Any feedback?
Information on EC 2.1.1.20 - glycine N-methyltransferase and Organism(s) Homo sapiens
for references in articles please use BRENDA:EC2.1.1.20Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
2.1.1.20 glycine N-methyltransferaseIUBMB 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.
Specify your search results
Word Map
- 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
The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
gnmt, glycine n-methyltransferase, glycine methyltransferase, s-adenosyl-l-methionine:glycine n-methyltransferase, glycine-n methyltransferase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
glycine methyltransferase
GNMT
methyltransferase, glycine
-
-
-
-
S-adenosyl-L-methionine:glycine methyltransferase
-
-
-
-
glycine methyltransferase
-
-
-
-
GNMT
-
-
-
-
GNMT
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
S-adenosyl-L-methionine + glycine = S-adenosyl-L-homocysteine + sarcosine
overview mechanism
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
methyl group transfer
-
-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
-
-, -
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.
CAS REGISTRY NUMBER
COMMENTARY
37228-72-1
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
S-adenosyl-L-methionine + glycine
S-adenosyl-L-homocysteine + N-methylglycine
-
-
-
-
?
S-adenosyl-L-methionine + glycine
S-adenosyl-L-homocysteine + N-methylglycine
-
N-methylglycine = sarcosine
-
?
S-adenosyl-L-methionine + glycine
S-adenosyl-L-homocysteine + N-methylglycine
-
key regulatory enzyme for methyl group metabolism by regulating the S-adenosyl-L-methionine/S-adenosyl-L-homocysteine ratio
-
-
?
S-adenosyl-L-methionine + glycine
S-adenosyl-L-homocysteine + N-methylglycine
-
key enzyme for the regulation of the ratio of S-adenosylmethionine to S-adenosylhomocysteine
N-methylglycine = sarcosine
-
?
S-adenosyl-L-methionine + glycine
S-adenosyl-L-homocysteine + N-methylglycine
key enzyme for the regulation of the ratio of S-adenosylmethionine to S-adenosylhomocysteine
N-methylglycine = sarcosine
-
?
S-adenosyl-L-methionine + glycine
S-adenosyl-L-homocysteine + N-methylglycine
-
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
N-methylglycine = sarcosine
-
?
S-adenosyl-L-methionine + glycine
S-adenosyl-L-homocysteine + sarcosine
-
-
-
-
?
S-adenosyl-L-methionine + glycine
S-adenosyl-L-homocysteine + sarcosine
-
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
-
-
?
additional information
?
-
-
interaction of benzo(a)pyrene with the enzyme may contribute to carcinogenesis
-
-
?
additional information
?
-
-
major folate binding protein, interacts with environmental carcinogens such as benzo(a)pyrene
-
-
?
additional information
?
-
-
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
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
S-adenosyl-L-methionine + glycine
S-adenosyl-L-homocysteine + N-methylglycine
-
key regulatory enzyme for methyl group metabolism by regulating the S-adenosyl-L-methionine/S-adenosyl-L-homocysteine ratio
-
-
?
S-adenosyl-L-methionine + glycine
S-adenosyl-L-homocysteine + N-methylglycine
-
key enzyme for the regulation of the ratio of S-adenosylmethionine to S-adenosylhomocysteine
N-methylglycine = sarcosine
-
?
S-adenosyl-L-methionine + glycine
S-adenosyl-L-homocysteine + N-methylglycine
key enzyme for the regulation of the ratio of S-adenosylmethionine to S-adenosylhomocysteine
N-methylglycine = sarcosine
-
?
S-adenosyl-L-methionine + glycine
S-adenosyl-L-homocysteine + N-methylglycine
-
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
N-methylglycine = sarcosine
-
?
additional information
?
-
-
interaction of benzo(a)pyrene with the enzyme may contribute to carcinogenesis
-
-
?
additional information
?
-
-
major folate binding protein, interacts with environmental carcinogens such as benzo(a)pyrene
-
-
?
additional information
?
-
-
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
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
5-Methyltetrahydrofolate pentaglutamate
-
noncompetitive inhibitor with respect to substrates S-adenosyl-L-methionine and glycine
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
485226, 485227, 657755, 658385, 660421, 660475, 673122, 677194, 703849, 704524, 706826, 706903, 720299, 720403, 720481, 734506, 735096
-
-
normal enzyme and naturally occurring H176N mutation which is found in humans with hypermethioninaemia
UniProt
three cases of GNMT mutations known, all suffering from mild liver disease and display elevated methionine levels
-
-
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
high expression in normal tissue, reduced expression in tumorous tissue, some tumor samples show no enzyme expression
-
36.4% of tissues show loss of heterozygosity of the GNMT gene, GNMT expression diminished in 82.2% of tissues
additional information
-
high expression in normal tissue, only 4% of hepatocellular carcinoma show GNMT expression
-
high GNMT-expression in normal prostatic and benign prostatic hyperplasia tissues, whereas it was diminished in 82% of the prostate cancer tissues
additional information
-
abundant GNMT expression in benign prostatic hyperplasia tissue
additional information
-
no GNMT activity is detected in fetal liver, Novikoff hepatoma cells, Morris hepatoma cells, and Ehrlich ascites cells
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
GNMT is expressed in cytoplasm before treatment with benzo(a)pyrene and translocated to cell nuclei after treatment with benzo(a)pyrene
-
concentrated in the paranuclear region near the bile duct lumen
-
GNMT is expressed in cytoplasm before treatment with benzo(a)pyrene and translocated to cell nuclei after treatment with benzo(a)pyrene
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
-
GNMT is involved in both hepatic methyl group and one-carbon metabolism
physiological function
malfunction
-
overexpression of GNMT causes activation of mTOR/raptor downstream signaling and delays G2/M cell cycle progression, which altogether results in cellular senescence
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
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
-
GNMT plays a major role in maintaining normal S-adenosyl-L-methionine levels
physiological function
-
GNMT regulates hepatocellular growth in part through interacting with DEPDC6/DEPTOR and modulating mTOR/raptor signaling pathway
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
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). GNMT_HUMAN
295
0
32742
Swiss-Prot
other Location (Reliability: 2)
V9HW60_HUMAN
295
0
32742
TrEMBL
other Location (Reliability: 2)
A0A0S2Z594_HUMAN
151
0
16916
TrEMBL
other Location (Reliability: 2)
A0A0S2Z5F2_HUMAN
276
0
30664
TrEMBL
other Location (Reliability: 2)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
130000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
tetramer
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
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phosphoprotein
-
GNMT is phosphorylated by cAMP-dependent protein kinase at Ser9, Ser71, Ser139, Ser182, and Ser241
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
wild type and H176N mutant enzyme as cocrystals with a citrate molecule bound in the active site
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
additional information
-
patients with mutations Leu49Pro and His176Asn suffer from mild liver disease
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
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
-
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
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
full-length human GNMT is used as the bait in a yeast two-hybrid screen system with a human kidney cDNA library
-
PC-3 cells, LNCaP cells, HA22T/VGH cells and HEK-293A cells transfected with plasmid containing haplotype C
-
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
-
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
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
diagnostics
medicine
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
-
patients with mutations Leu49Pro and His176Asn suffer from mild liver disease
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
-
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
-
glycine N-methyltransferase is a tumor susceptibility gene for both hepatocellular carcinoma and prostate cancer
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
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
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
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
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
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
Luka, Z.; Wagner, C.
Expression and purification of glycine N-methyltransferases in Escherichia coli
Protein Expr. Purif.
28
280-286
2003
Homo sapiens, Mus musculus, Rattus norvegicus
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
Homo sapiens, Mus musculus
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
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
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
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
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
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
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
Luka, Z.; Mudd, S.H.; Wagner, C.
Glycine N-methyltransferase and regulation of S-adenosylmethionine levels
J. Biol. Chem.
284
22507-22511
2009
Danio rerio, Oryctolagus cuniculus, Homo sapiens, Mus musculus, Sus scrofa, Rattus norvegicus (P13255)
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
Luka, Z.
Methyltetrahydrofolate in folate-binding protein glycine N-methyltransferase
Vitam. Horm.
79
325-345
2008
Oryctolagus cuniculus, Homo sapiens, Rattus norvegicus, Sus scrofa (Q29555), Mus musculus (Q9QXF8), Mus musculus
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
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
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
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
EXTERNAL LINKS (specific for EC-Number 2.1.1.20)
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
