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
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adenosyltransferase
- cystathionine
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transmethylation
- adomet
-
betaine-homocysteine
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remethylation
- beta-synthase
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one-carbon
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transsulfuration
- 5-methyltetrahydrofolate
- medicine
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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
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General Information
General Information on EC 2.1.1.20 - glycine N-methyltransferase
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malfunction
metabolism
physiological function
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Gnmt knockout mice develop fatty livers when they have increased S-adenosyl-L-methionine
malfunction
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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
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overexpression of GNMT causes activation of mTOR/raptor downstream signaling and delays G2/M cell cycle progression, which altogether results in cellular senescence
malfunction
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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
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GNMT is involved in both hepatic methyl group and one-carbon metabolism
metabolism
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GNMT is involved in both hepatic methyl group and one-carbon metabolism
metabolism
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GNMT is involved in both hepatic methyl group and one-carbon metabolism
metabolism
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GNMT is involved in both hepatic methyl group and one-carbon metabolism
metabolism
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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
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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
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GNMT plays a major role in maintaining normal S-adenosyl-L-methionine levels
physiological function
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GNMT plays a major role in maintaining normal S-adenosyl-L-methionine levels
physiological function
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GNMT plays a major role in maintaining normal S-adenosyl-L-methionine levels
physiological function
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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
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GNMT regulates hepatocellular growth in part through interacting with DEPDC6/DEPTOR and modulating mTOR/raptor signaling pathway
physiological function
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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
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
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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
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
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
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