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S-adenosyl-L-methionine + guanidinoacetate
S-adenosyl-L-homocysteine + creatine
S-adenosyl-L-methionine + guanidinoacetic acid + glutathione
?
-
assay at pH 7.4, 37°C, 1 h, reaction stopped with 5% trichloroacetic acid
-
-
?
additional information
?
-
S-adenosyl-L-methionine + guanidinoacetate
S-adenosyl-L-homocysteine + creatine
-
-
-
-
?
S-adenosyl-L-methionine + guanidinoacetate
S-adenosyl-L-homocysteine + creatine
-
S-adenosyl-L-methionine is the only possible methyl donor
-
?
S-adenosyl-L-methionine + guanidinoacetate
S-adenosyl-L-homocysteine + creatine
-
biosynthesis of creatine
-
?
S-adenosyl-L-methionine + guanidinoacetate
S-adenosyl-L-homocysteine + creatine
-
-
-
?
S-adenosyl-L-methionine + guanidinoacetate
S-adenosyl-L-homocysteine + creatine
-
S-adenosyl-L-methionine is the only possible methyl donor
-
?
S-adenosyl-L-methionine + guanidinoacetate
S-adenosyl-L-homocysteine + creatine
-
biosynthesis of creatine
-
?
S-adenosyl-L-methionine + guanidinoacetate
S-adenosyl-L-homocysteine + creatine
-
-
-
-
?
S-adenosyl-L-methionine + guanidinoacetate
S-adenosyl-L-homocysteine + creatine
-
-
-
?
S-adenosyl-L-methionine + guanidinoacetate
S-adenosyl-L-homocysteine + creatine
-
-
-
-
?
S-adenosyl-L-methionine + guanidinoacetate
S-adenosyl-L-homocysteine + creatine
-
S-adenosyl-L-methionine is the only possible methyl donor
-
?
S-adenosyl-L-methionine + guanidinoacetate
S-adenosyl-L-homocysteine + creatine
-
biosynthesis of creatine
-
?
S-adenosyl-L-methionine + guanidinoacetate
S-adenosyl-L-homocysteine + creatine
-
-
-
?
S-adenosyl-L-methionine + guanidinoacetate
S-adenosyl-L-homocysteine + creatine
-
-
-
?
S-adenosyl-L-methionine + guanidinoacetate
S-adenosyl-L-homocysteine + creatine
-
-
-
?
S-adenosyl-L-methionine + guanidinoacetate
S-adenosyl-L-homocysteine + creatine
-
-
-
?
S-adenosyl-L-methionine + guanidinoacetate
S-adenosyl-L-homocysteine + creatine
-
-
-
?
S-adenosyl-L-methionine + guanidinoacetate
S-adenosyl-L-homocysteine + creatine
-
-
-
?
S-adenosyl-L-methionine + guanidinoacetate
S-adenosyl-L-homocysteine + creatine
-
-
-
?
S-adenosyl-L-methionine + guanidinoacetate
S-adenosyl-L-homocysteine + creatine
-
-
-
-
?
S-adenosyl-L-methionine + guanidinoacetate
S-adenosyl-L-homocysteine + creatine
-
-
?
S-adenosyl-L-methionine + guanidinoacetate
S-adenosyl-L-homocysteine + creatine
-
-
?
S-adenosyl-L-methionine + guanidinoacetate
S-adenosyl-L-homocysteine + creatine
-
-
-
?
S-adenosyl-L-methionine + guanidinoacetate
S-adenosyl-L-homocysteine + creatine
-
-
-
?
S-adenosyl-L-methionine + guanidinoacetate
S-adenosyl-L-homocysteine + creatine
-
-
-
?
S-adenosyl-L-methionine + guanidinoacetate
S-adenosyl-L-homocysteine + creatine
-
-
-
-
ir
S-adenosyl-L-methionine + guanidinoacetate
S-adenosyl-L-homocysteine + creatine
-
S-adenosyl-L-methionine is the only possible methyl donor
-
?
S-adenosyl-L-methionine + guanidinoacetate
S-adenosyl-L-homocysteine + creatine
-
biosynthesis of creatine
-
?
additional information
?
-
-
since the L197P mutation in the exon 6 of the guanidinoacetate N-methyltransferase gene leaves the isoform B of the enzyme unaffected, the occurrence of biochemical alterations and disease in this subject testifies against the possibility that isoform B has guanidinoacetate N-methyltransferase activity
-
-
?
additional information
?
-
-
together with creatine/phosphocreatine shuttle system involved in brain energy homeostasis through a neuron-glial relationship
-
-
?
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weak GAMT expression is detected in the epithelium of alimentary tract
brenda
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highest enzyme level
brenda
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-
brenda
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-
brenda
-
brenda
-
brenda
-
brenda
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in embryos at 12.5 days of gestation guanidinoacetate N-methyltransferase is detectable in the hepatic primordium only, with all other tissues being negative. Non-radioactive in situ hybridization (58°C for 40 h in 5 x SSC, 50% formamide and 40 microg/ml salmon sperm DNA) with digoxigenin-labeled antisense and sense riboprobes (400 ng/ml) for rat guanidinoacetate N-methyltransferase. guanidinoacetate N-methyltransferase proteins are detected with rabbit polyclonal antibodies
brenda
-
-
brenda
in embryos at 18.5 days of gestation guanidinoacetate N-methyltransferase is detectable. Non-radioactive in situ hybridization (58°C for 40 h in 5 x SSC, 50% formamide and 40 microg/ml salmon sperm DNA) with digoxigenin-labeled antisense and sense riboprobes (400 ng/ml) for rat guanidinoacetate N-methyltransferase. guanidinoacetate N-methyltransferase proteins are detected with rabbit polyclonal antibodies
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low activity
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-
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-
-
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-
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GAMT is strongly expressed in all neurons and glia cells of neural cord
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low enzyme level
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GAMT is highly expressed in perivascular pericytes and smooth muscle cells after birth
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S180 cells
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GAMT was highly expressed in perivascular pericytes and smooth muscle cells after birth
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-
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mainly found in Sertoli cells of seminiferous tubules
brenda
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-
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L197P mutation in exon 6: guanidinoacetate increases to 2566 microMol/l, creatine decreases to 3.7 microMol/l
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low enzyme level
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-
-
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-
-
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moderate expression levels throughout development
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-
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-
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-
-
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L197P mutation in exon 6: guanidinoacetate increases to 33.6 microMol/l, creatine decreases to 24 microMol/l
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-
-
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-
-
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expressed within the brain, both during development and in adulthood
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-
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high expression in oligodendrocytes and olfactory ensheathing glia, moderate expression in astrocytes, low expression in neurons and microglia
brenda
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expressed within the brain, both during development and in adulthood
brenda
two waves of high GAMT expression. The first involves high expression in mitotic cells in the ventricular zone of the brain wall and the external granular layer of the cerebellum at the embryonic and neonatal stages. The second is initiated by striking up-regulation of GAMT in oligodendrocytes during the second and third postnatal weeks and continues to adulthood
brenda
all parts of brain, neurons and glia, very low levels in astrocytes
brenda
in embryos at 15.5 days of gestation guanidinoacetate N-methyltransferase is detectable in pons and striatum. In embryos at 18.5 days of gestation guanidinoacetate N-methyltransferase is detectable in neocortex, hippocampus, striatum, pallidum and spinal cord. Non-radioactive in situ hybridization (58°C for 40 h in 5 x SSC, 50% formamide and 40 microg/ml salmon sperm DNA) with digoxigenin-labeled antisense and sense riboprobes (400 ng/ml) for rat guanidinoacetate N-methyltransferase. guanidinoacetate N-methyltransferase proteins are detected with rabbit polyclonal antibodies
brenda
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-
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low activity
brenda
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-
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-
brenda
-
-
brenda
-
-
brenda
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-
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primary
brenda
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-
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low enzyme level
brenda
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-
brenda
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low enzyme level
brenda
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-
brenda
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low activity
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-
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-
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-
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-
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higher levels in female than in male
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-
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in embryos at 15.5 and 18.5 days of gestation guanidinoacetate N-methyltransferase is detectable in liver. Non-radioactive in situ hybridization (58°C for 40 h in 5 x SSC, 50% formamide and 40 microg/ml salmon sperm DNA) with digoxigenin-labeled antisense and sense riboprobes (400 ng/ml) for rat guanidinoacetate N-methyltransferase. guanidinoacetate N-methyltransferase proteins are detected with rabbit polyclonal antibodies
brenda
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highly active in the liver
brenda
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-
brenda
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high activity
brenda
-
-
brenda
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L197P mutation in exon 6, reduces the activity of guanidinoacetate N-methyltransferase
brenda
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low enzyme level
brenda
-
-
brenda
-
low activity
brenda
-
-
brenda
-
-
brenda
GAMT levels are low to moderate in neuroblasts residing in the ventricular zone, increase during the second postnatal week, and decrease to very low levels thereafter
brenda
-
-
brenda
-
-
brenda
striking up-regulation of GAMT in oligodendrocytes during the second and third postnatal weeks, expression continues to adulthood
brenda
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-
brenda
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-
brenda
in embryos at 15.5 and 18.5 days of gestation guanidinoacetate N-methyltransferase is detectable in pancreas. Non-radioactive in situ hybridization (58°C for 40 h in 5 x SSC, 50% formamide and 40 microg/ml salmon sperm DNA) with digoxigenin-labeled antisense and sense riboprobes (400 ng/ml) for rat guanidinoacetate N-methyltransferase. guanidinoacetate N-methyltransferase proteins are detected with rabbit polyclonal antibodies
brenda
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-
brenda
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the piglet pancreatic GAMT activity is only 1% of that found in the liver
brenda
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-
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hind leg muscle
brenda
in embryos at 18.5 days of gestation guanidinoacetate N-methyltransferase is detectable. Non-radioactive in situ hybridization (58°C for 40 h in 5 x SSC, 50% formamide and 40 microg/ml salmon sperm DNA) with digoxigenin-labeled antisense and sense riboprobes (400 ng/ml) for rat guanidinoacetate N-methyltransferase. guanidinoacetate N-methyltransferase proteins are detected with rabbit polyclonal antibodies
brenda
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-
brenda
additional information
-
not expressed in microcapillary endothelial cells
brenda
additional information
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absent in brain, small intestine, seminal vesicle, lung, vas deferens, cauda epididymis, coagulating gland and spleen
brenda
additional information
-
not expressed in microcapillary endothelial cells
brenda
additional information
guanidinoacetate N-methyltransferase can not be detected in kidney of embryos of 12.5, 15.5 and 18.5 days of gestation. Non-radioactive in situ hybridization (58°C for 40 h in 5 x SSC, 50% formamide and 40 microg/ml salmon sperm DNA) with digoxigenin-labeled antisense and sense riboprobes (400 ng/ml) for rat guanidinoacetate N-methyltransferase. guanidinoacetate N-methyltransferase proteins are detected with rabbit polyclonal antibodies
brenda
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A54P
naturally occuring mutation from enzyme deficiency patients, no recombinant expression of the mutant achieved, inactive mutant
A74P
naturally occuring mutation from enzyme deficiency patients, no recombinant expression of the mutant achieved, inactive mutant
C169Y
naturally occuring mutation from enzyme deficiency patients, no recombinant expression of the mutant achieved
D135N
naturally occuring mutation from enzyme deficiency patients, inactive mutant
G68C
naturally occuring mutation from enzyme deficiency patients, no recombinant expression of the mutant achieved
H147Y
naturally occuring mutation from enzyme deficiency patients, almost inactive mutant
H51P
naturally occuring mutation from enzyme deficiency patients, no recombinant expression of the mutant achieved
L166P
naturally occuring mutation from enzyme deficiency patients, inactive mutant
N92D
naturally occuring mutation from enzyme deficiency patients, inactive mutant
P8T
naturally occuring mutation from enzyme deficiency patients, the mutant shows similar activity as the wild-type enzyme
R208P
naturally occuring mutation from enzyme deficiency patients, almost inactive mutant
T136M
naturally occuring mutation from enzyme deficiency patients, inactive mutant
W45R
naturally occuring mutation from enzyme deficiency patients, inactive mutant
Y27H
naturally occuring mutation from enzyme deficiency patients, the mutant shows similar activity as the wild-type enzyme
D134E
lower activity than wild type enzyme
D134N
much lower activity than wild type enzyme
D92N
-
lower activity than wild type enzyme
E45D
decrease in kcat-value, increase in Km-value of S-adenosyl-L-methionine
E45Q
decrease in kcat-value, increase in Km-value of S-adenosyl-L-methionine
E45S
no residual activity
E89Q
-
lower activity than wild type enzyme
T135A
lower activity than wild type enzyme
W143F
-
lower activity than wild type enzyme
W143L
-
lower activity than wild type enzyme
Y133F
lower activity than wild type enzyme
Y133V
-
lower activity than wild type enzyme
Y221F
decrease in kcat-value
L197P
-
the sequencing of the guanidinoacetate N-methyltransferase gene reveals a homozygous missense mutation on exon 6, resulting in the substitution of leucine in position 197 with proline. The 13-year old girl has mental retardation, as main symptom, associated with a typical pattern of biochemical and neurochemical alterations.
L197P
naturally occuring mutation from enzyme deficiency patients, no recombinant expression of the mutant achieved, inactive mutant
Y136F
-
higher turnover than wild type enzyme
Y136F
higher turnover than wild type enzyme
Y136F
-
retains considerable activity, structural changes compared to wild-type
Y136V
-
lower activity than wild type enzyme
Y136V
-
loss of activity, structural changes compared to wild-type
additional information
-
finding of a novel homozygous missense mutation in exon 5, p.Leu166Pro, c.497T>C
additional information
-
mutation analysis of the guanidinoacetate methyltransferase gene is performed, the patient is found to be compound heterozygous for a known mitation in exon 2, c.327G>A, and for a novel mutation in exon 1, c170C>A
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Cantoni, G.L.; Vignos, P.J.
Enzymatic mechanism of creatine synthesis
J. Biol. Chem.
209
647-659
1954
Bos taurus, Cavia porcellus, Oryctolagus cuniculus, Sus scrofa
brenda
Im, Y.S.; Chiang, P.K.; Cantoni, G.L.
Guanidoacetate methyltransferase. Purification and molecular properties
J. Biol. Chem.
254
11047-11050
1979
Sus scrofa
brenda
Im, Y.S.; Cantoni, G.L.; Chiang, P.K.
A radioactive assay for guanidoacetate methyltransferase
Anal. Biochem.
95
87-88
1979
Sus scrofa
brenda
Ogawa, H.; Ishiguro, Y.; Fujioka, M.
Guanidoacetate methyltransferase from rat liver: purification, properties, and evidence for the involvement of sulfhydryl groups for activity
Arch. Biochem. Biophys.
226
265-275
1983
Rattus norvegicus
brenda
Ogawa, H.; Date, T.; Gomi, T.; Konishi, K.; Pitot, H.C.; Cantoni, G.L.; Fujioka, M.
Molecular cloning, sequence analysis, and expression in Escherichia coli of the cDNA for guanidinoacetate methyltransferase from rat liver
Proc. Natl. Acad. Sci. USA
85
694-698
1988
Rattus norvegicus
brenda
Fujioka, M.; Konishi, K.; Takata, Y.
Recombinant rat liver guanidinoacetate methyltransferase: reactivity and function of sulfhydryl groups
Biochemistry
27
7658-7664
1988
Rattus norvegicus
brenda
Konishi, K.; Fujioka, M.
Reversible inactivation of recombinant rat liver guanidinoacetate methyltransferase by glutathione disulfide
Arch. Biochem. Biophys.
289
90-96
1991
Rattus norvegicus
brenda
Takata, Y.; Fujioka, M.
Identification of a tyrosine residue in rat guanidinoacetate methyltransferase that is photolabeled with S-adenosyl-L-methionine
Biochemistry
31
4369-4374
1992
Rattus norvegicus
brenda
Lee, H.; Ogawa, H.; Fujioka, M.; Gerton, G.L.
Guanidinoacetate methyltransferase in the mouse: extensive expression in Sertoli cells of testis and in microvilli of caput epididymis
Biol. Reprod.
50
152-162
1994
Mus musculus
brenda
Takata, Y.; Konishi, K.; Gomi, T.; Fujioka, M.
Rat guanidinoacetate methyltransferase. Effect of site-directed alteration of an aspartic acid residue that is conserved across most mammalian S-adenosylmethionine-dependent methyltransferases
J. Biol. Chem.
269
5537-5542
1994
Rattus norvegicus (P10868)
brenda
Hamahata, A.; Takata, Y.; Gomi, T.; Fujioka, M.
Probing the S-adenosylmethionine-binding site of rat guanidinoacetate methyltransferase: effect of site-directed mutagenesis of residues that are conserved across mammalian non-nucleic acid methyltransferases
Biochem. J.
317
141-145
1996
Rattus norvegicus
-
brenda
Braissant, O.; Henry, H.; Loup, M.; Eilers, B.; Bachmann, C.
Endogenous synthesis and transport of creatine in the rat brain: an in situ hybridization study
Mol. Brain Res.
86
193-201
2001
Rattus norvegicus (P10868)
brenda
Komoto, J.; Huang, Y.; Takata, Y.; Yamada, T.; Konishi, K.; Ogawa, H.; Gomi, T.; Fujioka, M.; Takusagawa, F.
Crystal structure of guanidinoacetate methyltransferase from rat liver: A model structure of protein arginine methyltransferase
J. Mol. Biol.
320
223-235
2002
Rattus norvegicus
brenda
Komoto, J.; Takata, Y.; Yamada, T.; Konishi, K.; Ogawa, H.; Gomi, T.; Fujioka, M.; Takusagawa, F.
Monoclinic guanidinoacetate methyltransferase and gadolinium ion-binding characteristics
Acta Crystallogr. Sect. D
59
1589-1596
2003
Rattus norvegicus
brenda
Grazia Alessandri, M.; Celati, L.; Battini, R.; Baldinotti, F.; Item, C.; Leuzzi, V.; Cioni, G.
HPLC assay for guanidinoacetate methyltransferase
Anal. Biochem.
331
189-191
2004
Homo sapiens
brenda
Komoto, J.; Yamada, T.; Takata, Y.; Konishi, K.; Ogawa, H.; Gomi, T.; Fujioka, M.; Takusagawa, F.
Catalytic mechanism of guanidinoacetate methyltransferase: crystal structures of guanidinoacetate methyltransferase ternary complexes
Biochemistry
43
14385-14394
2004
Rattus norvegicus (P10868)
brenda
Tachikawa, M.; Fukaya, M.; Terasaki, T.; Ohtsuki, S.; Watanabe, M.
Distinct cellular expressions of creatine synthetic enzyme GAMT and creatine kinases uCK-Mi and CK-B suggest a novel neuron-glial relationship for brain energy homeostasis
Eur. J. Neurosci.
20
144-160
2004
Mus musculus
brenda
Braissant, O.; Henry, H.; Villard, A.; Speer, O.; Wallimann, T.; Bachmann, C.
Creatine synthesis and transport during rat embryogenesis: Spatiotemporal expression of AGAT, GAMT and CT1
BMC Dev. Biol.
5
9
2005
Rattus norvegicus (P10868)
brenda
Velichkova, P.; Himo, F.
Theoretical study of the methyl transfer in guanidinoacetate methyltransferase
J. Phys. Chem. B
110
16-19
2006
Rattus norvegicus (P10868)
brenda
Leuzzi, V.; Carducci, C.; Carducci, C.; Matricardi, M.; Bianchi, M.C.; Di Sabato, M.L.; Artiola, C.; Antonozzi, I.
A mutation on exon 6 of guanidinoacetate methyltransferase (GAMT) gene supports a different function for isoform a and b of GAMT enzyme
Mol. Genet. Metab.
87
88-90
2006
Homo sapiens
brenda
Almeida, L.S.; Rosenberg, E.H.; Martinez-Munoz, C.; Verhoeven, N.M.; Vilarinho, L.; Jakobs, C.; Salomons, G.S.
Overexpression of GAMT restores GAMT activity in primary GAMT-deficient fibroblasts
Mol. Genet. Metab.
89
392-394
2006
Homo sapiens (Q14353), Homo sapiens
brenda
Zhang, X.; Bruice, T.C.
Reaction mechanism of guanidinoacetate methyltransferase, concerted or step-wise
Proc. Natl. Acad. Sci. USA
103
16141-16146
2006
Rattus norvegicus (P10868)
brenda
Wang, L.; Chen, D.; Zhang, Y.; Lin, Y.; Li, J.; Zhang, H.
Characterization of AGAT, GAMT and CT1 in amphioxus: implications for the evolutionary conservation of creatine metabolism related molecules at the invertebrate-to-vertebrate transition
Dev. Genes Evol.
218
681-689
2008
Branchiostoma belcheri (Q3S316)
brenda
Kan, H.E.; Meeuwissen, E.; van Asten, J.J.; Veltien, A.; Isbrandt, D.; Heerschap, A.
Creatine uptake in brain and skeletal muscle of mice lacking guanidinoacetate methyltransferase assessed by magnetic resonance spectroscopy
J. Appl. Physiol.
102
2121-2127
2007
Mus musculus
brenda
Schneider, J.E.; Stork, L.A.; Bell, J.T.; Hove, M.T.; Isbrandt, D.; Clarke, K.; Watkins, H.; Lygate, C.A.; Neubauer, S.
Cardiac structure and function during ageing in energetically compromised Guanidinoacetate N-methyltransferase (GAMT)-knockout mice - a one year longitudinal MRI study
J. Cardiovasc. Magn. Reson.
10
1-9
2008
Mus musculus
brenda
Vodopiutz, J.; Item, C.B.; Haeusler, M.; Korall, H.; Bodamer, O.A.
Severe speech delay as the presenting symptom of guanidinoacetate methyltransferase deficiency
J. Child Neurol.
22
773-774
2007
Homo sapiens
brenda
Braissant, O.; Henry, H.
AGAT, GAMT and SLC6A8 distribution in the central nervous system, in relation to creatine deficiency syndromes: A review
J. Inherit. Metab. Dis.
31
230-239
2008
Homo sapiens, Mus musculus
brenda
Verbruggen, K.T.; Sijens, P.E.; Schulze, A.; Lunsing, R.J.; Jakobs, C.; Salomons, G.S.; van Spronsen, F.J.
Successful treatment of a guanidinoacetate methyltransferase deficient patient: findings with relevance to treatment strategy and pathophysiology
Mol. Genet. Metab.
91
294-296
2007
Homo sapiens
brenda
Heerschap, A.; Kan, H.E.; Nabuurs, C.I.; Renema, W.K.; Isbrandt, D.; Wieringa, B.
In vivo magnetic resonance spectroscopy of transgenic mice with altered expression of guanidinoacetate methyltransferase and creatine kinase isoenzymes
Subcell. Biochem.
46
119-148
2007
Mus musculus
brenda
da Silva, R.P.; Nissim, I.; Brosnan, M.E.; Brosnan, J.T.
Creatine synthesis: hepatic metabolism of guanidinoacetate and creatine in the rat in vitro and in vivo
Am. J. Physiol. Endocrinol. Metab.
296
E256-E261
2009
Rattus norvegicus
brenda
Ireland, Z.; Russell, A.; Wallimann, T.; Walker, D.; Snow, R.
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Zhu, Y.; Prives, C.
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Mus musculus
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Ide, T.; Brown-Endres, L.; Chu, K.; Ongusaha, P.P.; Ohtsuka, T.; El-Deiry, W.S.; Aaronson, S.A.; Lee, S.W.
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Homo sapiens, Mus musculus
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Mercimek-Mahmutoglu, S.; Ndika, J.; Kanhai, W.; de Villemeur, T.B.; Cheillan, D.; Christensen, E.; Dorison, N.; Hannig, V.; Hendriks, Y.; Hofstede, F.C.; Lion-Francois, L.; Lund, A.M.; Mundy, H.; Pitelet, G.; Raspall-Chaure, M.; Scott-Schwoerer, J.A.; Szakszon, K.; Valayannopoulos, V.; William, M.; Salomons, G.S.
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Homo sapiens (Q14353), Homo sapiens
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Berends, L.M.; Struys, E.A.; Roos, B.; Holwerda, U.; Jansen, E.E.W.; Salomons, G.S.; Wamelink, M.M.C.
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Homo sapiens (Q14353), Homo sapiens
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Tachikawa, M.; Watanabe, M.; Fukaya, M.; Sakai, K.; Terasaki, T.; Hosoya, K.I.
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Mus musculus (O35969)
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