
overview mechanism
-
S-adenosyl-L-methionine + glycine = S-adenosyl-L-homocysteine + sarcosine
enzyme is also a polycyclic aromatic hydrocarbon binding protein
-
S-adenosyl-L-methionine + glycine = S-adenosyl-L-homocysteine + sarcosine
homodimer of enzyme acts as polycyclic aromatic hydrocarbon binding protein involved in cytochrome P-450IA1 expression
-
S-adenosyl-L-methionine + glycine = S-adenosyl-L-homocysteine + sarcosine
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
methyl group transfer
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
MetaCyc
glycine betaine biosynthesis IV (from glycine), glycine betaine biosynthesis V (from glycine)
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SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:glycine N-methyltransferase
This enzyme is thought to play an important role in the regulation of methyl group metabolism in the liver and pancreas by regulating the ratio between S-adenosyl-L-methionine and S-adenosyl-L-homocysteine. It is inhibited by 5-methyltetrahydrofolate pentaglutamate [4]. Sarcosine, which has no physiological role, is converted back into glycine by the action of EC 1.5.8.3, sarcosine dehydrogenase.
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CAS REGISTRY NUMBER
COMMENTARY
37228-72-1
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
S-adenosyl-L-methionine + glycine
S-adenosyl-L-homocysteine + N-methylglycine
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + glycine
S-adenosyl-L-homocysteine + N-methylglycine
-
Substrates: key regulatory enzyme for methyl group metabolism by regulating the S-adenosyl-L-methionine/S-adenosyl-L-homocysteine ratio
Products: -
Products: -
?
S-adenosyl-L-methionine + glycine
S-adenosyl-L-homocysteine + N-methylglycine
-
Substrates: key enzyme for the regulation of the ratio of S-adenosylmethionine to S-adenosylhomocysteine
Products: N-methylglycine = sarcosine
Products: N-methylglycine = sarcosine
?
S-adenosyl-L-methionine + glycine
S-adenosyl-L-homocysteine + N-methylglycine
-
Substrates: key enzyme for the regulation of the ratio of S-adenosylmethionine to S-adenosylhomocysteine, affects genetic stability by regulating DNA-methylation, key role in the one-carbon metabolism pathway
Products: N-methylglycine = sarcosine
Products: N-methylglycine = sarcosine
?
S-adenosyl-L-methionine + glycine
S-adenosyl-L-homocysteine + N-methylglycine
Substrates: key enzyme for the regulation of the ratio of S-adenosylmethionine to S-adenosylhomocysteine
Products: N-methylglycine = sarcosine
Products: N-methylglycine = sarcosine
?
S-adenosyl-L-methionine + glycine
S-adenosyl-L-homocysteine + N-methylglycine
Substrates: -
Products: N-methylglycine = sarcosine
Products: N-methylglycine = sarcosine
?
S-adenosyl-L-methionine + glycine
S-adenosyl-L-homocysteine + N-methylglycine
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + glycine
S-adenosyl-L-homocysteine + N-methylglycine
Substrates: key regulatory enzyme for methyl group metabolism by regulating the S-adenosyl-L-methionine/S-adenosyl-L-homocysteine ratio
Products: -
Products: -
?
S-adenosyl-L-methionine + glycine
S-adenosyl-L-homocysteine + N-methylglycine
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + glycine
S-adenosyl-L-homocysteine + N-methylglycine
-
Substrates: key enzyme for the regulation of the ratio of S-adenosylmethionine to S-adenosylhomocysteine, affects genetic stability by regulating DNA methylation and interacting with environmental carcinogens
Products: N-methylglycine = sarcosine
Products: N-methylglycine = sarcosine
?
S-adenosyl-L-methionine + glycine
S-adenosyl-L-homocysteine + N-methylglycine
-
Substrates: key enzyme for the regulation of the ratio of S-adenosylmethionine to S-adenosylhomocysteine
Products: N-methylglycine = sarcosine
Products: N-methylglycine = sarcosine
?
S-adenosyl-L-methionine + glycine
S-adenosyl-L-homocysteine + N-methylglycine
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + glycine
S-adenosyl-L-homocysteine + N-methylglycine
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + glycine
S-adenosyl-L-homocysteine + N-methylglycine
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + glycine
S-adenosyl-L-homocysteine + N-methylglycine
Substrates: key regulatory enzyme for methyl group metabolism by regulating the S-adenosyl-L-methionine/S-adenosyl-L-homocysteine ratio
Products: -
Products: -
?
S-adenosyl-L-methionine + glycine
S-adenosyl-L-homocysteine + N-methylglycine
-
Substrates: key enzyme for the regulation of the ratio of S-adenosylmethionine to S-adenosylhomocysteine
Products: N-methylglycine = sarcosine
Products: N-methylglycine = sarcosine
?
S-adenosyl-L-methionine + glycine
S-adenosyl-L-homocysteine + N-methylglycine
Substrates: key enzyme for the regulation of the ratio of S-adenosylmethionine to S-adenosylhomocysteine, control of the methylating potential of the cell
Products: N-methylglycine = sarcosine
Products: N-methylglycine = sarcosine
?
S-adenosyl-L-methionine + glycine
S-adenosyl-L-homocysteine + N-methylglycine
-
Substrates: -
Products: N-methylglycine = sarcosine
Products: N-methylglycine = sarcosine
?
S-adenosyl-L-methionine + glycine
S-adenosyl-L-homocysteine + N-methylglycine
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + glycine
S-adenosyl-L-homocysteine + N-methylglycine
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + glycine
S-adenosyl-L-homocysteine + N-methylglycine
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + glycine
S-adenosyl-L-homocysteine + N-methylglycine
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + glycine
S-adenosyl-L-homocysteine + sarcosine
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + glycine
S-adenosyl-L-homocysteine + sarcosine
-
Substrates: mechanism: the bound S-adenosyl-L-methionine is firmly connected to protein and a Gly pocket" is created near the bound S-adenosyl-L-methionine. The second substrate Gly binds to Arg175 and is brought into the Gly pocket. Five hydrogen bonds connect the Gly in the proximity of the bound S-adenosyl-L-methionine and orient the lone pair orbital on the amino nitrogen of Gly towards the donor methyl group of S-adenosyl-L-methionine. Thermal motion of the enzyme leads to a collision of the N and C(E) so that a SN2 methyltransfer reaction occurs
Products: -
Products: -
?
S-adenosyl-L-methionine + glycine
S-adenosyl-L-homocysteine + sarcosine
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + glycine
S-adenosyl-L-homocysteine + sarcosine
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + glycine
S-adenosyl-L-homocysteine + sarcosine
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + glycine
S-adenosyl-L-homocysteine + sarcosine
-
Substrates: mechanism: the bound S-adenosyl-L-methionine is firmly connected to protein and a Gly pocket" is created near the bound S-adenosyl-L-methionine. The second substrate Gly binds to Arg175 and is brought into the Gly pocket. Five hydrogen bonds connect the Gly in the proximity of the bound S-adenosyl-L-methionine and orient the lone pair orbital on the amino nitrogen of Gly towards the donor methyl group of S-adenosyl-L-methionine. Thermal motion of the enzyme leads to a collision of the N and C(E) so that a SN2 methyltransfer reaction occurs
Products: -
Products: -
?
S-adenosyl-L-methionine + glycine
S-adenosyl-L-homocysteine + sarcosine
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + glycine
S-adenosyl-L-homocysteine + sarcosine
-
Substrates: strict specificity for glycine as methyl acceptor
Products: -
Products: -
?
S-adenosyl-L-methionine + glycine
S-adenosyl-L-homocysteine + sarcosine
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + glycine
S-adenosyl-L-homocysteine + sarcosine
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + glycine
S-adenosyl-L-homocysteine + sarcosine
-
Substrates: strict specificity for glycine as methyl acceptor
Products: -
Products: -
?
S-adenosyl-L-methionine + glycine
S-adenosyl-L-homocysteine + sarcosine
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + glycine
S-adenosyl-L-homocysteine + sarcosine
-
Substrates: regulates the ratio of S-adenosylmethionine to S-adenosylhomocysteine
Products: -
Products: -
?
S-adenosyl-L-methionine + glycine
S-adenosyl-L-homocysteine + sarcosine
-
Substrates: the enzyme regulates the methyl group supply for S-adenosylmethionine-dependent transmethylation reactions. All-trans-retinoic acid rapidly induces glycine N-methyltransferase in a dose-dependent manner and reduces circulating methionine and homocysteine levels in rats
Products: -
Products: -
?
S-adenosyl-L-methionine + glycine
S-adenosyl-L-homocysteine + sarcosine
Substrates: mechanism: the bound S-adenosyl-L-methionine is firmly connected to protein and a Gly pocket" is created near the bound S-adenosyl-L-methionine. The second substrate Gly binds to Arg175 and is brought into the Gly pocket. Five hydrogen bonds connect the Gly in the proximity of the bound S-adenosyl-L-methionine and orient the lone pair orbital on the amino nitrogen of Gly towards the donor methyl group of S-adenosyl-L-methionine. Thermal motion of the enzyme leads to a collision of the N and C(E) so that a SN2 methyltransfer reaction occurs
Products: -
Products: -
?
S-adenosyl-L-methionine + glycine
S-adenosyl-L-homocysteine + sarcosine
-
Substrates: mechanism: the bound S-adenosyl-L-methionine is firmly connected to protein and a Gly pocket" is created near the bound S-adenosyl-L-methionine. The second substrate Gly binds to Arg175 and is brought into the Gly pocket. Five hydrogen bonds connect the Gly in the proximity of the bound S-adenosyl-L-methionine and orient the lone pair orbital on the amino nitrogen of Gly towards the donor methyl group of S-adenosyl-L-methionine. Thermal motion of the enzyme leads to a collision of the N and C(E) so that a SN2 methyltransfer reaction occurs
Products: -
Products: -
?
S-adenosyl-L-methionine + glycine
S-adenosyl-L-homocysteine + sarcosine
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + glycine
S-adenosyl-L-homocysteine + sarcosine
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + glycine
S-adenosyl-L-homocysteine + sarcosine
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + glycine
S-adenosyl-L-homocysteine + sarcosine
Substrates: -
Products: -
Products: -
?
additional information
?
-
-
Substrates: interaction of benzo(a)pyrene with the enzyme may contribute to carcinogenesis
Products: -
Products: -
?
additional information
?
-
-
Substrates: major folate binding protein
Products: -
Products: -
?
additional information
?
-
-
Substrates: major folate binding protein, interacts with environmental carcinogens such as benzo(a)pyrene
Products: -
Products: -
?
additional information
?
-
Substrates: major folate binding protein
Products: -
Products: -
?
additional information
?
-
-
Substrates: major folate binding protein
Products: -
Products: -
?
additional information
?
-
-
Substrates: a mammalian target of rapamycin (mTOR) inhibitor (DEP domain containing MTOR-interacting protein [DEPDC6/DEPTOR]) is identified as a GNMT-binding protein by using yeast two-hybrid screening. The C-terminal half of GNMT interacts with the PSD-95/Dlg1/ZO-1 (PDZ) domain of DEPDC6/DEPTOR
Products: -
Products: -
?
additional information
?
-
-
Substrates: major folate binding protein, involved in the regulation of the expression of S-adenosylhomocysteine hydrolase and formiminotransferase cyclodeaminase, binds benzo(a)pyrene and prevents DNA-adduct formation
Products: -
Products: -
?
additional information
?
-
-
Substrates: major folate binding protein
Products: -
Products: -
?
additional information
?
-
Substrates: GNMT is phosphorylated by cAMP-dependent protein kinase at Ser9, Ser71, Ser139, Ser182, and Ser241
Products: -
Products: -
?
additional information
?
-
-
Substrates: GNMT is phosphorylated by cAMP-dependent protein kinase at Ser9, Ser71, Ser139, Ser182, and Ser241
Products: -
Products: -
?
additional information
?
-
-
Substrates: all-trans-retinoic acid and dexamethasone independently induce GNMT in liver, no effect on enzyme from pancreas
Products: -
Products: -
?
additional information
?
-
-
Substrates: major folate binding protein
Products: -
Products: -
?
additional information
?
-
Substrates: major folate binding protein
Products: -
Products: -
?
additional information
?
-
Substrates: kinetic isotope effects at the transferred methyl group implicate a compaction effect that is conferred by the protein structure
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
S-adenosyl-L-methionine + glycine
S-adenosyl-L-homocysteine + N-methylglycine
-
Substrates: key regulatory enzyme for methyl group metabolism by regulating the S-adenosyl-L-methionine/S-adenosyl-L-homocysteine ratio
Products: -
Products: -
?
S-adenosyl-L-methionine + glycine
S-adenosyl-L-homocysteine + N-methylglycine
-
Substrates: key enzyme for the regulation of the ratio of S-adenosylmethionine to S-adenosylhomocysteine
Products: N-methylglycine = sarcosine
Products: N-methylglycine = sarcosine
?
S-adenosyl-L-methionine + glycine
S-adenosyl-L-homocysteine + N-methylglycine
-
Substrates: key enzyme for the regulation of the ratio of S-adenosylmethionine to S-adenosylhomocysteine, affects genetic stability by regulating DNA-methylation, key role in the one-carbon metabolism pathway
Products: N-methylglycine = sarcosine
Products: N-methylglycine = sarcosine
?
S-adenosyl-L-methionine + glycine
S-adenosyl-L-homocysteine + N-methylglycine
Substrates: key enzyme for the regulation of the ratio of S-adenosylmethionine to S-adenosylhomocysteine
Products: N-methylglycine = sarcosine
Products: N-methylglycine = sarcosine
?
S-adenosyl-L-methionine + glycine
S-adenosyl-L-homocysteine + N-methylglycine
Substrates: key regulatory enzyme for methyl group metabolism by regulating the S-adenosyl-L-methionine/S-adenosyl-L-homocysteine ratio
Products: -
Products: -
?
S-adenosyl-L-methionine + glycine
S-adenosyl-L-homocysteine + N-methylglycine
-
Substrates: key enzyme for the regulation of the ratio of S-adenosylmethionine to S-adenosylhomocysteine, affects genetic stability by regulating DNA methylation and interacting with environmental carcinogens
Products: N-methylglycine = sarcosine
Products: N-methylglycine = sarcosine
?
S-adenosyl-L-methionine + glycine
S-adenosyl-L-homocysteine + N-methylglycine
-
Substrates: key enzyme for the regulation of the ratio of S-adenosylmethionine to S-adenosylhomocysteine
Products: N-methylglycine = sarcosine
Products: N-methylglycine = sarcosine
?
S-adenosyl-L-methionine + glycine
S-adenosyl-L-homocysteine + N-methylglycine
Substrates: key regulatory enzyme for methyl group metabolism by regulating the S-adenosyl-L-methionine/S-adenosyl-L-homocysteine ratio
Products: -
Products: -
?
S-adenosyl-L-methionine + glycine
S-adenosyl-L-homocysteine + N-methylglycine
-
Substrates: key enzyme for the regulation of the ratio of S-adenosylmethionine to S-adenosylhomocysteine
Products: N-methylglycine = sarcosine
Products: N-methylglycine = sarcosine
?
S-adenosyl-L-methionine + glycine
S-adenosyl-L-homocysteine + N-methylglycine
Substrates: key enzyme for the regulation of the ratio of S-adenosylmethionine to S-adenosylhomocysteine, control of the methylating potential of the cell
Products: N-methylglycine = sarcosine
Products: N-methylglycine = sarcosine
?
S-adenosyl-L-methionine + glycine
S-adenosyl-L-homocysteine + sarcosine
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + glycine
S-adenosyl-L-homocysteine + sarcosine
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + glycine
S-adenosyl-L-homocysteine + sarcosine
-
Substrates: regulates the ratio of S-adenosylmethionine to S-adenosylhomocysteine
Products: -
Products: -
?
S-adenosyl-L-methionine + glycine
S-adenosyl-L-homocysteine + sarcosine
-
Substrates: the enzyme regulates the methyl group supply for S-adenosylmethionine-dependent transmethylation reactions. All-trans-retinoic acid rapidly induces glycine N-methyltransferase in a dose-dependent manner and reduces circulating methionine and homocysteine levels in rats
Products: -
Products: -
?
S-adenosyl-L-methionine + glycine
S-adenosyl-L-homocysteine + sarcosine
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + glycine
S-adenosyl-L-homocysteine + sarcosine
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + glycine
S-adenosyl-L-homocysteine + sarcosine
Substrates: -
Products: -
Products: -
?
additional information
?
-
-
Substrates: interaction of benzo(a)pyrene with the enzyme may contribute to carcinogenesis
Products: -
Products: -
?
additional information
?
-
-
Substrates: major folate binding protein
Products: -
Products: -
?
additional information
?
-
-
Substrates: major folate binding protein, interacts with environmental carcinogens such as benzo(a)pyrene
Products: -
Products: -
?
additional information
?
-
Substrates: major folate binding protein
Products: -
Products: -
?
additional information
?
-
-
Substrates: major folate binding protein
Products: -
Products: -
?
additional information
?
-
-
Substrates: a mammalian target of rapamycin (mTOR) inhibitor (DEP domain containing MTOR-interacting protein [DEPDC6/DEPTOR]) is identified as a GNMT-binding protein by using yeast two-hybrid screening. The C-terminal half of GNMT interacts with the PSD-95/Dlg1/ZO-1 (PDZ) domain of DEPDC6/DEPTOR
Products: -
Products: -
?
additional information
?
-
-
Substrates: major folate binding protein, involved in the regulation of the expression of S-adenosylhomocysteine hydrolase and formiminotransferase cyclodeaminase, binds benzo(a)pyrene and prevents DNA-adduct formation
Products: -
Products: -
?
additional information
?
-
-
Substrates: major folate binding protein
Products: -
Products: -
?
additional information
?
-
-
Substrates: all-trans-retinoic acid and dexamethasone independently induce GNMT in liver, no effect on enzyme from pancreas
Products: -
Products: -
?
additional information
?
-
-
Substrates: major folate binding protein
Products: -
Products: -
?
additional information
?
-
Substrates: major folate binding protein
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
5-methyltetrahydrofolate monoglutamate
-
native N-acetylated form of the enzyme shows 50% inhibition at 0.05 mM while the recombinant non-acetylated form shows 50% inhibition at 1.89 mM
folate
the native rat liver GNMT contains an acetylated N-terminal valine and is inhibited much more efficiently compared to the recombinant protein
additional information
-
folate-containing diets attenuate GNMT activity in diabetic rats but are without effect on abundance
-
5-Methyltetrahydrofolate pentaglutamate
-
noncompetitive inhibitor with respect to substrates S-adenosyl-L-methionine and glycine
5-Methyltetrahydrofolate pentaglutamate
noncompetitive inhibitor regarding substrates S-adenosyl-L-methionine and glycine
5-Methyltetrahydrofolate pentaglutamate
-
noncompetitive inhibitor with respect to substrates S-adenosyl-L-methionine and glycine
5-Methyltetrahydrofolate pentaglutamate
-
native N-acetylated form of the enzyme shows 50% inhibition at 0.0013 mM while the recombinant non-acetylated form shows 50% inhibition at 0.59 mM
5-Methyltetrahydrofolate pentaglutamate
-
noncompetitive inhibitor with respect to substrates S-adenosyl-L-methionine and glycine
5-Methyltetrahydrofolate pentaglutamate
noncompetitive inhibitor with respect to substrates S-adenosyl-L-methionine and glycine
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
phosphate
-
in vitro phosphorylation increases activity, about 0.55 mol of phosphate present per mol of N-methyltransferase subunit
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5 - 9.5
-
pH 7.5: about 40% of maximal activity, pH 9.5: about 45% of maximal activity
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
37
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
485226, 485227, 657755, 658385, 660421, 660475, 673122, 677194, 703849, 704524, 706826, 706903, 720299, 720403, 720481, 734506, 735096
-
-
brenda
normal enzyme and naturally occurring H176N mutation which is found in humans with hypermethioninaemia
UniProt
brenda
three cases of GNMT mutations known, all suffering from mild liver disease and display elevated methionine levels
-
-
brenda
construction of GNMT knockout mice, loss of enzyme results in highly elevated levels of free methionine and S-adenosyl-L-methionine
SwissProt
brenda
-
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
high expression in normal tissue, reduced expression in tumorous tissue, some tumor samples show no enzyme expression
brenda
-
GNMT is expressed in the epithelium of the colon under normal conditions, and with dextran sulfate sodium treatment, its expression is predominant in infiltrated leukocytes of lesions
brenda
in unfertilized, 2 days postfertilization, and 3 days postfertilization embryos GNMT is constitutively higher than in 4, 7, 10 or 14 days postfertilization embryos
brenda
-
GNMT is expressed in the epithelium of the colon under normal conditions, and with dextran sulfate sodium treatment, its expression is predominant in infiltrated leukocytes of lesions
brenda
-
36.4% of tissues show loss of heterozygosity of the GNMT gene, GNMT expression diminished in 82.2% of tissues
brenda
additional information
-
high expression in normal tissue, only 4% of hepatocellular carcinoma show GNMT expression
brenda
-
high GNMT-expression in normal prostatic and benign prostatic hyperplasia tissues, whereas it was diminished in 82% of the prostate cancer tissues
brenda
additional information
-
abundant GNMT expression in benign prostatic hyperplasia tissue
brenda
additional information
-
no GNMT activity is detected in fetal liver, Novikoff hepatoma cells, Morris hepatoma cells, and Ehrlich ascites cells
brenda
additional information
no GNMT activity is detected in fetal liver, Novikoff hepatoma cells, Morris hepatoma cells, and Ehrlich ascites cells
brenda
additional information
-
no GNMT activity is detected in fetal liver, Novikoff hepatoma cells, Morris hepatoma cells, and Ehrlich ascites cells
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
-
GNMT is expressed in cytoplasm before treatment with benzo(a)pyrene and translocated to cell nuclei after treatment with benzo(a)pyrene
brenda
-
concentrated in the paranuclear region near the bile duct lumen
brenda
-
GNMT is expressed in cytoplasm before treatment with benzo(a)pyrene and translocated to cell nuclei after treatment with benzo(a)pyrene
brenda
-
GNMT is translocated into nuclei after aflatoxin B1 treatment
brenda
Highest Expressing Human Cell Lines
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
physiological function
malfunction
-
Gnmt knockout mice develop hepatocellular carcinoma, hemangioma, dysplastic nodules, fatty nodules and lung metastasis, DNA methyltransferase activity is decreased in 11 weeks old Gnmt knockout mice, the MAPK pathway is activated in female Gnmt knockout mice
malfunction
-
Gnmt knockout mice develop fatty livers when they have increased S-adenosyl-L-methionine
malfunction
-
siRNA mediated GNMT knockdown results in an inhibition of proliferation, and induces G1 arrest and apoptosis in prostate cancer cell lines. Patients with high GNMT cytoplasmic expression showed significantly lower disease-free survival rates than patients with low expression
malfunction
-
overexpression of GNMT causes activation of mTOR/raptor downstream signaling and delays G2/M cell cycle progression, which altogether results in cellular senescence
metabolism
-
GNMT is involved in both hepatic methyl group and one-carbon metabolism
metabolism
GNMT is involved in both hepatic methyl group and one-carbon metabolism
metabolism
-
GNMT is involved in both hepatic methyl group and one-carbon metabolism
metabolism
-
GNMT is involved in both hepatic methyl group and one-carbon metabolism
metabolism
-
GNMT is involved in both hepatic methyl group and one-carbon metabolism
metabolism
-
GNMT is involved in both hepatic methyl group and one-carbon metabolism
metabolism
substrate specificities of enzymes GMT and SDMT are quite different from the enzymes for glycine methylation in halophilic Halorhodospira halochloris, GSMT and SDMT
metabolism
-
substrate specificities of enzymes GMT and SDMT are quite different from the enzymes for glycine methylation in halophilic Halorhodospira halochloris, GSMT and SDMT
-
physiological function
-
GNMT plays a major role in maintaining normal S-adenosyl-L-methionine levels
physiological function
GNMT plays a major role in maintaining normal S-adenosyl-L-methionine levels
physiological function
-
GNMT plays a major role in maintaining normal S-adenosyl-L-methionine levels
physiological function
-
GNMT plays a major role in maintaining normal S-adenosyl-L-methionine levels
physiological function
-
GNMT plays a major role in maintaining normal S-adenosyl-L-methionine levels
physiological function
-
GNMT is a tumor suppressor for hepatocellular carcinoma cells and it exerts protective effects in hepatocytes via direct interaction with aflatoxin B1, resulting in reduced aflatoxin B1-DNA adducts formation and cell death
physiological function
-
using HepG2 -/- cells and HepG2 cells overexpressing GNMT it is shown that GNMT in is involved in methyl group homeostasis by regulating transmethylation kinetics and DNA methylation
physiological function
-
GNMT regulates hepatocellular growth in part through interacting with DEPDC6/DEPTOR and modulating mTOR/raptor signaling pathway
physiological function
-
mice with genetic deletion of GNMT show increased susceptibility to dextran sulfate sodium induction of colitis. Severe colonic inflammation, including increased crypt loss, leukocyte infiltration, and hemorrhage, are greater with dextran sulfate sodium treatment in GNMT?/? than wild-type mice. The expression of adhesion molecule and inflammatory mediators in the colon is significantly higher with dextran sulfate sodium treatment in GNMT?/? than wild-type mice. Loss of GNMT decreases cell apoptosis in colitis lesions with dextran sulfate sodium treatment
physiological function
experimental autoimmune encephalomyelitis severity is reduced significantly in Gnmt-/- mice. Gnmt-/- mice have significantly lower levels of mononuclear cell infiltration and demyelination than the wild-type mice. Expression levels of proinflammatory cytokines, including interferon-gamma and interleukin 17A, are much lower in the spinal cord of Gnmt-/- than in that of wild-type mice. Myelin oligodendrocyte glycoprotein-specific T-cell proliferation and induction of T-helper Th1 and Th17 cells are markedly suppressed in myelin oligodendrocyte glycoprotein-induced Gnmt-/- mice. The number of regulatory T cells is significantly increased in these mice
physiological function
GNMT affects transmethylation kinetics and S-adenosylmethionine synthesis, and facilitates the conservation of methyl groups by limiting homocysteine remethylation fluxes. Restoring GNMT assists methylfolate-dependent reactions and ameliorates the consequences of folate depletion. GNMT expression in vivo improves folate retention and bioavailability in the liver. Loss of GNMT impairs nucleotide biosynthesis. Over-expression of GNMT enhances nucleotide biosynthesis and improves DNA integrity by reducing uracil misincorporation in DNA both in vitro and in vivo
physiological function
reduced insulin/IGF signaling activity modulates methionine metabolism, through tissue-specific regulation of glycine N-methyltransferase Gnmt. This regulation is required for full insulin/IGF signaling-mediated longevity. Fat body-specific expression of Gnmt is sufficient to extend lifespan. Reducing insulin/IGF signaling activity leads to a Gnmt-dependent increase in spermidine levels. Both spermidine treatment and reduced insulin/IGF signaling activity are sufficient to extend the lifespan of Drosophila, but only in the presence of Gnmt
physiological function
in the liver of liver-specific IRS1 KO mice, expression of GNMT is increased
physiological function
QM/MM kinetic ananlysis. The methyl-group charge reaches a maximum after passing the transition state and decreases again. The donor-acceptor distance reaches the minimum value at this point, and the averaged electrostatic potentials created by the different environments at the S donor, N acceptor and C methyl atoms change from the reactant state to the point with a value of the reaction coordinate around +0.5 A and it remain stable from this point on in all environments
physiological function
glycine N-methyltransferase (TvGMT) and sarcosine dimethylglycine N-methyltransferase (TvSDMT, EC 2.1.1.157) are responsible for the conversion of glycine to glycine betaine by adding three methyl groups to the amino group of glycine. N-containing glycine betaine is a main compatible solute in Thioalkalivibrio versutus strain D301. Glycine betaine contributes to the increased tolerance to extreme environments in some of Thioalkalivibrio species, glycine betaine is responsible for the high-salt tolerance in Thioalkalivibrio versutus strain D301
physiological function
enzyme expression is required for the onset of invasive prostate cancer
physiological function
enzyme expression is required for the onset of invasive prostate cancer
physiological function
the glycine/enzyme/sarcosine axis is involved in benzene-induced hematotoxicity
physiological function
in Huh-7 and Hep-G2 cell lines, the enzyme forced expression inhibits the proliferation and promotes apoptosis. At the molecular level, enzyme overexpression inhibits the expression of CYP1A, phosphatidylinositol-3,4,5-trisphosphate-dependent Rac exchange factor 2, poly(ADP-ribose) polymerase 1, and nuclear factor-kappa B genes
physiological function
enzyme overexpression inhibits the expression of CYP1A, phosphatidylinositol-3,4,5-trisphosphate-dependent Rac exchange factor 2, poly(ADP-ribose) polymerase 1, and nuclear factor-kappa B genes
physiological function
the enzyme is involved in the folic acid-related mechanisms relevant to renal fibrosis
physiological function
the enzyme is involved in the folic acid-related mechanisms relevant to renal fibrosis
physiological function
-
glycine N-methyltransferase (TvGMT) and sarcosine dimethylglycine N-methyltransferase (TvSDMT, EC 2.1.1.157) are responsible for the conversion of glycine to glycine betaine by adding three methyl groups to the amino group of glycine. N-containing glycine betaine is a main compatible solute in Thioalkalivibrio versutus strain D301. Glycine betaine contributes to the increased tolerance to extreme environments in some of Thioalkalivibrio species, glycine betaine is responsible for the high-salt tolerance in Thioalkalivibrio versutus strain D301
-
Show AA Sequence and Transmembrane Helices (1279 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
130000
32420 - 79000
-
mass spectrometry, mass spectra of the proteins greatly depend on the method of sample preparation and storage
32500
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homotetramer
tetramer
trimer or tetramer
-
3 or 4 * 27000-33000, nonidentical subunits, SDS-PAGE
tetramer
crystal structure analysis, in the presence of moderate (2-4 M) urea concentrations the tetrameric enzyme dissociates into compact monomers, higher concentrations of urea (7-8 M) promote complete denaturation of enzyme
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
acetylated protein
-
N-terminal valine of native GNMT is N-acetylated while in the recombinant enzyme it is not
glycoprotein
-
4 residues of sialic acid and 2 residues of hexose per mol of protein
phosphoprotein
phosphoprotein
-
GNMT is phosphorylated by cAMP-dependent protein kinase at Ser9, Ser71, Ser139, Ser182, and Ser241
phosphoprotein
-
GNMT is phosphorylated by cAMP-dependent protein kinase at Ser9, Ser71, Ser139, Ser182, and Ser241
phosphoprotein
-
GNMT is phosphorylated by cAMP-dependent protein kinase at Ser9, Ser71, Ser139, Ser182, and Ser241
phosphoprotein
GNMT is phosphorylated by cAMP-dependent protein kinase at Ser9, Ser71, Ser139, Ser182, and Ser241
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
wild type and H176N mutant enzyme as cocrystals with a citrate molecule bound in the active site
crystals are grown at 22°C by hanging drop vapor diffusion method, crystallized in two crystal forms, a monoclinic form and a tetragonal form, P2(1) and P4(1)2(1)2
-
crystallized by the sitting drop method in complex with (6S)-5-methyltetrahydrofolat monoglutamate
GNMT complexed with 5-methyltetrahydrofolate, by the sitting drop method at room temperature, two folate binding sites in the intersubunit areas of the tetramer, each folate binding site is formed primarily by two 1-7 N-terminal regions of one pair of subunits and two 205-218 regions of the other pair of subunits. Both the pteridine and p-aminobenzoyl rings are located in the hydrophobic cavities formed by Tyr5, Leu207, and Met215 residues of all subunits
hanging drop method of vapor diffusion, crystal structure of the enzyme complexed with S-adenosyl-L-methionine and acetate (a potent competitive inhibitor of Gly) and the R175K mutated enzyme complexed with S-adenosyl-L-methionine are determined at 2.8 A and 3.0 A resolution, respectively
native and recombinant protein, to 2.55 A resolution. The native rat liver GNMT contains an acetylated N-terminal valine and is inhibited much more efficiently compared to the recombinant protein. In the folate-GNMT complexes with the native enzyme, two folate molecules establish three and four hydrogen bonds with the protein. In the folate-recombinant GNMT complex only one hydrogen bond is established. This difference results in more effective inhibition by folate of the native liver GNMT activity compared to the recombinant enzyme
sitting-drop vapor diffusion method in complex with 5-methyltetrahydrofolate pentaglutamate, two molecules of inhibitor bound to a tetramer
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
DELTA171-295
-
to map the interactive domain of GNMT plasmids containing different domains GNMT are constructed: The C-terminal 171-295 amino acid fragment of GNMT is identified as interactive domain
H176N
N140S
R175K
Y194F
the ratio of turnover-number to KM-value for S-adenosyl-L-methionine is 2.4fold lower than the wild-type value, the ratio of turnover-number to KM-value for Gly is 16.4fold lower than the wild-type value
Y21A
Y21F
Y21G
Y21S
mutant yields the same magnitude of binary isotope effect as wild-type
Y21T
mutant yields the same magnitude of binary isotope effect as wild-type
Y21V
mutant yields the same magnitude of binary isotope effect as wild-type
Y220F
the ratio of turnover-number to KM-value for S-adenosyl-L-methionine is nearly identical to the wild-type value, the ratio of turnover-number to KM-value for Gly is 179fold lower than the wild-type value
Y242F
the ratio of turnover-number to KM-value for S-adenosyl-L-methionine is 1.14fold higher than the wild-type value, the ratio of turnover-number to KM-value for Gly is 2325fold lower than the wild-type value
Y33F
the ratio of turnover-number to KM-value for S-adenosyl-L-methionine is nearly identical to the wild-type value, the ratio of turnover-number to KM-value for Gly is 123fold lower than the wild-type value
additional information
H176N
naturally occurring mutation, 25% less activity and highly reduced stability compared with the native enzyme, completely inactive at 2 M urea compared with 60% remaining activity of the wild type enzyme
R175K
crystal structure: N-terminal domains of subunits have moved out of the active sites of adjacent subunits
R175K
the mutation reduces the binding affinity of glycine but not of S-adenosyl-L-methionine and reduces the catalytic efficiency compared to the wild type enzyme
Y21A
mutant yields the same magnitude of binary isotope effect as wild-type
Y21A
comparison of QM/MM kinetic data for the methyl transfer among wild-type and mutants. Wild-type protein generates the most favorable electrostatic environment to stabilize the charge developed on the methyl group in the transition state, and thus is the most favourable environment to catalyze the reaction. The detrimental effect of substitution of Tyr21 on the electrostatic potential is partially compensated by His142 that, by approaching to the methyl group, generates a higher potential
Y21F
the ratio of turnover-number to KM-value for S-adenosyl-L-methionine is 5fold lower than the wild-type value, the ratio of turnover-number to KM-value for Gly is 2.4fold lower than the wild-type value
Y21F
mutant yields the same magnitude of binary isotope effect as wild-type
Y21F
comparison of QM/MM kinetic data for the methyl transfer among wild-type and mutants. Wild-type protein generates the most favorable electrostatic environment to stabilize the charge developed on the methyl group in the transition state, and thus is the most favourable environment to catalyze the reaction. The detrimental effect of substitution of Tyr21 on the electrostatic potential is partially compensated by His142 that, by approaching to the methyl group, generates a higher potential
Y21G
mutant yields the same magnitude of binary isotope effect as wild-type
Y21G
comparison of QM/MM kinetic data for the methyl transfer among wild-type and mutants. Wild-type protein generates the most favorable electrostatic environment to stabilize the charge developed on the methyl group in the transition state, and thus is the most favourable environment to catalyze the reaction. The detrimental effect of substitution of Tyr21 on the electrostatic potential is partially compensated by His142 that, by approaching to the methyl group, generates a higher potential
additional information
-
patients with mutations Leu49Pro and His176Asn suffer from mild liver disease
additional information
-
construction of -/- and +/- knockout mutants, Gnmt -/- mice show hepatomegaly, hypermethioninemia, and significantly higher levels of serum alanine aminotransferase and hepatic S-adenosylmethionine, down regulation of S-adenosylhomocysteine hydrolase and formiminotransferase cyclodeaminase, abnormally high glycogen accumulation in liver, hypoglycemia, increased serum cholesterol, and significantly lower numbers of white blood cells, neutrophils, and monocytes, some genes of gluconeogenesis enzyme significantly down regulated in Gnmt -/- mice
additional information
-
construction of GNMT knockout mice, knockout mice have elevated serum aminotransferase, methionine, and S-adenosyl-L-methionine levels and develop liver steatosis, fibrosis, and hepatocellular carcinoma, loss of GNMT induces aberrant methylation of DNA and histones, resulting in epigenetic modulation of critical carcinogenic pathways, several Ras and JAK/STAT inhibitors are reduced in liver tumors of enzyme knockout mice
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
urea unfolding of GNMT is a two-step process. The first transition is a reversible dissociation of the GNMT tetramer to compact monomers in 1.0-3.5 M urea with enzyme inactivation. The second step of GNMT unfolding is a reversible transition of monomers from compact to a fully unfolded state with R(S) of 50 A, exposed tryptophan residues, and disrupted secondary structure in 8 M urea
-
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ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
urea
H176N mutant completely inactive at 2 M urea compared with 60% remaining activity of the wild type enzyme
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4C, 5.0 mM DTT, 2.0 mM EDTA, 0.02% NaN3, stable for at least 2 weeks
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
from liver by anion and cation exchange chromatography and from isolated hepatocytes and liver tissue by immunoprecipitation
-
native enzyme from rat liver and recombinant enzyme from Escherichia coli
-
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
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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
-
overview
PC-3 cells, LNCaP cells, HA22T/VGH cells and HEK-293A cells transfected with plasmid containing haplotype C
-
recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)
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
-
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
-
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
-
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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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
benzo[a]pyrene treatment of HepG2 cells (0.001 or 0.01 mM) induces GNMT expression
-
GNMT expression is down-regulated or even completely blocked in liver and prostate tumor tissue
GNMT expression is stimulated by androgen in androgen receptor expressing cells, the stimulation occurs at the mRNA and protein levels. Androgen receptor binds to an androgen response element within the first exon of the GNMT gene in vitro and in vivo
-
the enzyme expression is upregulated both in 1,4-benzoquinone-treated AHH-1 cells and benzene-exposed workers
the enzyme is expressed at low level in human hepatocellular carcinomas with a better prognosis while it is almost absent in fast-growing tumors
the enzyme is repressed upon activation of the oncogenic phosphoinositide-3-kinase pathway
unilateral ureteral obstruction significantly increases the enzyme expression in mice
GNMT expression is down-regulated or even completely blocked in liver and prostate tumor tissue
-
GNMT expression is down-regulated or even completely blocked in liver and prostate tumor tissue
GNMT expression is down-regulated or even completely blocked in liver and prostate tumor tissue
-
GNMT expression is down-regulated or even completely blocked in liver and prostate tumor tissue
-
GNMT expression is down-regulated or even completely blocked in liver and prostate tumor tissue
-
GNMT expression is down-regulated or even completely blocked in liver and prostate tumor tissue
-
the enzyme is expressed at low level in human hepatocellular carcinomas with a better prognosis while it is almost absent in fast-growing tumors
the enzyme is expressed at low level in human hepatocellular carcinomas with a better prognosis while it is almost absent in fast-growing tumors
the enzyme is repressed upon activation of the oncogenic phosphoinositide-3-kinase pathway
the enzyme is repressed upon activation of the oncogenic phosphoinositide-3-kinase pathway
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
diagnostics
medicine
additional information
-
phosphorylated serine residues 71, 182, and 241, in GNMT prepared from liver tissue and hepatocytes an S9 additional residue is phosphorylated, in hepatocytes and in recombinant GNMT S139 is detected, serine 9 is also identified as a target for cAMP-dependent protein kinase in vitro, positions of these phosphorylated residues in the tertiary structure of GNMT indicate their possible effect on enzyme conformation and activity
diagnostics
-
enzyme level suitable as prognostic marker for human cholangiocarcinoma and hepatocellular carcinoma
diagnostics
-
partially suitable to distinguish between benign and malign tumor forms
medicine
-
feeding with excess methionine leads to upregulation of hepatic enzyme
medicine
-
patients with mutations Leu49Pro and His176Asn suffer from mild liver disease
medicine
-
activation and induction of enzyme by retinoids are tissue- and gender-specific
medicine
-
vitamin A may induce enzyme, induction by all-trans-retinoic acid can lead to impairment of essential transmethylation processes
medicine
-
all-trans-retinoic acid and dexamethasone independently induce GNMT in liver, thereby having substantial implications for the potential interaction of retinoic administration with diabetes
medicine
-
GNMT is a tumor susceptibility gene for prostate cancer, three major GNMT haplotypes in our populations, haplotype C conferred protection from the development of prostate cancer and exhibits the highest promoter activity
medicine
-
GNMT sequesters benzo[a]pyrene, diminishes benzo[a]pyrene's effects to the liver detoxification pathway and prevents subsequent cytotoxicity
medicine
-
diabetes increases the activity and abundance of GNMT, lack of dietary folate results in the highest activity of GNMT in diabetic rats without the abundance of the protein being altered
medicine
-
GNMT 1289 C->T polymorphism influences plasma homocysteine and is responsive to folate intake, plasma homocysteine concentrations do not differ among the GNMT C1289T genotypes at baseline. After folate restriction, women with the GNMT 1289 TT genotype have higher homocysteine concentrations than women with the CT or CC genotype. The influence of the GNMT 1289 C->T variant on homocysteine is dependent on the MTHFR C677T genotype. In subjects with the MTHFR 677 CC genotype, homocysteine is greater for GNMT 1289 TT subjects relative to 1289 CT or CC subjects. In subjects with the MTHFR 677 TT genotype, plasma homocysteine concentrations do not differ among the GNMT C1289T genotypes
medicine
-
glycine N-methyltransferase is a tumor susceptibility gene for both hepatocellular carcinoma and prostate cancer
medicine
-
GNMT is a tumor suppressor gene for liver cancer, and is associated with gender disparity in liver cancer susceptibility
medicine
-
GNMT may represent a novel marker of malignant progression and poor prognosis in prostate cancer
medicine
-
GNMT is strongly downregulated in human cancers and is undetectable in cancer cell lines while the transient expression of the protein in cancer cells induces apoptosis and results in the activation of ERK1/2. The antiproliferative effect of GNMT can be partially reversed by treatment with the pancaspase inhibitor zVAD-fmk but not by supplementation with high folate or SAM. GNMT exerts the suppressor effect primarily in cells originated from malignant tumors. High levels of GNMT, detected in regenerating liver and in NIH3T3 mouse fibroblasts, do not produce cytotoxic effects. GNMT, a predominantly cytoplasmic protein, is translocated into nuclei upon transfection of cancer cells. The induction of apoptosis is associated with the GNMT nuclear localization but is independent of its catalytic activity or folate binding
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Heady, J.E.; Kerr, S.J.
Purification and characterization of glycine N-methyltransferase
J. Biol. Chem.
248
69-72
1973
Oryctolagus cuniculus
brenda
Wagner, C.; Decha-Umphai, W.; Corbin, J.
Phosphorylation modulates the activity of glycine N-methyltransferase, a folate binding protein. In vitro phosphorylation is inhibited by the natural folate ligand
J. Biol. Chem.
264
9638-9642
1989
Rattus norvegicus
brenda
Ogawa, H.; Fujioka, M.
Purification and properties of glycine N-methyltransferase from rat liver
J. Biol. Chem.
257
3447-3452
1982
Rattus norvegicus
brenda
Fujioka, M.; Ishiguro, Y.
Reaction of rat liver glycine methyltransferase with 5-p-fluorosulfonylbenzoyladenosine
J. Biol. Chem.
261
6346-6351
1986
Rattus norvegicus
brenda
Yeo, E.J.; Wagner, C.
Purification and properties of pancreatic glycine N-methyltransferase
J. Biol. Chem.
267
24669-24674
1992
Rattus norvegicus
brenda
Fujioka, M.; Takata, Y.; Konishi, K.; Ogawa, H.
Function and reactivity of sulfhydryl groups of rat liver glycine methyltransferase
Biochemistry
26
5696-5702
1987
Rattus norvegicus
brenda
Wagner, C.; Briggs, W.T.; Cook, R.J.
Inhibition of glycine N-methyltransferase activity by folate derivatives: implications for regulation of methyl group metabolism
Biochem. Biophys. Res. Commun.
127
746-752
1985
Rattus norvegicus
brenda
Pattanayek, R.; Newcomer, M.E.; Wagner, C.
Crystal structure of apo-glycine N-methyltransferase (GNMT)
Protein Sci.
7
1326-1331
1998
Rattus norvegicus
brenda
Fu, Z.; Hu, Y.; Konishi, K.; Takata, Y.; Ogawa, H.; Gomi, T.; Fujioka, M.; Takusagawa, F.
Crystal structure of glycine N-methyltransferase from rat liver
Biochemistry
35
11985-11993
1996
Rattus norvegicus (P13255)
brenda
Huang, Y.; Komoto, J.; Konishi, K.; Takata, Y.; Ogawa, H.; Gomi, T.; Fujioka, M.; Takusagawa, F.
Mechanisms for auto-inhibition and forced product release in glycine N-methyltransferase: Crystal structures of wild-type, mutant R175K and S-adenosylhomocysteine-bound R175K enzymes
J. Mol. Biol.
298
149-162
2000
Rattus norvegicus (P13255)
brenda
Bhat, R.; Bresnick, E.
Glycine N-methyltransferase is an example of functional diversity. Role as a polycyclic aromatic hydrocarbon-binding receptor
J. Biol. Chem.
272
21221-21226
1997
Rattus norvegicus
brenda
Bhat, R.; Wagner, C.; Bresnick, E.
The homodimeric form of glycine N-methyltransferase acts as a polycyclic aromatic hydrocarbon-binding receptor
Biochemistry
36
9906-9910
1997
Rattus norvegicus
brenda
Ogawa, H.; Gomi, T.; Imamura, T.; Kobayashi, M.; Huh, N.H.
Rat liver 4 S-benzo[a]pyrene-binding protein is distinct from glycine N-methyltransferase
Biochem. Biophys. Res. Commun.
233
300-304
1997
Rattus norvegicus
brenda
Raha, A.; Wagner, C.; MacDonald, R.G.; Bresnick, E.
Rat liver cytosolic 4 S polycyclic aromatic hydrocarbon-binding protein is glycine N-methyltransferase
J. Biol. Chem.
269
5750-5756
1994
Rattus norvegicus
brenda
Ogawa, H.; Gomi, T.; Takusagawa, F.; Fujioka, M.
Structure, function and physiological role of glycine N-methyltransferase
Int. J. Biochem. Cell Biol.
30
13-26
1998
Homo sapiens, Mus musculus, Oryctolagus cuniculus, Rattus norvegicus
brenda
Luka, Z.; Cerone, R.; Phillips, J.A.; Mudd, S.H.; Wagner, C.
Mutations in human glycine N-methyltransferase give insights into its role in methionine metabolism
Hum. Genet.
110
68-74
2002
Homo sapiens
brenda
Rowling, M.J.; McMullen, M.H.; Schalinske, K.L.
Vitamin A and its derivatives induce hepatic glycine N-methyltransferase and hypomethylation of DNA in rats
J. Nutr.
132
365-369
2002
Rattus norvegicus
brenda
Rowling, M.J.; McMullen, M.H.; Chipman, D.C.; Schalinske, K.L.
Hepatic glycine N-methyltransferase is up-regulated by excess dietary methionine in rats
J. Nutr.
132
2545-2550
2002
Rattus norvegicus
brenda
Aida, K.; Tawata, M.; Negishi, M.; Onaya, T.
Mouse glycine N-methyltransferase is sexually dimorphic and regulated by growth hormone
Horm. Metab. Res.
29
646-649
1997
Mus musculus
brenda
Yeo, E.J.; Wagner, C.
Tissue distribution of glycine N-methyltransferase, a major folate-binding protein of liver
Proc. Natl. Acad. Sci. USA
91
210-214
1994
Rattus norvegicus
brenda
McMullen, M.H.; Rowling, M.J.; Ozias, M.K.; Schalinske, K.L.
Activation and induction of glycine N-methyltransferase by retinoids are tissue- and gender-specific
Arch. Biochem. Biophys.
401
73-80
2002
Rattus norvegicus
brenda
Luka, Z.; Wagner, C.
Human glycine N-methyltransferase is unfolded by urea through a compact monomer state
Arch. Biochem. Biophys.
420
153-160
2003
Homo sapiens
brenda
Luka, Z.; Wagner, C.
Effect of naturally occurring mutations in human glycine N-methyltransferase on activity and conformation
Biochem. Biophys. Res. Commun.
312
1067-1072
2003
Homo sapiens
brenda
Kloor, D.; Karnahl, K.; Kompf, J.
Characterization of glycine N-methyltransferase from rabbit liver
Biochem. Cell Biol.
82
369-374
2004
Oryctolagus cuniculus
brenda
Takata, Y.; Huang, Y.; Komoto, J.; Yamada, T.; Konishi, K.; Ogawa, H.; Gomi, T.; Fujioka, M.; Takusagawa, F.
Catalytic mechanism of glycine N-methyltransferase
Biochemistry
42
8394-8402
2003
Rattus norvegicus (P13255)
brenda
Chen, S.Y.; Lin, J.R.; Darbha, R.; Lin, P.; Liu, T.Y.; Chen, Y.M.
Glycine N-methyltransferase tumor susceptibility gene in the benzo(a)pyrene-detoxification pathway
Cancer Res.
64
3617-3623
2004
Homo sapiens
brenda
Rowling, M.J.; Schalinske, K.L.
Retinoic acid and glucocorticoid treatment induce hepatic glycine N-methyltransferase and lower plasma homocysteine concentrations in rats and rat hepatoma cells
J. Nutr.
133
3392-3398
2003
Rattus norvegicus
brenda
Ozias, M.K.; Schalinske, K.L.
All-trans-retinoic acid rapidly induces glycine N-methyltransferase in a dose-dependent manner and reduces circulating methionine and homocysteine levels in rats
J. Nutr.
133
4090-4094
2003
Rattus norvegicus
brenda
Luka, Z.; Wagner, C.
Expression and purification of glycine N-methyltransferases in Escherichia coli
Protein Expr. Purif.
28
280-286
2003
Mus musculus, Rattus norvegicus, Homo sapiens
brenda
Pakhomova, S.; Luka, Z.; Grohmann, S.; Wagner, C.; Newcomer, M.E.
Glycine N-methyltransferases: a comparison of the crystal structures and kinetic properties of recombinant human, mouse and rat enzymes
Proteins
57
331-337
2004
Mus musculus, Homo sapiens
brenda
Nieman, K.M.; Hartz, C.S.; Szegedi, S.S.; Garrow, T.A.; Sparks, J.D.; Schalinske, K.L.
Folate status modulates the induction of hepatic glycine N-methyltransferase and homocysteine metabolism in diabetic rats
Am. J. Physiol. Endocrinol. Metab.
291
E1235-E1242
2006
Rattus norvegicus
brenda
Huang, Y.C.; Lee, C.M.; Chen, M.; Chung, M.Y.; Chang, Y.H.; Huang, W.J.; Ho, D.M.; Pan, C.C.; Wu, T.T.; Yang, S.; Lin, M.W.; Hsieh, J.T.; Chen, Y.M.
Haplotypes, loss of heterozygosity, and expression levels of glycine N-methyltransferase in prostate cancer
Clin. Cancer Res.
13
1412-1420
2007
Homo sapiens
brenda
Luka, Z.; Pakhomova, S.; Loukachevitch, L.V.; Egli, M.; Newcomer, M.E.; Wagner, C.
5-methyltetrahydrofolate is bound in intersubunit areas of rat liver folate-binding protein glycine N-methyltransferase
J. Biol. Chem.
282
4069-4075
2007
Rattus norvegicus (P13255)
brenda
Beagle, B.; Yang, T.L.; Hung, J.; Cogger, E.A.; Moriarty, D.J.; Caudill, M.A.
The glycine N-methyltransferase (GNMT) 1289 C->T variant influences plasma total homocysteine concentrations in young women after restricting folate intake
J. Nutr.
135
2780-2785
2005
Homo sapiens
brenda
Luka, Z.; Ham, A.J.; Norris, J.L.; Yeo, E.J.; Yermalitsky, V.; Glenn, B.; Caprioli, R.M.; Liebler, D.C.; Wagner, C.
Identification of phosphorylation sites in glycine N-methyltransferase from rat liver
Protein Sci.
15
785-794
2006
Rattus norvegicus
brenda
Lee, C.M.; Chen, S.Y.; Lee, Y.C.; Huang, C.Y.; Chen, Y.M.
Benzo[a]pyrene and glycine N-methyltransferse interactions: gene expression profiles of the liver detoxification pathway
Toxicol. Appl. Pharmacol.
214
126-135
2006
Homo sapiens
brenda
Luka, Z.; Capdevila, A.; Mato, J.M.; Wagner, C.
A glycine N-methyltransferase knockout mouse model for humans with deficiency of this enzyme
Transgenic Res.
15
393-397
2006
Homo sapiens, Mus musculus (Q9QXF8), Mus musculus
brenda
Luka, Z.; Loukachevitch, L.V.; Wagner, C.
Acetylation of N-terminal valine of glycine N-methyltransferase affects enzyme inhibition by folate
Biochim. Biophys. Acta
1784
1342-1346
2008
Rattus norvegicus
brenda
Martinez-Chantar, M.L.; Vazquez-Chantada, M.; Ariz, U.; Martinez, N.; Varela, M.; Luka, Z.; Capdevila, A.; Rodriguez, J.; Aransay, A.M.; Matthiesen, R.; Yang, H.; Calvisi, D.F.; Esteller, M.; Fraga, M.; Lu, S.C.; Wagner, C.; Mato, J.M.
Loss of the glycine N-methyltransferase gene leads to steatosis and hepatocellular carcinoma in mice
Hepatology
47
1191-1199
2008
Mus musculus
brenda
Liu, S.; Li, Y.; Chen, Y.; Chiang, E.; Li, A.F.; Lee, Y.; Tsai, T.; Hsiao, M.; Huang, S.; Chen, Y.A.
Glycine N-methyltransferase -/- mice develop chronic hepatitis and glycogen storage disease in the liver
Hepatology
47
768-769
2008
Mus musculus
-
brenda
Huang, Y.C.; Chen, M.; Shyr, Y.M.; Su, C.H.; Chen, C.K.; Li, A.F.; Ho, D.M.; Chen, Y.M.
Glycine N-methyltransferase is a favorable prognostic marker for human cholangiocarcinoma
J. Gastroenterol. Hepatol.
23
1384-1389
2008
Homo sapiens
brenda
Luka, Z.; Pakhomova, S.; Luka, Y.; Newcomer, M.E.; Wagner, C.
Destabilization of human glycine N-methyltransferase by H176N mutation
Protein Sci.
16
1957-1964
2007
Homo sapiens (Q14749), Homo sapiens
brenda
Fang, X.; Dong, W.; Thornton, C.; Scheffler, B.; Willett, K.L.
Benzo(a)pyrene induced glycine N-methyltransferase messenger RNA expression in Fundulus heteroclitus embryos
Mar. Environ. Res.
69S1
S74-S76
2010
Fundulus heteroclitus (D3GAN3), Fundulus heteroclitus
brenda
Lee, C.M.; Shih, Y.P.; Wu, C.H.; Chen, Y.M.
Characterization of the 5 regulatory region of the human glycine N-methyltransferase gene
Gene
443
151-157
2009
Homo sapiens
brenda
Liao, Y.J.; Liu, S.P.; Lee, C.M.; Yen, C.H.; Chuang, P.C.; Chen, C.Y.; Tsai, T.F.; Huang, S.F.; Lee, Y.H.; Chen, Y.M.
Characterization of a glycine N-methyltransferase gene knockout mouse model for hepatocellular carcinoma: Implications of the gender disparity in liver cancer susceptibility
Int. J. Cancer
124
816-826
2009
Mus musculus
brenda
Luka, Z.; Mudd, S.H.; Wagner, C.
Glycine N-methyltransferase and regulation of S-adenosylmethionine levels
J. Biol. Chem.
284
22507-22511
2009
Sus scrofa, Rattus norvegicus (P13255), Oryctolagus cuniculus, Homo sapiens, Mus musculus, Danio rerio
brenda
Yen, C.H.; Hung, J.H.; Ueng, Y.F.; Liu, S.P.; Chen, S.Y.; Liu, H.H.; Chou, T.Y.; Tsai, T.F.; Darbha, R.; Hsieh, L.L.; Chen, Y.M.
Glycine N-methyltransferase affects the metabolism of aflatoxin B1 and blocks its carcinogenic effect
Toxicol. Appl. Pharmacol.
235
296-304
2009
Homo sapiens
brenda
Luka, Z.
Methyltetrahydrofolate in folate-binding protein glycine N-methyltransferase
Vitam. Horm.
79
325-345
2008
Rattus norvegicus, Oryctolagus cuniculus, Homo sapiens, Mus musculus (Q9QXF8), Mus musculus, Sus scrofa (Q29555)
brenda
Wang, Y.C.; Tang, F.Y.; Chen, S.Y.; Chen, Y.M.; Chiang, E.P.
Glycine-N methyltransferase expression in HepG2 cells is involved in methyl group homeostasis by regulating transmethylation kinetics and DNA methylation
J. Nutr.
141
777-782
2011
Homo sapiens
brenda
Song, Y.H.; Shiota, M.; Kuroiwa, K.; Naito, S.; Oda, Y.
The important role of glycine N-methyltransferase in the carcinogenesis and progression of prostate cancer
Mod. Pathol.
24
1272-1280
2011
Homo sapiens
brenda
Yen, C.H.; Lu, Y.C.; Li, C.H.; Lee, C.M.; Chen, C.Y.; Cheng, M.Y.; Huang, S.F.; Chen, K.F.; Cheng, A.L.; Liao, L.Y.; Lee, Y.H.; Chen, Y.M.
Functional characterization of glycine N-methyltransferase and its interactive protein DEPDC6/DEPTOR in hepatocellular carcinoma
Mol. Med.
18
286-296
2012
Homo sapiens
brenda
Luka, Z.; Pakhomova, S.; Loukachevitch, L.; Newcomer, M.; Wagner, C.
Differences in folate-protein interactions result in differing inhibition of native rat liver and recombinant glycine N-methyltransferase by 5-methyltetrahydrofolate
Biochim. Biophys. Acta
1824
286-291
2012
Rattus norvegicus (P13255)
brenda
Chou, W.Y.; Zhao, J.F.; Chen, Y.M.; Lee, K.I.; Su, K.H.; Shyue, S.K.; Lee, T.S.
Role of glycine N-methyltransferase in experimental ulcerative colitis
J. Gastroenterol. Hepatol.
29
494-501
2014
Mus musculus
brenda
Ottaviani, S.; Brooke, G.N.; OHanlon-Brown, C.; Waxman, J.; Ali, S.; Buluwela, L.
Characterisation of the androgen regulation of glycine N-methyltransferase in prostate cancer cells
J. Mol. Endocrinol.
51
301-312
2013
Homo sapiens
brenda
Li, C.H.; Lin, M.H.; Chu, S.H.; Tu, P.H.; Fang, C.C.; Yen, C.H.; Liang, P.I.; Huang, J.C.; Su, Y.C.; Sytwu, H.K.; Chen, Y.M.
Role of glycine N-methyltransferase in the regulation of T-cell responses in experimental autoimmune encephalomyelitis
Mol. Med.
20
684-696
2014
Mus musculus (Q9QXF8)
brenda
DebRoy, S.; Kramarenko, I.I.; Ghose, S.; Oleinik, N.V.; Krupenko, S.A.; Krupenko, N.I.
A novel tumor suppressor function of glycine N-methyltransferase is independent of its catalytic activity but requires nuclear localization
PLoS ONE
8
e70062
2013
Homo sapiens
brenda
Tain, L.S.; Jain, C.; Nespital, T.; Froehlich, J.; Hinze, Y.; Groenke, S.; Partridge, L.
Longevity in response to lowered insulin signaling requires glycine N-methyltransferase-dependent spermidine production
Aging Cell
19
e13043
2019
Drosophila melanogaster (Q9VG42), Mus musculus (Q9QXF8)
brenda
Zhang, J.; Klinman, J.P.
Convergent mechanistic features between the structurally diverse N- and O-methyltransferases glycine N-methyltransferase and catechol O-methyltransferase
J. Am. Chem. Soc.
138
9158-9165
2016
Rattus norvegicus (P13255)
brenda
Swiderek, K.; Tunon, I.; Williams,I. H.; Moliner, V.
Insights on the origin of catalysis on glycine N-methyltransferase from computational modeling
J. Am. Chem. Soc.
140
4327-4334
2018
Rattus norvegicus (P13255)
brenda
Wang, Y.; Wu, M.; Lin, Y.; Tang, F.; Ko, H.; Chiang, E.
Regulation of folate-mediated one-carbon metabolism by glycine N-methyltransferase (GNMT) and methylenetetrahydrofolate reductase (MTHFR)
J. Nutr. Sci. Vitaminol.
61
S148-S150
2015
Mus musculus (Q9QXF8)
brenda
Liu, M.; Liu, H.; Mei, F.; Yang, N.; Zhao, D.; Ai, G.; Xiang, H.; Zheng, Y.
Identification of the biosynthetic pathway of glycine betaine that is responsible for salinity tolerance in halophilic Thioalkalivibrio versutus D301
Front. Microbiol.
13
875843
2022
Thioalkalivibrio versutus (A0A0G3G560), Thioalkalivibrio versutus D301 (A0A0G3G560)
brenda
Kuo, K.L.; Chiang, C.W.; Chen, Y.A.; Yu, C.C.; Lee, T.S.
Folic acid ameliorates renal injury in experimental obstructive nephropathy role of glycine N-methyltransferase
Int. J. Mol. Sci.
24
6859
2023
Homo sapiens (Q14749), Mus musculus (Q9QXF8)
brenda
Cheng, Q.; DeYonker, N.J.
The glycine N-methyltransferase case study Another challenge for QM-cluster models?
J. Phys. Chem. B
127
9282-9294
2023
Rattus norvegicus (P13255)
brenda
Zabala-Letona, A.; Arruabarrena-Aristorena, A.; Fernandez-Ruiz, S.; Viera, C.; Carlevaris, O.; Ercilla, A.; Mendizabal, I.; Martin, T.; Macchia, A.; Camacho, L.; Pujana-Vaquerizo, M.; Sanchez-Mosquera, P.; Torrano, V.; Martin-Martin, N.; Zuniga-Garcia, P.; Castillo-Martin, M.; Ugalde-Olano, A.; Loizaga-Iriarte, A.; Unda, M.; Mato, J.M.; Berra, E.
PI3K-regulated glycine N-methyltransferase is required for the development of prostate cancer
Oncogenesis
11
10
2022
Homo sapiens (Q14749), Mus musculus (Q9QXF8)
brenda
Zhang, W.; Guo, X.; Ren, J.; Chen, Y.; Wang, J.; Gao, A.
Glycine/glycine N-methyltransferase/sarcosine axis mediates benzene-induced hematotoxicity
Toxicol. Appl. Pharmacol.
428
115682
2021
Homo sapiens (Q14749)
brenda
Simile, M.M.; Cigliano, A.; Paliogiannis, P.; Daino, L.; Manetti, R.; Feo, C.F.; Calvisi, D.F.; Feo, F.; Pascale, R.M.
Nuclear localization dictates hepatocarcinogenesis suppression by glycine N-methyltransferase
Transl. Oncol.
15
101239
2022
Homo sapiens (Q14749), Rattus norvegicus (P13255)
brenda
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