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Information on EC 2.1.4.1 - glycine amidinotransferase
for references in articles please use BRENDA:EC2.1.4.1
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EC Tree 2 Transferases
2.1 Transferring one-carbon groups
2.1.4 Amidinotransferases
2.1.4.1 glycine amidinotransferase
IUBMB Comments
Canavanine can act instead of arginine.
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
- 2.1.4.1
- creatine
- guanidinoacetate
- homoarginine
-
slc6a8
- harg
- phosphocreatine
- medicine
-
creatine-deficient
-
transamidination
showSynonyms
l-arginine:glycine amidinotransferase, glycine amidinotransferase, arginine:glycine amidinotransferase, arginine-glycine amidinotransferase, glycine aminotransferase, arginine-glycine transamidinase, glycine transamidinase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
AGAT
AkAGAT
amidinotransferase
arginine-glycine amidinotransferase
-
-
-
-
arginine-glycine transamidinase
-
-
-
-
arginine:glycine amidinotransferase
CrAGAT
CyrA
EC 2.6.2.1
-
-
formerly
-
GAT
GATM
glycine amidinotransferase
glycine amidinotransferase, mitochondrial
glycine transamidinase
-
-
-
-
L-arginine:glycine amidinotransferase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
L-arginine + glycine = L-ornithine + guanidinoacetate
canavanine can act instead of arginine
-
-
-
L-arginine + glycine = L-ornithine + guanidinoacetate
reaction and kinetic mechanisms, overview
L-arginine + glycine = L-ornithine + guanidinoacetate
reaction and kinetic mechanisms, overview
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
amidine group transfer
transamidination
-
-
-
-
amidine group transfer
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
MetaCyc
creatine biosynthesis, cylindrospermopsin biosynthesis, guadinomine B biosynthesis
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SYSTEMATIC NAME
IUBMB Comments
L-arginine:glycine amidinotransferase
Canavanine can act instead of arginine.
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CAS REGISTRY NUMBER
COMMENTARY
9027-35-4
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
arginine + 5-aminovaleric acid
5-guanidinovaleric acid + ornithine
-
Substrates: -
Products: -
Products: -
?
arginine + delta-aminovaleric acid
delta-guanidinovaleric acid + ornithine
-
Substrates: -
Products: -
Products: -
?
arginine + gamma-aminobutyric acid
gamma-guanidinobutyric acid + ornithine
-
Substrates: -
Products: -
Products: -
?
hydroxyguanidine + glycine
hydroxylamine + guanidinoacetate
-
Substrates: -
Products: -
Products: -
?
arginine + 3-aminopropionic acid
3-guanidinopropionic acid + ornithine
-
Substrates: -
Products: -
Products: -
?
arginine + 3-aminopropionic acid
3-guanidinopropionic acid + ornithine
-
Substrates: -
Products: -
Products: -
?
arginine + 4-aminobutyric acid
4-guanidinobutyric acid + ornithine
-
Substrates: -
Products: -
Products: -
?
arginine + 4-aminobutyric acid
4-guanidinobutyric acid + ornithine
-
Substrates: -
Products: -
Products: -
?
arginine + 4-aminobutyric acid
4-guanidinobutyric acid + ornithine
-
Substrates: -
Products: -
Products: -
?
arginine + ethanolamine
2-guanidinoethanol + ornithine
-
Substrates: -
Products: -
Products: -
?
arginine + ethanolamine
2-guanidinoethanol + ornithine
-
Substrates: -
Products: -
Products: -
?
arginine + ethanolamine
2-guanidinoethanol + ornithine
-
Substrates: -
Products: -
Products: -
?
arginine + ethanolamine
2-guanidinoethanol + ornithine
-
Substrates: -
Products: -
Products: -
?
arginine + hydroxylamine
ornithine + hydroxyguanidine
-
Substrates: -
Products: -
Products: -
?
arginine + hydroxylamine
ornithine + hydroxyguanidine
-
Substrates: -
Products: -
Products: -
?
arginine + taurine
2-guanidinoethanesulfonic acid + ornithine
-
Substrates: -
Products: -
Products: -
?
arginine + taurine
2-guanidinoethanesulfonic acid + ornithine
-
Substrates: -
Products: -
Products: -
?
canavanine + canaline
canaline + canavanine
-
Substrates: -
Products: -
Products: -
?
canavanine + glycine
guanidinoacetate + canaline
-
Substrates: -
Products: -
Products: -
r
canavanine + glycine
guanidinoacetate + canaline
-
Substrates: -
Products: -
Products: -
r
canavanine + glycine
guanidinoacetate + canaline
-
Substrates: -
Products: -
Products: -
r
canavanine + glycine
guanidinoacetate + canaline
-
Substrates: -
Products: -
Products: -
r
canavanine + hydroxylamine
canaline + hydroxyguanidine
-
Substrates: -
Products: -
Products: -
?
canavanine + hydroxylamine
canaline + hydroxyguanidine
-
Substrates: -
Products: -
Products: -
?
canavanine + ornithine
arginine + canaline
-
Substrates: -
Products: -
Products: -
r
canavanine + ornithine
arginine + canaline
-
Substrates: -
Products: -
Products: -
r
canavanine + ornithine
arginine + canaline
-
Substrates: -
Products: -
Products: -
r
canavanine + ornithine
arginine + canaline
-
Substrates: -
Products: -
Products: -
r
canavanine + ornithine
arginine + canaline
-
Substrates: -
Products: -
Products: -
r
canavanine + ornithine
arginine + canaline
-
Substrates: -
Products: -
Products: -
r
canavanine + ornithine
arginine + canaline
Substrates: -
Products: -
Products: -
r
canavanine + ornithine
arginine + canaline
-
Substrates: -
Products: -
Products: -
r
canavanine + ornithine
arginine + canaline
Substrates: -
Products: -
Products: -
r
canavanine + ornithine
arginine + canaline
-
Substrates: -
Products: -
Products: -
r
canavanine + ornithine
arginine + canaline
-
Substrates: -
Products: -
Products: -
r
canavanine + ornithine
arginine + canaline
-
485960, 485961, 485962, 485963, 485964, 485965, 485966, 485967, 485968, 485971, 485973, 485974, 485975, 485976, 485978
Substrates: -
Products: -
Products: -
r
glycine + guanidinoacetate
guanidinoacetate + glycine
-
Substrates: -
Products: -
Products: -
r
glycine + guanidinoacetate
guanidinoacetate + glycine
-
Substrates: -
Products: -
Products: -
r
guanidinoacetate + canaline
glycine + canavanine
-
Substrates: -
Products: -
Products: -
?
guanidinoacetate + glycine
?
Substrates: -
Products: -
Products: -
?
guanidinoacetate + glycine
?
Substrates: -
Products: -
Products: -
?
guanidinoacetate + hydroxylamine
hydroxyguanidine + glycine
-
Substrates: -
Products: -
Products: -
?
guanidinoacetate + hydroxylamine
hydroxyguanidine + glycine
-
Substrates: -
Products: -
Products: -
?
guanidinoacetate + hydroxylamine
hydroxyguanidine + glycine
-
Substrates: -
Products: -
Products: -
?
guanidinoacetate + ornithine
glycine + arginine
-
Substrates: -
Products: -
Products: -
?
guanidinoacetate + ornithine
glycine + arginine
-
Substrates: -
Products: -
Products: -
?
homoarginine + glycine
homoornithine + guanidinoacetate
-
Substrates: -
Products: -
Products: -
r
homoarginine + glycine
homoornithine + guanidinoacetate
-
Substrates: -
Products: -
Products: -
r
homoarginine + glycine
homoornithine + guanidinoacetate
-
Substrates: -
Products: -
Products: -
r
homoarginine + glycine
homoornithine + guanidinoacetate
-
Substrates: -
Products: -
Products: -
r
hydroxylamine + glycine
L-ornithine + hydroxyguanidine
Substrates: -
Products: -
Products: -
?
hydroxylamine + glycine
L-ornithine + hydroxyguanidine
Substrates: -
Products: -
Products: -
?
L-arginine + glycine
L-ornithine + guanidinoacetate
Substrates: -
Products: -
Products: -
r
L-arginine + glycine
L-ornithine + guanidinoacetate
-
Substrates: -
Products: -
Products: -
r
L-arginine + glycine
L-ornithine + guanidinoacetate
-
Substrates: -
Products: -
Products: -
r
L-arginine + glycine
L-ornithine + guanidinoacetate
Substrates: -
Products: -
Products: -
?
L-arginine + glycine
L-ornithine + guanidinoacetate
-
Substrates: -
Products: -
Products: -
r
L-arginine + glycine
L-ornithine + guanidinoacetate
Substrates: -
Products: -
Products: -
?
L-arginine + glycine
L-ornithine + guanidinoacetate
Substrates: -
Products: -
Products: -
?
L-arginine + glycine
L-ornithine + guanidinoacetate
Substrates: L-ornithine is formed in the presence of only a single substrate, arginine, and its production therefore does not require the presence of the second substrate, glycine
Products: -
Products: -
?
L-arginine + glycine
L-ornithine + guanidinoacetate
Substrates: -
Products: -
Products: -
r
L-arginine + glycine
L-ornithine + guanidinoacetate
Substrates: -
Products: -
Products: -
?
L-arginine + glycine
L-ornithine + guanidinoacetate
Substrates: L-ornithine is formed in the presence of only a single substrate, arginine, and its production therefore does not require the presence of the second substrate, glycine
Products: -
Products: -
?
L-arginine + glycine
L-ornithine + guanidinoacetate
Substrates: -
Products: -
Products: -
?
L-arginine + glycine
L-ornithine + guanidinoacetate
Substrates: -
Products: -
Products: -
r
L-arginine + glycine
L-ornithine + guanidinoacetate
Felis domestica
-
Substrates: -
Products: -
Products: -
r
L-arginine + glycine
L-ornithine + guanidinoacetate
-
Substrates: -
Products: -
Products: -
r
L-arginine + glycine
L-ornithine + guanidinoacetate
Substrates: -
Products: -
Products: -
r
L-arginine + glycine
L-ornithine + guanidinoacetate
Substrates: -
Products: -
Products: -
?
L-arginine + glycine
L-ornithine + guanidinoacetate
Substrates: -
Products: -
Products: -
?
L-arginine + glycine
L-ornithine + guanidinoacetate
Substrates: -
Products: -
Products: -
?
L-arginine + glycine
L-ornithine + guanidinoacetate
-
Substrates: nitrogen metabolism, putrescine biosynthesis
Products: -
Products: -
r
L-arginine + glycine
L-ornithine + guanidinoacetate
-
Substrates: -
Products: -
Products: -
r
L-arginine + glycine
L-ornithine + guanidinoacetate
Substrates: -
Products: -
Products: -
r
L-arginine + glycine
L-ornithine + guanidinoacetate
-
Substrates: -
Products: -
Products: -
r
L-arginine + glycine
L-ornithine + guanidinoacetate
Substrates: -
Products: -
Products: -
r
L-arginine + glycine
L-ornithine + guanidinoacetate
-
Substrates: -
Products: -
Products: -
r
L-arginine + glycine
L-ornithine + guanidinoacetate
Substrates: first reaction in the de novo biosynthesis of creatine
Products: -
Products: -
r
L-arginine + glycine
L-ornithine + guanidinoacetate
Substrates: first reaction in the de novo biosynthesis of creatine
Products: -
Products: -
r
L-arginine + glycine
L-ornithine + guanidinoacetate
-
Substrates: enzyme is involved in biosynthesis of creatine. Patients with AGAT deficiency show mental and motor retardation and severe delay in speech development. Both creatine and guanidinoacetate are decreased in body fluids of AGAT-deficient patients
Products: -
Products: -
?
L-arginine + glycine
L-ornithine + guanidinoacetate
Substrates: -
Products: -
Products: -
?
L-arginine + glycine
L-ornithine + guanidinoacetate
Substrates: -
Products: -
Products: -
r
L-arginine + glycine
L-ornithine + guanidinoacetate
Substrates: -
Products: -
Products: -
?
L-arginine + glycine
L-ornithine + guanidinoacetate
Lacerta sp.
-
Substrates: -
Products: -
Products: -
r
L-arginine + glycine
L-ornithine + guanidinoacetate
-
Substrates: -
Products: -
Products: -
r
L-arginine + glycine
L-ornithine + guanidinoacetate
Substrates: -
Products: -
Products: -
r
L-arginine + glycine
L-ornithine + guanidinoacetate
Substrates: -
Products: -
Products: -
r
L-arginine + glycine
L-ornithine + guanidinoacetate
-
Substrates: -
Products: -
Products: -
r
L-arginine + glycine
L-ornithine + guanidinoacetate
Substrates: -
Products: -
Products: -
?
L-arginine + glycine
L-ornithine + guanidinoacetate
-
Substrates: -
Products: -
Products: -
?
L-arginine + glycine
L-ornithine + guanidinoacetate
Substrates: -
Products: -
Products: -
?
L-arginine + glycine
L-ornithine + guanidinoacetate
Substrates: -
Products: -
Products: -
?
L-arginine + glycine
L-ornithine + guanidinoacetate
-
Substrates: -
Products: -
Products: -
r
L-arginine + glycine
L-ornithine + guanidinoacetate
-
Substrates: -
Products: -
Products: -
r
L-arginine + glycine
L-ornithine + guanidinoacetate
-
Substrates: -
Products: -
Products: -
r
L-arginine + glycine
L-ornithine + guanidinoacetate
Substrates: -
Products: -
Products: -
r
L-arginine + glycine
L-ornithine + guanidinoacetate
-
Substrates: -
Products: -
Products: -
r
L-arginine + glycine
L-ornithine + guanidinoacetate
Substrates: first reaction in the de novo biosynthesis of creatine
Products: -
Products: -
r
L-arginine + glycine
L-ornithine + guanidinoacetate
Substrates: first reaction in the de novo biosynthesis of creatine
Products: -
Products: -
r
L-arginine + glycine
L-ornithine + guanidinoacetate
Substrates: -
Products: -
Products: -
?
L-arginine + glycine
L-ornithine + guanidinoacetate
-
Substrates: -
Products: -
Products: -
?
L-arginine + glycine
L-ornithine + guanidinoacetate
-
Substrates: -
Products: -
Products: -
r
L-arginine + glycine
L-ornithine + guanidinoacetate
-
Substrates: -
Products: -
Products: -
r
L-arginine + glycine
L-ornithine + guanidinoacetate
-
485960, 485961, 485962, 485963, 485964, 485965, 485966, 485967, 485968, 485971, 485973, 485974, 485975, 485976, 485978
Substrates: -
Products: -
Products: -
r
L-ornithine + guanidinoacetate
L-arginine + glycine
-
Substrates: -
Products: -
Products: -
r
L-ornithine + guanidinoacetate
L-arginine + glycine
Substrates: -
Products: -
Products: -
r
L-ornithine + guanidinoacetate
L-arginine + glycine
-
Substrates: -
Products: -
Products: -
r
L-ornithine + guanidinoacetate
L-arginine + glycine
Substrates: -
Products: -
Products: -
r
L-ornithine + guanidinoacetate
L-arginine + glycine
Substrates: -
Products: -
Products: -
r
L-ornithine + guanidinoacetate
L-arginine + glycine
Substrates: -
Products: -
Products: -
r
L-ornithine + guanidinoacetate
L-arginine + glycine
Substrates: -
Products: -
Products: -
r
L-ornithine + guanidinoacetate
L-arginine + glycine
-
485960, 485961, 485962, 485963, 485964, 485965, 485966, 485967, 485968, 485971, 485973, 485974, 485975, 485976, 485978
Substrates: -
Products: -
Products: -
r
additional information
?
-
Substrates: narrow substrate specificity, no activity with L-homoarginine, agmatine, L-canavanine, guanidine hydrochloride, urea, gamma-guanidinobutyric acid, and beta-guanidinoproprionic acid as amidino group donors, or L-alanine, beta-alanine, gamma-aminobutyric acid, ethanolamine, taurine, L-lysine, alpha-amino-oxyacetic acid and L-norvaline as amidino group acceptors, overview
Products: -
Products: -
?
additional information
?
-
Substrates: no activity with creatine, L-homoarginine, and L-canavanine by the wild-type enzyme, while mutants F245N, S247M, and F245N/S247M are also active L-homoarginine and L-canavanine, mutant F254N also slightly with creatine, overview
Products: -
Products: -
?
additional information
?
-
Substrates: narrow substrate specificity, no activity with L-homoarginine, agmatine, L-canavanine, guanidine hydrochloride, urea, gamma-guanidinobutyric acid, and beta-guanidinoproprionic acid as amidino group donors, or L-alanine, beta-alanine, gamma-aminobutyric acid, ethanolamine, taurine, L-lysine, alpha-amino-oxyacetic acid and L-norvaline as amidino group acceptors, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: narrow substrate specificity, no activity with L-homoarginine, agmatine, L-canavanine, guanidine hydrochloride, urea, gamma-guanidinobutyric acid, and beta-guanidinoproprionic acid as amidino group donors, or L-alanine, beta-alanine, gamma-aminobutyric acid, ethanolamine, taurine, L-lysine, alpha-amino-oxyacetic acid and L-norvaline as amidino group acceptors, overview
Products: -
Products: -
?
additional information
?
-
Substrates: no activity with creatine, L-homoarginine, and L-canavanine by the wild-type enzyme, while mutants F245N, S247M, and F245N/S247M are also active L-homoarginine and L-canavanine, mutant F254N also slightly with creatine, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: homoarginine, alpha-amino-gamma-guanidinobutyric acid and alpha-amino-beta-guanidinopropionic acid are not substrates
Products: -
Products: -
?
additional information
?
-
Substrates: based on the circulating concentrations of Arg, Lys, Gly, Orn, GAA, and hArg in healthy humans, the Kgaa and Kharg values are expected to be far below 1 each, and that of KAGAT about 1, overview
Products: -
Products: -
-
additional information
?
-
-
Substrates: L-glutamic acid, L-aspartic acid and histidine are no substrates
Products: -
Products: -
?
additional information
?
-
-
Substrates: L-glutamic acid, L-aspartic acid and histidine are no substrates
Products: -
Products: -
?
additional information
?
-
-
Substrates: possible amidino group acceptors gamma-aminobutyric acid, beta-alanine, hydroxylamine
Products: -
Products: -
?
additional information
?
-
-
Substrates: lysine will not substitute for ornithine
Products: -
Products: -
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
additional information
?
-
Substrates: based on the circulating concentrations of Arg, Lys, Gly, Orn, GAA, and hArg in healthy humans, the Kgaa and Kharg values are expected to be far below 1 each, and that of KAGAT about 1, overview
Products: -
Products: -
-
L-arginine + glycine
L-ornithine + guanidinoacetate
Substrates: -
Products: -
Products: -
r
L-arginine + glycine
L-ornithine + guanidinoacetate
-
Substrates: -
Products: -
Products: -
r
L-arginine + glycine
L-ornithine + guanidinoacetate
-
Substrates: -
Products: -
Products: -
r
L-arginine + glycine
L-ornithine + guanidinoacetate
Substrates: -
Products: -
Products: -
?
L-arginine + glycine
L-ornithine + guanidinoacetate
-
Substrates: -
Products: -
Products: -
r
L-arginine + glycine
L-ornithine + guanidinoacetate
Substrates: -
Products: -
Products: -
?
L-arginine + glycine
L-ornithine + guanidinoacetate
Substrates: -
Products: -
Products: -
?
L-arginine + glycine
L-ornithine + guanidinoacetate
Substrates: -
Products: -
Products: -
r
L-arginine + glycine
L-ornithine + guanidinoacetate
Substrates: -
Products: -
Products: -
?
L-arginine + glycine
L-ornithine + guanidinoacetate
Substrates: -
Products: -
Products: -
r
L-arginine + glycine
L-ornithine + guanidinoacetate
Felis domestica
-
Substrates: -
Products: -
Products: -
r
L-arginine + glycine
L-ornithine + guanidinoacetate
-
Substrates: -
Products: -
Products: -
r
L-arginine + glycine
L-ornithine + guanidinoacetate
Substrates: -
Products: -
Products: -
r
L-arginine + glycine
L-ornithine + guanidinoacetate
-
Substrates: nitrogen metabolism, putrescine biosynthesis
Products: -
Products: -
r
L-arginine + glycine
L-ornithine + guanidinoacetate
-
Substrates: -
Products: -
Products: -
r
L-arginine + glycine
L-ornithine + guanidinoacetate
Substrates: -
Products: -
Products: -
r
L-arginine + glycine
L-ornithine + guanidinoacetate
-
Substrates: -
Products: -
Products: -
r
L-arginine + glycine
L-ornithine + guanidinoacetate
Substrates: -
Products: -
Products: -
r
L-arginine + glycine
L-ornithine + guanidinoacetate
-
Substrates: -
Products: -
Products: -
r
L-arginine + glycine
L-ornithine + guanidinoacetate
Substrates: first reaction in the de novo biosynthesis of creatine
Products: -
Products: -
r
L-arginine + glycine
L-ornithine + guanidinoacetate
Substrates: first reaction in the de novo biosynthesis of creatine
Products: -
Products: -
r
L-arginine + glycine
L-ornithine + guanidinoacetate
-
Substrates: enzyme is involved in biosynthesis of creatine. Patients with AGAT deficiency show mental and motor retardation and severe delay in speech development. Both creatine and guanidinoacetate are decreased in body fluids of AGAT-deficient patients
Products: -
Products: -
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L-arginine + glycine
L-ornithine + guanidinoacetate
Substrates: -
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L-arginine + glycine
L-ornithine + guanidinoacetate
Substrates: -
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r
L-arginine + glycine
L-ornithine + guanidinoacetate
Substrates: -
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?
L-arginine + glycine
L-ornithine + guanidinoacetate
Lacerta sp.
-
Substrates: -
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r
L-arginine + glycine
L-ornithine + guanidinoacetate
-
Substrates: -
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r
L-arginine + glycine
L-ornithine + guanidinoacetate
Substrates: -
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r
L-arginine + glycine
L-ornithine + guanidinoacetate
Substrates: -
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r
L-arginine + glycine
L-ornithine + guanidinoacetate
-
Substrates: -
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r
L-arginine + glycine
L-ornithine + guanidinoacetate
Substrates: -
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?
L-arginine + glycine
L-ornithine + guanidinoacetate
-
Substrates: -
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?
L-arginine + glycine
L-ornithine + guanidinoacetate
Substrates: -
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L-arginine + glycine
L-ornithine + guanidinoacetate
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L-arginine + glycine
L-ornithine + guanidinoacetate
-
Substrates: -
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r
L-arginine + glycine
L-ornithine + guanidinoacetate
-
Substrates: -
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r
L-arginine + glycine
L-ornithine + guanidinoacetate
-
Substrates: -
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r
L-arginine + glycine
L-ornithine + guanidinoacetate
Substrates: -
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r
L-arginine + glycine
L-ornithine + guanidinoacetate
-
Substrates: -
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r
L-arginine + glycine
L-ornithine + guanidinoacetate
Substrates: first reaction in the de novo biosynthesis of creatine
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r
L-arginine + glycine
L-ornithine + guanidinoacetate
Substrates: first reaction in the de novo biosynthesis of creatine
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r
L-arginine + glycine
L-ornithine + guanidinoacetate
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?
L-arginine + glycine
L-ornithine + guanidinoacetate
-
Substrates: -
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L-arginine + glycine
L-ornithine + guanidinoacetate
-
Substrates: -
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r
L-arginine + glycine
L-ornithine + guanidinoacetate
-
Substrates: -
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r
L-arginine + glycine
L-ornithine + guanidinoacetate
-
485960, 485961, 485962, 485963, 485964, 485965, 485966, 485967, 485968, 485971, 485973, 485974, 485975, 485976, 485978
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L-ornithine + guanidinoacetate
L-arginine + glycine
-
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r
L-ornithine + guanidinoacetate
L-arginine + glycine
Substrates: -
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r
L-ornithine + guanidinoacetate
L-arginine + glycine
-
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r
L-ornithine + guanidinoacetate
L-arginine + glycine
Substrates: -
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r
L-ornithine + guanidinoacetate
L-arginine + glycine
Substrates: -
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r
L-ornithine + guanidinoacetate
L-arginine + glycine
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r
L-ornithine + guanidinoacetate
L-arginine + glycine
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r
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NH4+
NH4+-induced decrease in creatine and guanidinoacetate probably occurs through inhibition of AGAT enzymatic activity
additional information
pharmacological treatment of Becker muscular dystrophy (BMD) patients with metformin or L-citrulline results in antidromic effects on serum hArg and GAA concentrations, seemingly acting as an inhibitor and effector of AGAT activity, respectively
-
L-ornithine
partial mixed product inhibition, L-ornithine therefore binds to the active site of CyrA at a binding site distinct from the hydroxylamine-binding site
ornithine
-
above 1 mg per ml guanidinoacetate-ornithine transamidination is inhibited
ornithine
-
above 1 mg per ml guanidinoacetate-ornithine transamidination is inhibited
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Acute Kidney Injury
Interrelation of urinary and plasma levels of guanidinoacetic acid with alteration in renal activity of glycine amidinotransferase in acute renal failure rats.
Acute Kidney Injury
[Activity of glycine amidinotransferase and its isoforms in dog kidney tissue normally and in acute renal insufficiency]
Breast Neoplasms
Creatine-mediated crosstalk between adipocytes and cancer cells regulates obesity-driven breast cancer.
Carcinoma
A short review on creatine-creatine kinase system in relation to cancer and some experimental results on creatine as adjuvant in cancer therapy.
Carcinoma
Enzymes of creatine biosynthesis, arginine and methionine metabolism in normal and malignant cells.
Dent Disease
Novel Fanconi renotubular syndromes provide insights in proximal tubule pathophysiology.
Diabetes Mellitus
[Study of impaired metabolism of guanidinoacetic acid in uremia--the compensatory role of the pancreas in guanidinoacetic acid synthesis]
Fanconi Syndrome
Glycine Amidinotransferase (GATM), Renal Fanconi Syndrome, and Kidney Failure.
Genetic Diseases, Inborn
LC-MS/MS measurements of urinary guanidinoacetic acid and creatine: Method optimization by deleting derivatization step.
Glomerulonephritis
[Glycine amidinotransferase activity of the blood and urine of children with acute streptococcal glomerulonephritis]
glycine amidinotransferase deficiency
Arginine-Glycine Amidinotransferase Deficiency and Functional Characterization of Missense Variants in GATM.
glycine amidinotransferase deficiency
Arginine:glycine amidinotransferase (AGAT) deficiency in a newborn: early treatment can prevent phenotypic expression of the disease.
glycine amidinotransferase deficiency
Arginine:glycine amidinotransferase deficiency: a treatable metabolic encephalomyopathy.
glycine amidinotransferase deficiency
Arginine:glycine amidinotransferase deficiency: the third inborn error of creatine metabolism in humans.
glycine amidinotransferase deficiency
Cerebral creatine deficiency syndromes: clinical aspects, treatment and pathophysiology.
glycine amidinotransferase deficiency
Creatine and creatine deficiency syndromes: biochemical and clinical aspects.
glycine amidinotransferase deficiency
Developmental progress and creatine restoration upon long-term creatine supplementation of a patient with arginine:glycine amidinotransferase deficiency.
glycine amidinotransferase deficiency
Diagnostic enzyme assay that uses stable-isotope-labeled substrates to detect L-arginine:glycine amidinotransferase deficiency.
glycine amidinotransferase deficiency
Fifteen-year follow-up of Italian families affected by arginine glycine amidinotransferase deficiency.
glycine amidinotransferase deficiency
Homoarginine- and Creatine-Dependent Gene Regulation in Murine Brains with l-Arginine:Glycine Amidinotransferase Deficiency.
glycine amidinotransferase deficiency
Inborn errors of creatine metabolism and epilepsy: clinical features, diagnosis, and treatment.
glycine amidinotransferase deficiency
L-arginine:glycine amidinotransferase deficiency protects from metabolic syndrome.
glycine amidinotransferase deficiency
LC-MS/MS measurements of urinary guanidinoacetic acid and creatine: Method optimization by deleting derivatization step.
guanidinoacetate n-methyltransferase deficiency
Cerebral creatine deficiency syndromes: clinical aspects, treatment and pathophysiology.
guanidinoacetate n-methyltransferase deficiency
Creatine and creatine deficiency syndromes: biochemical and clinical aspects.
guanidinoacetate n-methyltransferase deficiency
Guanidinoacetate and creatine plus creatinine assessment in physiologic fluids: an effective diagnostic tool for the biochemical diagnosis of arginine:glycine amidinotransferase and guanidinoacetate methyltransferase deficiencies.
guanidinoacetate n-methyltransferase deficiency
LC-MS/MS measurements of urinary guanidinoacetic acid and creatine: Method optimization by deleting derivatization step.
Gyrate Atrophy
Inhibition of arginine-glycine amidinotransferase by ornithine. A possible mechanism for the muscular and chorioretinal atrophies in gyrate atrophy of the choroid and retina with hyperornithinemia.
Heart Failure
Myocardial expression of the arginine:glycine amidinotransferase gene is elevated in heart failure and normalized after recovery: potential implications for local creatine synthesis.
Intellectual Disability
Arginine:glycine amidinotransferase (AGAT) deficiency in a newborn: early treatment can prevent phenotypic expression of the disease.
Intellectual Disability
Creatine depletion in a new case with AGAT deficiency: clinical and genetic study in a large pedigree.
Intellectual Disability
Fifteen-year follow-up of Italian families affected by arginine glycine amidinotransferase deficiency.
Intellectual Disability
Inborn errors of creatine metabolism and epilepsy: clinical features, diagnosis, and treatment.
Language Disorders
Inborn errors of creatine metabolism and epilepsy: clinical features, diagnosis, and treatment.
Metabolic Syndrome
Differential regulation of AMPK activation in leptin- and creatine-deficient mice.
Metabolic Syndrome
L-arginine:glycine amidinotransferase deficiency protects from metabolic syndrome.
Metabolism, Inborn Errors
Health implications of creatine: can oral creatine supplementation protect against neurological and atherosclerotic disease?
Metabolism, Inborn Errors
[Cerebral creatine transporter deficiency: an infradiagnosed neurometabolic disease]
Muscular Diseases
Creatine deficiency syndrome. A treatable myopathy due to arginine-glycine amidinotransferase (AGAT) deficiency.
Muscular Diseases
Muscle phenotype of AGAT- and GAMT-deficient mice after simvastatin exposure.
Muscular Diseases
Statins and skeletal muscles toxicity: from clinical trials to everyday practice.
Muscular Dystrophies
Reduced renal arginine-glycine transamidinase activity in myotonic goats and in patients with myotonic muscular dystrophy.
Neoplasms
Creatine-mediated crosstalk between adipocytes and cancer cells regulates obesity-driven breast cancer.
Neoplasms
Enzymes of creatine biosynthesis, arginine and methionine metabolism in normal and malignant cells.
Nephrosis, Lipoid
[Glycine transamidinase (ADT) activity in the serum and urine of children with lipoid nephrosis]
Pancreatitis
[Repression and depression of glycine amidinotransferase in the rat pancreas at different stages of the development of pancreatitis]
Renal Insufficiency
Genetic mitochondrial glycine amidinotransferase protein aggregate formation triggers microparticle sensing and kidney failure.
Renal Insufficiency
Glycine Amidinotransferase (GATM), Renal Fanconi Syndrome, and Kidney Failure.
Renal Insufficiency
Interrelation of urinary and plasma levels of guanidinoacetic acid with alteration in renal activity of glycine amidinotransferase in acute renal failure rats.
Renal Insufficiency
[Study of impaired metabolism of guanidinoacetic acid in uremia--the compensatory role of the pancreas in guanidinoacetic acid synthesis]
Sarcoma
A short review on creatine-creatine kinase system in relation to cancer and some experimental results on creatine as adjuvant in cancer therapy.
Sarcoma
Enzymes of creatine biosynthesis, arginine and methionine metabolism in normal and malignant cells.
Sarcoma 180
A short review on creatine-creatine kinase system in relation to cancer and some experimental results on creatine as adjuvant in cancer therapy.
Sarcoma 180
Enzymes of creatine biosynthesis, arginine and methionine metabolism in normal and malignant cells.
Stroke
Homoarginine Levels Are Regulated by L-Arginine:Glycine Amidinotransferase and Affect Stroke Outcome: Results From Human and Murine Studies.
Stroke
Homoarginine- and Creatine-Dependent Gene Regulation in Murine Brains with l-Arginine:Glycine Amidinotransferase Deficiency.
Tuberous Sclerosis
Proteomes analysis reveals the involvement of autophagy in AD-like neuropathology induced by noise exposure and ApoE4.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
Michaelis-Menten kinetics with non-natural substrate hydroxylamine, kinetic mechanism of CyrA as a hybrid of ping-pong and sequential mechanisms, overview
-
additional information
additional information
in vivo kinetic analysis, overview
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.0004
additional information
additional information
-
in vitro assay for enzyme activity based on stable-isotope-labeled substrates L-(guanidino-15N2)arginine and U-(13C,15N)glycine
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.4
7.5
8.5
9.2
-
synthesis of 3-guanidinopropionic acid, 2-guanidinoethanol and 2-guanidinoethanesulfonic acid
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7 - 8.5
25% of maximal activity at pH 7.0, maximal activity at pH 8.5
7 - 9
above pH 9, the activity dropped rapidly for all enzymes
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
37
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30 - 45
different optima for wild-type and mutant CyrAs, above 40°C activity decreases rapidly for all enzymes, including the S247M variant, which shows 18% of maximal activity at 45°C
32 - 40
20% of maximal activity at 40°C, maximal activity at 32°C
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
cytosolic enzyme, DDBJ/EMBL/GenBank database, cDNA sequence
SwissProt
brenda
human
485964, 485965, 485967, 485968, 485971, 485972, 485973, 485974, 485975, 485976, 485977, 485978, 485979
-
-
brenda
mitochondrial enzyme, DDBJ/EMBL/GenBank database, cDNA sequence
SwissProt
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
ependymal epithelium, adult brain, developing embryonic brain
brenda
additional information
the GATM gene displays biallelic expression in somatic embryonic and extraembryonic tissues
brenda
-
the GATM gene displays biallelic expression in somatic embryonic and extraembryonic tissues
-
brenda
-
the GATM gene displays biallelic expression in somatic embryonic and extraembryonic tissues
-
brenda
the GATM gene displays biallelic expression in primordial germ cells
brenda
-
the GATM gene displays biallelic expression in primordial germ cells
-
brenda
-
the GATM gene displays biallelic expression in primordial germ cells
-
brenda
-
-
485960, 485961, 485962, 485963, 485964, 485965, 485966, 485967, 485968, 485971, 485973, 485974, 485976, 705297
brenda
-
-
brenda
additional information
the GATM gene displays biallelic expression in primordial germ cells as well as somatic embryonic, extraembryonic, and adult chicken tissues, tissue-specific expression analysis, overview. Very low expression in embryonic heart and fibroblasts
brenda
additional information
-
the GATM gene displays biallelic expression in primordial germ cells as well as somatic embryonic, extraembryonic, and adult chicken tissues, tissue-specific expression analysis, overview. Very low expression in embryonic heart and fibroblasts
brenda
additional information
-
the GATM gene displays biallelic expression in primordial germ cells as well as somatic embryonic, extraembryonic, and adult chicken tissues, tissue-specific expression analysis, overview. Very low expression in embryonic heart and fibroblasts
-
brenda
additional information
-
the GATM gene displays biallelic expression in primordial germ cells as well as somatic embryonic, extraembryonic, and adult chicken tissues, tissue-specific expression analysis, overview. Very low expression in embryonic heart and fibroblasts
-
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
evolution
CyrA is phylogenetically distinct from other amidinotransferases
evolution
-
CyrA is phylogenetically distinct from other amidinotransferases
-
malfunction
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
-
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
arginine:glycine amidinotransferase (AGAT) deficiency is an ultrarare disorder of creatine metabolism, presenting with developmental delay, characteristic biochemical findings and muscle weakness. Most known cases have been identified and treated in early childhood. A 27-year-old female patient shows learning difficulties and significant myopathy. Treatment with creatine (10-15 g/day) led to a significant and rapid improvement of muscle strength. AGAT deficiency, a partially treatable condition, should be considered in the differential diagnosis of a genetic myopathy, particularly in people with developmental delay and progressive myopathy
malfunction
analysis of survival and cardiac outcome of AGAT knockout (Agat-/-) mice under hypoxia and a possible rescue of the phenotype. Mutant Agat-/- mice are nonviable in hypoxia. Creatine rescues the lethal phenotype, but does not reduce right ventricular hypertrophy of Agat-/- mice in hypoxia. Genes Agat and Gamt (guanidinoacetate N-methyltransferase, EC 2.1.1.2) expressions are differentially downregulated by hypoxia in lung, liver, and kidneys. hArg and creatine play differential roles in mediating the pathophysiological phenotypes of Agat-/- mice
malfunction
significant differences of gene expression are observed between AGAT-/- mutant and wild-type mice, affecting cardiac energy metabolism (Fbp2, Ucp2), cardiac hypertrophy and fibrosis (Nppa, Ctgf), immune response (Fgl2), and the conduction system of the heart (Dsc2, Ehd4, Hcn2, Hcn4, Scn4a, Scn4b). All of these genes are expressed on wild-type level in creatine-supplemented mice. Most of the candidate genes (Ctgf, Dsc2, Fbp2, Fgl2, Hcn2, Nppa) reveal significant alterations in a wild-typexa0mouse model of myocardial infarction underlining a pathophysiological relationship between AGAT metabolism and cardiovascular disease, transcriptome profiling and network clusters analysis, overview. In humans, single-nucleotide polymorphisms (SNPs) within the AGAT gene are associated with variations of HA plasma concentrations
malfunction
pharmacological treatment of Becker muscular dystrophy (BMD) patients with metformin or L-citrulline results in antidromic effects on serum hArg and GAA concentrations, seemingly acting as an inhibitor and effector of AGAT activity, respectively
malfunction
-
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
-
metabolism
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
there is little evidence for an essential regulatory role at the level of guanidinoacetate N-methyltransferase (GAMT). Instead, the GATM activity determines the rate of creatine synthesis..Influencing metabolic pathways and fluctuations in the levels of endogenous metabolites by epsilon-lysine (i) causes changes in the content of L-arginine and creatine induced by an enzymatic reaction of glycine amidinotransferase accelerated by epsilon-polylysine, (ii) induces significant upregulation of amino acids (L-phenylalanine, L-tyrosine, L-valine, and L-isoleucine) associated with the nutritional quality of sausages, (iii) downregulates remarkably levels of bile acid-CoA: amino acid N-acyltransferase, glutamate decarboxylase 1, and phenylalanine 4-monooxygenase and increases the content of carnosine dipeptidase 1 and carnosine N-methyltransferase.
metabolism
L-arginine:glycine amidinotransferase (AGAT) is essential for homoarginine (hArg) and guanidinoacetate synthesis, the latter being converted to creatine by guanidinoacetate methyltransferase (GAMT, EC 2.1.1.2). hArg is a weak substrate of NO synthase (NOS) and an inhibitor of arginase
metabolism
effects of amino acids and drugs on AGAT-catalyzed reactions in vivo in humans, 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
-
CyrA is involved in the pathway for biosynthesis of the polyketide-derived hepatotoxin cylindrospermopsin
-
physiological function
homo-L-arginine (hArg) is a non-proteinogenic amino acid that is synthesized by L-arginine:glycine amidinotransferase (AGAT), which is essential for homoarginine (hArg) and guanidinoacetate synthesis
physiological function
L-arginine:glycine amidinotransferase (AGAT, EC: 2.1.4.1) is the common enzyme for endogenous L-homoarginine and creatine formation
physiological function
arginine:glycine amidinotransferase (AGAT) catalyzes mainly two reactions that generate 1. L-homoarginine (hArg) from L-arginine and L-lysine (EC 2.1.4.3) and 2. guanidinoacetate (GAA) and L-ornithine from L-arginine and glycine
additional information
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
-
Biallelic expression of the L-arginine:glycine amidinotransferase gene with different methylation status between male and female primordial germ cells in chickens
additional information
epsilon-polylysine treatment of animal-derived foods as preservation leads to glycine amidinotransferase activity which implicates upregulation of L-arginine and creatine, biochemical mechanism of epsilon-polylysine in goat meat products, analysis of metabolite transformation and protein expression in preservative-added goat meat by metabolomics and proteomics, and mass spectrometry, method, overview. Comparison with common chemical preservative sodium dehydroacetate. As a preservative for goat meat, epsilon-polylysine can improve the nutritional quality of goat meat
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
-
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
-
Show AA Sequence and Transmembrane Helices (1355 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
100000
42000
-
2 * 42000, alpha-transamidinase, SDS-PAGE, 2 * 44000, beta-transamidinase, SDS-PAGE
44000
45680
50120
52000 - 56000
-
wild-type enzyme AT, mutant ATdelta11, mutant ATdeltaM302, gel filtration
44000
-
2 * 42000, alpha-transamidinase, SDS-PAGE, 2 * 44000, beta-transamidinase, SDS-PAGE
45680
2 * 45680, native enzyme, sequence calculation, 2 * 50120, His6-tagged enzyme, sequence calculation
45680
4 * 45680, native enzyme, sequence calculation, 4 * 50120, His6-tagged enzyme, sequence calculation
50120
2 * 45680, native enzyme, sequence calculation, 2 * 50120, His6-tagged enzyme, sequence calculation
50120
4 * 45680, native enzyme, sequence calculation, 4 * 50120, His6-tagged enzyme, sequence calculation
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
tetramer
additional information
dimer
2 * 45680, native enzyme, sequence calculation, 2 * 50120, His6-tagged enzyme, sequence calculation
dimer
-
2 * 45680, native enzyme, sequence calculation, 2 * 50120, His6-tagged enzyme, sequence calculation
-
dimer
-
2 * 42000, alpha-transamidinase, SDS-PAGE, 2 * 44000, beta-transamidinase, SDS-PAGE
tetramer
4 * 45680, native enzyme, sequence calculation, 4 * 50120, His6-tagged enzyme, sequence calculation
tetramer
-
4 * 45680, native enzyme, sequence calculation, 4 * 50120, His6-tagged enzyme, sequence calculation
-
additional information
structure-function-stability relationship, overview
additional information
-
structure-function-stability relationship, overview
-
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant human enzyme, bipyramidal, tetragonal crystals, belonging to space group P4(3)2(1)2, lattice constants a = b = 83.6 A, c = 200.4 A and alpha = beta = gamma = 90°
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
-
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
-
medicine
-
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
additional information
reconstitution of the ornithine cycle with arginine:glycine amidinotransferase to engineer Escherichia coli into an efficient whole-cell catalyst of guanidinoacetate, overview. To alleviate the inhibition of ornithine, a citrulline synthetic module is constructed and optimized by introducing a glutamine self-sufficient system. To improve the pathway from citrulline to arginine, an aspartate self-sufficient system is introduced into the arginine synthetic module. By combining these modules (GAA, citrulline, and arginine synthetic modules), a reconstituted ornithine cycle is developed, which significantly improves the biocatalyst efficiency. In the system, arginine is regenerated efficiently through the reconstituted ornithine cycle, which converts arginine from a substrate to a cofactor for the transamidination reaction, thereby relieving the ornithine inhibition
additional information
-
reconstitution of the ornithine cycle with arginine:glycine amidinotransferase to engineer Escherichia coli into an efficient whole-cell catalyst of guanidinoacetate, overview. To alleviate the inhibition of ornithine, a citrulline synthetic module is constructed and optimized by introducing a glutamine self-sufficient system. To improve the pathway from citrulline to arginine, an aspartate self-sufficient system is introduced into the arginine synthetic module. By combining these modules (GAA, citrulline, and arginine synthetic modules), a reconstituted ornithine cycle is developed, which significantly improves the biocatalyst efficiency (3.9fold increase). In the system, arginine is regenerated efficiently through the reconstituted ornithine cycle, which converts arginine from a substrate to a cofactor for the transamidination reaction, thereby relieving the ornithine inhibition. 8.61 g/l GAA (73.56 mM) with a productivity of 0.39 g/l/h is achieved in a 22 h bioconversion
additional information
-
reconstitution of the ornithine cycle with arginine:glycine amidinotransferase to engineer Escherichia coli into an efficient whole-cell catalyst of guanidinoacetate, overview. To alleviate the inhibition of ornithine, a citrulline synthetic module is constructed and optimized by introducing a glutamine self-sufficient system. To improve the pathway from citrulline to arginine, an aspartate self-sufficient system is introduced into the arginine synthetic module. By combining these modules (GAA, citrulline, and arginine synthetic modules), a reconstituted ornithine cycle is developed, which significantly improves the biocatalyst efficiency (3.9fold increase). In the system, arginine is regenerated efficiently through the reconstituted ornithine cycle, which converts arginine from a substrate to a cofactor for the transamidination reaction, thereby relieving the ornithine inhibition. 8.61 g/l GAA (73.56 mM) with a productivity of 0.39 g/l/h is achieved in a 22 h bioconversion
-
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
reconstitution of the ornithine cycle with arginine:glycine amidinotransferase to engineer Escherichia coli into an efficient whole-cell catalyst of guanidinoacetate, overview. To alleviate the inhibition of ornithine, a citrulline synthetic module is constructed and optimized by introducing a glutamine self-sufficient system. To improve the pathway from citrulline to arginine, an aspartate self-sufficient system is introduced into the arginine synthetic module. By combining these modules (GAA, citrulline, and arginine synthetic modules), a reconstituted ornithine cycle is developed, which significantly improves the biocatalyst efficiency. In the system, arginine is regenerated efficiently through the reconstituted ornithine cycle, which converts arginine from a substrate to a cofactor for the transamidination reaction, thereby relieving the ornithine inhibition
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
-
reconstitution of the ornithine cycle with arginine:glycine amidinotransferase to engineer Escherichia coli into an efficient whole-cell catalyst of guanidinoacetate, overview. To alleviate the inhibition of ornithine, a citrulline synthetic module is constructed and optimized by introducing a glutamine self-sufficient system. To improve the pathway from citrulline to arginine, an aspartate self-sufficient system is introduced into the arginine synthetic module. By combining these modules (GAA, citrulline, and arginine synthetic modules), a reconstituted ornithine cycle is developed, which significantly improves the biocatalyst efficiency. In the system, arginine is regenerated efficiently through the reconstituted ornithine cycle, which converts arginine from a substrate to a cofactor for the transamidination reaction, thereby relieving the ornithine inhibition
-
additional information
identification of a female patient with mutation of AGAT leading to arginine:glycine amidinotransferase (AGAT) deficiency
additional information
analysis of heart transcriptome variation using microarrays in an AGAT-deficient (AGAT-/-) mouse model to evaluate AGAT-, creatine- and HA-dependent gene regulation. significant differences of gene expression are observed between AGAT-/- mutant and wild-type mice, affecting cardiac energy metabolism (Fbp2, Ucp2), cardiac hypertrophy and fibrosis (Nppa, Ctgf), immune response (Fgl2), and the conduction system of the heart (Dsc2, Ehd4, Hcn2, Hcn4, Scn4a, Scn4b). All of these genes are expressed on wild-type level in creatine-supplemented mice. Most of the candidate genes (Ctgf, Dsc2, Fbp2, Fgl2, Hcn2, Nppa) reveal significant alterations in a wild-typexa0mouse model of myocardial infarction underlining a pathophysiological relationship between AGAT metabolism and cardiovascular disease, transcriptome profiling, overview. The single-nucleotide polymorphism (SNP) rs1288775 (AGAT missense), homozygous allele carriers of the minor allele have significantly higher plasma homoarginine levels compared with heterozygous or homozygous allele carriers of the major allele, representing a gene dose-dependent effect
additional information
reconstitution of the ornithine cycle with arginine:glycine amidinotransferase to engineer Escherichia coli into an efficient whole-cell catalyst of guanidinoacetate, overview. To alleviate the inhibition of ornithine, a citrulline synthetic module is constructed and optimized by introducing a glutamine self-sufficient system. To improve the pathway from citrulline to arginine, an aspartate self-sufficient system is introduced into the arginine synthetic module. By combining these modules (GAA, citrulline, and arginine synthetic modules), a reconstituted ornithine cycle is developed, which significantly improves the biocatalyst efficiency (3.9fold increase). In the system, arginine is regenerated efficiently through the reconstituted ornithine cycle, which converts arginine from a substrate to a cofactor for the transamidination reaction, thereby relieving the ornithine inhibition
additional information
reconstitution of the ornithine cycle with arginine:glycine amidinotransferase to engineer Escherichia coli into an efficient whole-cell catalyst of guanidinoacetate, overview. To alleviate the inhibition of ornithine, a citrulline synthetic module is constructed and optimized by introducing a glutamine self-sufficient system. To improve the pathway from citrulline to arginine, an aspartate self-sufficient system is introduced into the arginine synthetic module. By combining these modules (GAA, citrulline, and arginine synthetic modules), a reconstituted ornithine cycle is developed, which significantly improves the biocatalyst efficiency. In the system, arginine is regenerated efficiently through the reconstituted ornithine cycle, which converts arginine from a substrate to a cofactor for the transamidination reaction, thereby relieving the ornithine inhibition
additional information
reconstitution of the ornithine cycle with arginine:glycine amidinotransferase to engineer Escherichia coli into an efficient whole-cell catalyst of guanidinoacetate, overview. To alleviate the inhibition of ornithine, a citrulline synthetic module is constructed and optimized by introducing a glutamine self-sufficient system. To improve the pathway from citrulline to arginine, an aspartate self-sufficient system is introduced into the arginine synthetic module. By combining these modules (GAA, citrulline, and arginine synthetic modules), a reconstituted ornithine cycle is developed, which significantly improves the biocatalyst efficiency. In the system, arginine is regenerated efficiently through the reconstituted ornithine cycle, which converts arginine from a substrate to a cofactor for the transamidination reaction, thereby relieving the ornithine inhibition
additional information
Agat-deficient mice (Agat-/- mice) are characterized by low circulating hArg and creatine concentrations. Agat-/- mice develop significantly larger stroke areas in a temporary middle cerebral artery occlusion model as compared to wild-type littermates. Stroke size is significantly reduced to wild-type size in Agat-/- mice supplemented with hArg, but only slightly in creatine-supplemented animals
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
44.5
an inactivated form of this enzyme retains an appreciable amount of secondary structure elements even on heating to 94°C, but loses its tertiary structure at low temperature of 44.5°C resulting in a state reminiscent of a molten globule. The presence of 500 mm NaCl decreases Tmax at pH 7.5 from 54°C to 49°C
additional information
additional information
inactive CyrA lacks a well-defined tertiary structure at any temperature
additional information
the three mutant variants have lower Tmax values than the wild-type with 54°C compared to 48°C, 51.5°C and 49.5°C for F245N, S247M, and F245N/S247M, respectively
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-18°C, homogenized tissues stored during 1 month without any loss of enzyme activity
-
4°C, purified CyrA, total loss of activity occurs within 48 h despite addition of reducing agents such as dithiothreitol, Tris(2-carboxyethyl) phosphine, or beta-mercaptoethanol
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
2 fractions of enzyme, designated alpha- and beta transamidase individually purified
-
recombinant N-terminal His6-tagged CyrA from Escherichia coli strain BL21(DE3)
recombinant wild-type and mutant N-terminal His6-tagged CyrAs from Escherichia coli strain BL21(DE3) by metal affinity chromatography to over 95% purity
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cDNA, nucleotide sequence determined
cDNA, nucleotide sequence determined, cloned and expressed in Escherichia coli BL21(DE3)-pLysS
for sequencing and synthesizing of RNA probes for in situ hybridizations
gene AGAT, phylogenetic tree, recombinant expression in Escherichia coli strain strain BW25113
gene Agat, quantitative expression analysis, transcriptome profiling, overview
gene cyrA, DNA and amino acid sequence determination and analysis, phylogenetic analysis, overexpression of N-terminal His6-tagged CyrA in Escherichia coli strain BL21(DE3)
gene cyrA, expression of N-terminal His6-tagged CyrA in Escherichia coli strain BL21(DE3)
gene GATM, a differentially methylated region is detected in the eighth intron of the L-arginine:glycine amidinotransferase gene. The methylation in male primordial germ cells of 6-8-days-old embryos is higher than that in female primordial germ cells, genotyping, the GATM gene displays biallelic expression in primordial germ cells as well as somatic embryonic, extraembryonic, and adult chicken tissues, reverse-transcription PCR and quantitative real-time PCR expression analyses, sequence comparisons
cDNA, nucleotide sequence determined, cloned and expressed in Escherichia coli BL21(DE3)-pLysS
cDNA, nucleotide sequence determined, cloned and expressed in Escherichia coli BL21(DE3)-pLysS
gene AGAT, phylogenetic tree, recombinant expression in Escherichia coli strain strain BW25113
gene AGAT, phylogenetic tree, recombinant expression in Escherichia coli strain strain BW25113
-
gene AGAT, phylogenetic tree, recombinant expression in Escherichia coli strain strain BW25113
gene AGAT, phylogenetic tree, recombinant expression in Escherichia coli strain strain BW25113
gene AGAT, phylogenetic tree, recombinant expression in Escherichia coli strain strain BW25113
gene AGAT, phylogenetic tree, recombinant expression in Escherichia coli strain strain BW25113
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
a guanidinoacetate N-methyltransferase deletion (GAMT-/-) causes gene AGAT upregulation
epsilon-polylysine treatment of animal-derived foods as preservation leads to glycine amidinotransferase activity which implicates upregulation of L-arginine and creatine, biochemical mechanism of epsilon-polylysine in goat meat products, analysis of metabolite transformation and protein expression in preservative-added goat meat by metabolomics and proteomics, and mass spectrometry, method, overview
high expression patterns at gastrulation in dorsal region; in embryo high expression in somite and endodermal mass; at larval stage high expression in somites
weak expression in notochord of embryo, in embryo no expression in neural tube and lateral plate mesoderm, weak expression at larval stage in endoderm
a guanidinoacetate N-methyltransferase deletion (GAMT-/-) causes gene AGAT upregulation
a guanidinoacetate N-methyltransferase deletion (GAMT-/-) causes gene AGAT upregulation
-
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
diagnostics
L-homoarginine (HA) is identified as a prognostic factor for cardiovascular disease (CVD)
medicine
medicine
-
presence of the enzyme in serum or urine may prove useful in development of kidney disease diagnosis, hyperornithinemia, an autosomal recessive disease caused by decreased enzyme activity, enzyme activity is also dimished in thyrotoxicosis and myotonic muscular dystrophy
medicine
-
enzyme is a target of the estrogen receptor, is involved in carcinogenesis, mental disorder, osteoporosis and cardiovascular disease
medicine
-
diagnostic tool for biochemical diagnosis of creatine metabolism disorders
medicine
-
diagnosis of AGAT deficiency can be conformed by enzymatic assays in various cell types. The genetic defects can be proven by mutation analysis of the gene involved. Prenatal diagnosis is possible by mutation analysis
medicine
reaggregated brain cell three-dimensional cultures exposed to NH4Cl are used as an experimental model of hyperammonemia in the developing central nervous system
medicine
-
creatine deficiency syndromes, either due to AGAT, GAMT or SLC6A8 deficiencies, lead to a complete absence, or a very strong decrease, of creatine within the brain
medicine
-
creatine deficiency syndromes, either due to AGAT, GAMT or SLC6A8 deficiencies, lead to a complete absence, or a very strong decrease, of creatine within the brain
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Walker, J.B.
Biosynthesis of arginine from canavanine and ornithine in kidney
J. Biol. Chem.
218
549-556
1956
Sus scrofa, no activity in Leuconostoc mesenteroides
brenda
Walker, J.B.
Studies on the mechanism of action of kidney transamidinase
J. Biol. Chem.
224
57-66
1957
Rattus norvegicus, Sus scrofa
brenda
Conconi, F.; Grazi, E.
Transamidinase in hog kidney. I. Purification and properties
J. Biol. Chem.
240
2461-2463
1965
Sus scrofa
brenda
Grazi, E.; Conconi, F.; Vigi, V.
Transamidinase in hog kidney. II. Isolation of a stable enzyme-amidine complex
J. Biol. Chem.
240
2465-2467
1965
Sus scrofa
brenda
Walker, J.B.
Amidinotranferases
The Enzymes, 3rd Ed. (Boyer, P. D. , ed. )
9
497-509
1973
Bos taurus, Canavalia ensiformis, Gallus gallus, Homo sapiens, Lacerta sp., Rana sp., Rattus norvegicus, Sus scrofa
-
brenda
Dubach, U.C.
Transamidinase
Methods Enzym. Anal. , 3rd Ed. (Bergmeyer, H. U. , ed. )
1
740-743
1974
Homo sapiens, Rattus norvegicus, Sus scrofa
-
brenda
McGuire, D.M.; Tormanen, C.D.; Segal, I.S.; Van Pilsum, J.F.
The effect of growth hormone and thyroxine on the amount of L-arginine:glycine amidinotransferase in kidneys of hypophysectomized rats
J. Biol. Chem.
255
1152-1159
1980
Rattus norvegicus, Sus scrofa
brenda
Sipilae, I.
Inhibition of arginine-glycine amidinotransferase by ornithine. A possible mechanism for the muscular and chorioretinal atrophies in gyrate atrophy of the choroid and retina with hyperornithinemia
Biochim. Biophys. Acta
613
79-84
1980
Gallus gallus, Homo sapiens, Rattus norvegicus, Rattus norvegicus Sprague-Dawley, Sus scrofa
brenda
Gross, M.D.; Eggen, M.A.; Simon, A.M.; Van Pilsum, J.F.
The purification and charcterization of human kidney L-arginine:glycine amidinotransferase
Arch. Biochem. Biophys.
251
747-755
1986
Homo sapiens, Rattus norvegicus, Sus scrofa
brenda
Gross, M.D.; Simon, A.M.; Jenny, R.J.; Gray, E.D.; McGuire, D.M.; Van Pilsum, J.F.
Multiple forms of rat kidney L-arginine:glycine amidinotransferase
J. Nutr.
118
1403-1409
1988
Rattus norvegicus
brenda
Raman Rao, S.V.R.; Indira, K.
Effects of guanidine hydrochloride on catalytic efficiency of glycine amidinotransferase of rat
Biochem. Mol. Biol. Int.
29
63-67
1993
Rattus norvegicus, Rattus norvegicus Wistar
brenda
Guthmiller, P.; Van Pilsum, J.F.; Boen, J.R.; McGuire, D.M.
Cloning and sequencing of rat kidney L-arginine:glycine amidinotransferase. Studies on the mechanism of regulation by growth hormone and creatine
J. Biol. Chem.
269
17556-17560
1994
Homo sapiens, Rattus norvegicus, Sus scrofa
brenda
Watanabe, Y.; Van Pilsum, J.F.; Yokoi, I.; Mori, A.
Synthesis of neuroactive guanidino compounds by rat kidney L-arginine:glycine amidinotransferase
Life Sci.
55
351-358
1994
Felis domestica, Homo sapiens, Mus musculus, Oryctolagus cuniculus, Rattus norvegicus, Rattus norvegicus Sprague-Dawley
brenda
Humm, A.; Fritsche, E.; Mann, K.; Goehl, M.; Huber, R.
Recombinant expression and isolation of human L-arginine:glycine amidinotransferase and identification of its active-site cysteine residue
Biochem. J.
322
771-776
1997
Homo sapiens, Homo sapiens (P50440), Rattus norvegicus (P50442), Sus scrofa
-
brenda
Humm, A.; Fritsche, E.; Steinbacher, S.
Structure and reaction mechanism of L-arginine:glycine amidinotransferase
Biol. Chem.
378
193-197
1997
Homo sapiens, Rattus norvegicus, Sus scrofa
brenda
Humm, A.; Fritsche, E.; Steinbacher, S.; Huber, R.
Crystal structure and mechanism of human L-arginine:glycine amidinotransferase: a mitochondrial enzyme involved in creatine biosynthesis
EMBO J.
16
3373-3385
1997
Homo sapiens, Homo sapiens (P50440), Rattus norvegicus, Rattus norvegicus (P50442), Sus scrofa
brenda
Bedekar, A.; Zink, R.M.; Sherman, D.H.; Line, T.V.; Van Pilsum, J.F.
The comparative amino acid sequences, substrate specificities and gene or cDNA nucleotide sequences of some prokaryote and eukaryote amidinotransferases: implications for evolution
Comp. Biochem. Physiol. B
119B
677-690
1998
Homo sapiens, Lampetra planeri, no activity in Streptomyces sp., Rattus norvegicus, Sus scrofa
-
brenda
Fritsche, E.; Humm, A.; Huber, R.
The ligand-induced structural changes of human L-arginine:glycine amidinotransferase. A mutational and crystallographic study
J. Biol. Chem.
274
3026-3032
1999
Homo sapiens
brenda
Zhu, Y.; Evans, M.I.
Estrogen modulates the expression of L-arginine:glycine amidinotransferase in chick liver
Mol. Cell. Biochem.
221
139-145
2001
Gallus gallus, Gallus gallus (Q9I9K9), Homo sapiens, Rana sp., Rattus norvegicus, Sus scrofa
brenda
Carducci, C.; Birarelli, M.; Leuzzi, V.; Carducci, C.; Battini, R.; Cioni, G.; Antonozzi, I.
Guanidinoacetate and creatine plus creatinine assessment in physiologic fluids: an effective diagnostic tool for the biochemical diagnosis of arginine:glycine amidinotransferase and guanidinoacetate methyltransferase deficiencies
Clin. Chem.
48
1772-1778
2002
Homo sapiens
brenda
Lee, G.T.; Kim, W.J.; Cho, Y.D.
Polyamine synthesis in plants. Purification and properties of amidinotransferase from soybean (Glycine max) axes
Phytochemistry
61
781-789
2002
Glycine max
brenda
Verhoeven, N.M.; Schor, D.S.M.; Roos, B.; Battini, R.; Stockler-Ipsiroglu, S.; Salomons, G.S.; Jakobs, C.
Diagnostic enzyme assay that uses stable-isotope-labeled substrates to detect L-arginine: glycine amidinotransferase deficiency
Clin. Chem.
49
803-805
2003
Homo sapiens
brenda
Verhoeven, N.M.; Salomons, G.S.; Jakobs, C.
Laboratory diagnosis of defects of creatine biosynthesis and transport
Clin. Chim. Acta
361
1-9
2005
Homo sapiens
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 (Q0GU46)
brenda
Braissant, O.; Cagnon, L.; Monnet-Tschudi, F.; Speer, O.; Wallimann, T.; Honegger, P.; Henry, H.
Ammonium alters creatine transport and synthesis in a 3D culture of developing brain cells, resulting in secondary cerebral creatine deficiency
Eur. J. Neurosci.
27
1673-1685
2008
Rattus norvegicus (P50442)
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
Mammalia
brenda
Braissant, O.; Bachmann, C.; Henry, H.
Expression and function of AGAT, GAMT and CT1 in the mammalian brain
Subcell. Biochem.
46
67-81
2007
Rattus norvegicus
brenda
Bera, S.; Wallimann, T.; Ray, S.; Ray, M.
Enzymes of creatine biosynthesis, arginine and methionine metabolism in normal and malignant cells
FEBS J.
275
5899-5909
2008
Mus musculus
brenda
Bourdelas, A.; Li, H.Y.; Carron, C.; Shi, D.L.
Dynamic expression pattern of distinct genes in the presomitic and somitic mesoderm during Xenopus development
Int. J. Dev. Biol.
53
1075-1079
2009
Xenopus laevis (Q9IAJ6)
brenda
Brosnan, J.T.; Wijekoon, E.P.; Warford-Woolgar, L.; Trottier, N.L.; Brosnan, M.E.; Brunton, J.A.; Bertolo, R.F.
Creatine synthesis is a major metabolic process in neonatal piglets and has important implications for amino acid metabolism and methyl balance
J. Nutr.
139
1292-1297
2009
Sus scrofa
brenda
Muenchhoff, J.; Siddiqui, K.S.; Poljak, A.; Raftery, M.J.; Barrow, K.D.; Neilan, B.A.
A novel prokaryotic L-arginine:glycine amidinotransferase is involved in cylindrospermopsin biosynthesis
FEBS J.
277
3844-3860
2010
Cylindrospermopsis raciborskii (B0LI36), Cylindrospermopsis raciborskii AWT205 (B0LI36), Cylindrospermopsis raciborskii AWT205
brenda
Muenchhoff, J.; Siddiqui, K.S.; Neilan, B.A.
Identification of two residues essential for the stringent substrate specificity and active site stability of the prokaryotic L-arginine:glycine amidinotransferase CyrA
FEBS J.
279
805-815
2012
Cylindrospermopsis raciborskii (B0LI36), Cylindrospermopsis raciborskii AWT205 (B0LI36)
brenda
Choe, C.U.; Atzler, D.; Wild, P.S.; Carter, A.M.; Boeger, R.H.; Ojeda, F.; Simova, O.; Stockebrand, M.; Lackner, K.; Nabuurs, C.; Marescau, B.; Streichert, T.; Mueller, C.; Lueneburg, N.; De Deyn, P.P.; Benndorf, R.A.; Baldus, S.; Gerloff, C.; Blankenberg, S.; Heerschap, A.; Grant, P.J.; Magnus, T.; Zeller, T.; Isbrandt, D.; Schwedhelm, E.
Homoarginine levels are regulated by L-arginine:glycine amidinotransferase and affect stroke outcome: results from human and murine studies
Circulation
128
1451-1461
2013
Homo sapiens (P50440), Homo sapiens, Mus musculus (Q9D964), Mus musculus, Mus musculus C57BL6 (Q9D964)
brenda
Jang, H.J.; Lee, M.O.; Kim, S.; Kim, T.H.; Kim, S.K.; Song, G.; Womack, J.E.; Han, J.Y.
Biallelic expression of the L-arginine:glycine amidinotransferase gene with different methylation status between male and female primordial germ cells in chickens
Poult. Sci.
92
760-769
2013
Gallus gallus (Q9I9K9), Gallus gallus, Gallus gallus White leghorn (Q9I9K9), Gallus gallus Korean Oge (Q9I9K9)
brenda
Faller, K.M.E.; Atzler, D.; McAndrew, D.J.; Zervou, S.; Whittington, H.J.; Simon, J.N.; Aksentijevic, D.; Ten Hove, M.; Choe, C.U.; Isbrandt, D.; Casadei, B.; Schneider, J.E.; Neubauer, S.; Lygate, C.A.
Impaired cardiac contractile function in arginine glycine amidinotransferase knockout mice devoid of creatine is rescued by homoarginine but not creatine
Cardiovasc. Res.
114
417-430
2018
Mus musculus
brenda
Zhang, Y.; Zhou, H.; Tao, Y.; Lin, B.
Reconstitution of the ornithine cycle with arginine glycine amidinotransferase to engineer Escherichia coli into an efficient whole-cell catalyst of guanidinoacetate
ACS Synth. Biol.
9
2066-2075
2020
Homo sapiens (P50440), Cylindrospermopsis raciborskii (B0LI36), Actinokineospora terrae (A0A1H9NZ58), Micromonospora rifamycinica (A0A120FA53), Moorena producens (A0A1D9G0N3), Amycolatopsis kentuckyensis, Cylindrospermopsis raciborskii AWT205 (B0LI36), Amycolatopsis kentuckyensis B80
brenda
Tsikas, D.
Determination of equilibria constants of arginine glycine amidinotransferase (AGAT)-catalyzed reactions using concentrations of circulating amino acids
Amino Acids
55
203-213
2023
Homo sapiens (P50440)
brenda
Hannemann, J.; Cordts, K.; Seniuk, A.; Choe, C.U.; Schmidt-Hutten, L.; Duque Escobar, J.; Weinberger, F.; Boeger, R.; Schwedhelm, E.
Arginine glycine amidinotransferase is essential for creatine supply in mice during chronic hypoxia
Front. Physiol.
12
703069
2021
Mus musculus (Q9D964)
brenda
Jia, W.; Zhu, J.
Molecular mechanism of epsilon-polylysine treatment of animal-derived foods glycine amidinotransferase activity implicates upregulation of L-arginine and creatine
J. Agric. Food Chem.
71
15106-15120
2023
Capra hircus (A0A452EZU8)
brenda
Finezilber, Y.; Massey, C.; Radley, J.A.; Murphy, E.
Arginine glycine amidinotransferase (AGAT) deficiency an easy-to-miss treatable adult-onset myopathy
Pract. Neurol.
24
413-416
2024
Homo sapiens (P50440)
brenda
Jensen, M.; Mueller, C.; Choe, C.U.; Schwedhelm, E.; Zeller, T.
Analysis of L-arginine glycine amidinotransferase-, creatine- and homoarginine-dependent gene regulation in the murine heart
Sci. Rep.
10
4821
2020
Homo sapiens (P50440)
brenda
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