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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General Information
General Information on EC 2.1.4.1 - glycine amidinotransferase
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evolution
malfunction
metabolism
additional information
CyrA is phylogenetically distinct from other amidinotransferases
evolution
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CyrA is phylogenetically distinct from other amidinotransferases
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AGAT deficiency (and consequently homoarginine and creatine deficiency) is associated with larger infarct volumes and worse neurological deficits compared with wild-type littermates. Homoarginine is absent in enzyme knockout AGAT-/- mice and increased in guanidinoacetate N-methyltransferase knockout mice, GAMT-/-. Cerebral damage and neurological deficits in experimental stroke are increased in AGAT-/- mice and attenuated by homoarginine supplementation, whereas infarct size in GAMT-/- mice is decreased compared with controls
malfunction
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enzyme-deficient mice develop cardiac dysfunction. Enzyme-deficient mice have rescuable changes in body water and organ weights suggesting a role for creatine as a compatible osmolyte. Creatine-naive enzyme-deficient mice have haemodynamic impairment with low left ventricular systolic pressure and reduced inotropy, lusitropy, and contractile reserve
malfunction
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AGAT deficiency (and consequently homoarginine and creatine deficiency) is associated with larger infarct volumes and worse neurological deficits compared with wild-type littermates. Homoarginine is absent in enzyme knockout AGAT-/- mice and increased in guanidinoacetate N-methyltransferase knockout mice, GAMT-/-. Cerebral damage and neurological deficits in experimental stroke are increased in AGAT-/- mice and attenuated by homoarginine supplementation, whereas infarct size in GAMT-/- mice is decreased compared with controls
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CyrA is involved in the pathway for biosynthesis of the polyketide-derived hepatotoxin cylindrospermopsin
metabolism
plasma homoarginine as strongly associated with single nucleotide polymorphisms in the L-arginine:glycine amidinotransferase (AGAT) gene, and increased AGAT expression in a cell model is associated with increased homoarginine, link between plasma homoarginine and outcome after experimental ischemic stroke. Allele-specific homoarginine plasma levels across the L-arginine:glycine amidinotransferase (AGAT) genotypes, overview
metabolism
plasma homoarginine as strongly associated with single nucleotide polymorphisms in the L-arginine:glycine amidinotransferase (AGAT) gene, and increased AGAT expression in a cell model is associated with increased homoarginine, link between plasma homoarginine and outcome after experimental ischemic stroke. Allele-specific homoarginine plasma levels across the L-arginine:glycine amidinotransferase (AGAT) genotypes, overview
metabolism
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CyrA is involved in the pathway for biosynthesis of the polyketide-derived hepatotoxin cylindrospermopsin
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metabolism
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plasma homoarginine as strongly associated with single nucleotide polymorphisms in the L-arginine:glycine amidinotransferase (AGAT) gene, and increased AGAT expression in a cell model is associated with increased homoarginine, link between plasma homoarginine and outcome after experimental ischemic stroke. Allele-specific homoarginine plasma levels across the L-arginine:glycine amidinotransferase (AGAT) genotypes, overview
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ligand-induced conformational changes in wild-type CyrA, structure-function-stability relationship, overview
additional information
Biallelic expression of the L-arginine:glycine amidinotransferase gene with different methylation status between male and female primordial germ cells in chickens
additional information
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Biallelic expression of the L-arginine:glycine amidinotransferase gene with different methylation status between male and female primordial germ cells in chickens
additional information
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Biallelic expression of the L-arginine:glycine amidinotransferase gene with different methylation status between male and female primordial germ cells in chickens
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additional information
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ligand-induced conformational changes in wild-type CyrA, structure-function-stability relationship, overview
-
additional information
-
Biallelic expression of the L-arginine:glycine amidinotransferase gene with different methylation status between male and female primordial germ cells in chickens
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