2.1.1.20: glycine N-methyltransferase
This is an abbreviated version!
For detailed information about glycine N-methyltransferase, go to the full flat file.
Word Map on EC 2.1.1.20
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2.1.1.20
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s-adenosylmethionine
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s-adenosylhomocysteine
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homocysteine
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folate
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sarcosine
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adenosyltransferase
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cystathionine
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transmethylation
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adomet
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betaine-homocysteine
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remethylation
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beta-synthase
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one-carbon
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transsulfuration
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5-methyltetrahydrofolate
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medicine
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folate-dependent
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n-methylglycine
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s-methyltransferase
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glycine-n-methyltransferase
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guanidinoacetate
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folate-deficient
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pentaglutamate
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pah-binding
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adohcy
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diagnostics
- 2.1.1.20
- s-adenosylmethionine
- s-adenosylhomocysteine
- homocysteine
- folate
- sarcosine
-
adenosyltransferase
- cystathionine
-
transmethylation
- adomet
-
betaine-homocysteine
-
remethylation
- beta-synthase
-
one-carbon
-
transsulfuration
- 5-methyltetrahydrofolate
- medicine
-
folate-dependent
- n-methylglycine
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s-methyltransferase
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glycine-n-methyltransferase
- guanidinoacetate
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folate-deficient
- pentaglutamate
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pah-binding
-
adohcy
- diagnostics
Reaction
Synonyms
4S polycyclic aromatic hydrocarbon binding protein, glycine methyltransferase, glycine N-methyltransferase, glycine-N methyltransferase, GNMT, Gnmt gene product, methyltransferase, glycine, S-adenosyl-L-methionine:glycine methyltransferase
ECTree
2.1.1.20 glycine N-methyltransferaseAdvanced search results
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results (Engineering
Engineering on EC 2.1.1.20 - glycine N-methyltransferase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
DELTA171-295
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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
crystal structure: N-terminal domains of subunits have moved out of the active sites of adjacent subunits
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
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
Y21A
mutant yields the same magnitude of binary isotope effect as wild-type
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
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
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
Y21G
mutant yields the same magnitude of binary isotope effect as wild-type
additional information
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patients with mutations Leu49Pro and His176Asn suffer from mild liver disease
additional information
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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
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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
