2.1.4.1: glycine amidinotransferase
This is an abbreviated version!
For detailed information about glycine amidinotransferase, go to the full flat file.
Word Map on EC 2.1.4.1
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2.1.4.1
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creatine
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guanidinoacetate
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homoarginine
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slc6a8
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harg
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phosphocreatine
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medicine
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creatine-deficient
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transamidination
- 2.1.4.1
- creatine
- guanidinoacetate
- homoarginine
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slc6a8
- harg
- phosphocreatine
- medicine
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creatine-deficient
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transamidination
Reaction
Synonyms
AGAT, arginine-glycine amidinotransferase, arginine-glycine transamidinase, arginine:glycine amidinotransferase, CyrA, EC 2.6.2.1, GAT, GATM, glycine amidinotransferase, glycine aminotransferase, glycine transamidinase, L-arginine:glycine amidinotransferase
ECTree
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Engineering
Engineering on EC 2.1.4.1 - glycine amidinotransferase
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F245N
site-directed mutagenesis, exchange analogously to the human L-arginine:glycine amidinotransferase, h-AGAT. F245N variant seems to lack the potential ligand-induced conformational changes. Higher activity of the F245N variant is enthalpy-driven
F245N/S247M
site-directed mutagenesis, exchange analogously to the human L-arginine:glycine amidinotransferase, h-AGAT
S247M
site-directed mutagenesis, exchange analogously to the human L-arginine:glycine amidinotransferase, h-AGAT
F245N
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site-directed mutagenesis, exchange analogously to the human L-arginine:glycine amidinotransferase, h-AGAT. F245N variant seems to lack the potential ligand-induced conformational changes. Higher activity of the F245N variant is enthalpy-driven
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F245N/S247M
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site-directed mutagenesis, exchange analogously to the human L-arginine:glycine amidinotransferase, h-AGAT
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S247M
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site-directed mutagenesis, exchange analogously to the human L-arginine:glycine amidinotransferase, h-AGAT
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medicine
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in vitro assay for enzyme activity in lymphocytes based on stable-isotope-labeled substrates L-(guanidino-15N2)arginine and U-(13C,15N)glycine
additional information
the residue replacements do not change the kinetic mechanism of the three variant enzymes. The mutant protein variants have broad substrate specificity, e.g. the F245N variant additionally accepts creatine, with 7% relative activity
additional information
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the residue replacements do not change the kinetic mechanism of the three variant enzymes. The mutant protein variants have broad substrate specificity, e.g. the F245N variant additionally accepts creatine, with 7% relative activity
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