Information on EC 2.1.4.1 - glycine amidinotransferase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY
2.1.4.1
-
RECOMMENDED NAME
GeneOntology No.
glycine amidinotransferase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
L-arginine + glycine = L-ornithine + guanidinoacetate
show the reaction diagram
canavanine can act instead of arginine
-
-
-
L-arginine + glycine = L-ornithine + guanidinoacetate
show the reaction diagram
reaction and kinetic mechanisms, overview
-
L-arginine + glycine = L-ornithine + guanidinoacetate
show the reaction diagram
reaction and kinetic mechanisms, overview
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
amidine group transfer
-
-
-
-
amidine group transfer
Q0GU46
-
amidine group transfer
-
-
amidine group transfer
-
-
transamidination
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
Arginine and proline metabolism
-
creatine biosynthesis
-
Glycine, serine and threonine metabolism
-
Metabolic pathways
-
SYSTEMATIC NAME
IUBMB Comments
L-arginine:glycine amidinotransferase
Canavanine can act instead of arginine.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
AGAT
-
-
AGAT
-
-
AGAT
P50442
-
AGAT
-
-
AGAT
Q9IAJ6
-
arginine-glycine amidinotransferase
-
-
-
-
arginine-glycine transamidinase
-
-
-
-
arginine:glycine amidinotransferase
-
-
arginine:glycine amidinotransferase
-
-
arginine:glycine amidinotransferase
P50442
-
arginine:glycine amidinotransferase
-
-
CyrA
B0LI36
gene name; gene name
-
EC 2.6.2.1
-
-
formerly
-
GAT
Rattus norvegicus Wistar
-
-
-
glycine amidinotransferase
Q0GU46
-
glycine amidinotransferase
-
-
glycine amidinotransferase
-
-
glycine amidinotransferase
P50442
-
glycine aminotransferase
Q9IAJ6
-
glycine transamidinase
-
-
-
-
L-arginine:glycine amidinotransferase
-
-
L-arginine:glycine amidinotransferase
Q9IAJ6
-
CAS REGISTRY NUMBER
COMMENTARY
9027-35-4
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
cow
-
-
Manually annotated by BRENDA team
Felis domestica
cat
-
-
Manually annotated by BRENDA team
cDNA clone, sequence of the chicken AT gene, GenBank
SwissProt
Manually annotated by BRENDA team
chicken; white leghorn
-
-
Manually annotated by BRENDA team
soybean
-
-
Manually annotated by BRENDA team
cytosolic enzyme, DDBJ/EMBL/GenBank database, cDNA sequence; mitochondrial enzyme, DDBJ/EMBL/GenBank database, cDNA sequence
SwissProt
Manually annotated by BRENDA team
Lacerta sp.
lizard
-
-
Manually annotated by BRENDA team
lamprey
-
-
Manually annotated by BRENDA team
mouse
-
-
Manually annotated by BRENDA team
no activity in Leuconostoc mesenteroides
-
-
-
Manually annotated by BRENDA team
no activity in Streptomyces sp.
-
-
-
Manually annotated by BRENDA team
cDNA sequence, EMBL accession number
SwissProt
Manually annotated by BRENDA team
rat; strain Sprague-Dawley
-
-
Manually annotated by BRENDA team
rat; strain Wistar
-
-
Manually annotated by BRENDA team
Rattus norvegicus Sprague-Dawley
strain Sprague-Dawley
-
-
Manually annotated by BRENDA team
Rattus norvegicus Wistar
strain Wistar
-
-
Manually annotated by BRENDA team
7 to 8-d-old piglets, milk from lactating sows
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
evolution
-
CyrA is phylogenetically distinct from other amidinotransferases
evolution
-
CyrA is phylogenetically distinct from other amidinotransferases
-
metabolism
-
CyrA is involved in the pathway for biosynthesis of the polyketide-derived hepatotoxin cylindrospermopsin
physiological function
-
creatine synthesis
metabolism
-
CyrA is involved in the pathway for biosynthesis of the polyketide-derived hepatotoxin cylindrospermopsin
-
additional information
-
ligand-induced conformational changes in wild-type CyrA, structure-function-stability relationship, overview
additional information
-
ligand-induced conformational changes in wild-type CyrA, structure-function-stability relationship, overview
-
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
arginine + 3-aminopropionic acid
3-guanidinopropionic acid + ornithine
show the reaction diagram
-
-
-
-
?
arginine + 3-aminopropionic acid
3-guanidinopropionic acid + ornithine
show the reaction diagram
-
-
-
-
?
arginine + 4-aminobutyric acid
4-guanidinobutyric acid + ornithine
show the reaction diagram
-
-
-
-
?
arginine + 4-aminobutyric acid
4-guanidinobutyric acid + ornithine
show the reaction diagram
-
-
-
-
?
arginine + 4-aminobutyric acid
4-guanidinobutyric acid + ornithine
show the reaction diagram
-
-
-
-
?
arginine + 5-aminovaleric acid
5-guanidinovaleric acid + ornithine
show the reaction diagram
-
-
-
-
?
arginine + delta-aminovaleric acid
delta-guanidinovaleric acid + ornithine
show the reaction diagram
-
-
-
-
?
arginine + ethanolamine
2-guanidinoethanol + ornithine
show the reaction diagram
Homo sapiens, Rattus norvegicus, Oryctolagus cuniculus, Rattus norvegicus Sprague-Dawley
-
-
-
-
?
arginine + gamma-aminobutyric acid
gamma-guanidinobutyric acid + ornithine
show the reaction diagram
-
-
-
-
?
arginine + glycine
?
show the reaction diagram
-
assay at pH 7.4, 37C
-
-
?
arginine + hydroxylamine
ornithine + hydroxyguanidine
show the reaction diagram
-
-
-
-
?
arginine + lysine
homoarginine + ornithine
show the reaction diagram
-
-
-
-
?
arginine + ornithine
ornithine + arginine
show the reaction diagram
-
-
-
-
?
arginine + taurine
2-guanidinoethanesulfonic acid + ornithine
show the reaction diagram
-
-
-
-
?
canavanine + canaline
canaline + canavanine
show the reaction diagram
-
-
-
-
?
canavanine + canaline
canaline + canavanine
show the reaction diagram
-
-
-
-
?
canavanine + canaline
canaline + canavanine
show the reaction diagram
-
-
-
-
?
canavanine + glycine
guanidinoacetate + canaline
show the reaction diagram
-
-
-
-
r
canavanine + glycine
guanidinoacetate + canaline
show the reaction diagram
-
-
-
-
r
canavanine + glycine
guanidinoacetate + canaline
show the reaction diagram
-
-
-
-
r
canavanine + glycine
guanidinoacetate + canaline
show the reaction diagram
Rattus norvegicus Sprague-Dawley
-
-
-
-
r
canavanine + hydroxylamine
canaline + hydroxyguanidine
show the reaction diagram
-
-
-
-
?
canavanine + ornithine
arginine + canaline
show the reaction diagram
-
-
-
-
r
canavanine + ornithine
arginine + canaline
show the reaction diagram
Q9I9K9
-
-
-
r
canavanine + ornithine
arginine + canaline
show the reaction diagram
-
-
-
-
r
canavanine + ornithine
arginine + canaline
show the reaction diagram
-
-
-
-
r
canavanine + ornithine
arginine + canaline
show the reaction diagram
P50440
-
-
-
r
canavanine + ornithine
arginine + canaline
show the reaction diagram
-
-
-
-
r
canavanine + ornithine
arginine + canaline
show the reaction diagram
-
-
-
-
r
canavanine + ornithine
arginine + canaline
show the reaction diagram
-
-
-
-
r
canavanine + ornithine
arginine + canaline
show the reaction diagram
-
-
-
-
r
canavanine + ornithine
arginine + canaline
show the reaction diagram
-
-
-
-
r
canavanine + ornithine
arginine + canaline
show the reaction diagram
-
-
-
-
r
canavanine + ornithine
arginine + canaline
show the reaction diagram
-
-
-
-
r
canavanine + ornithine
arginine + canaline
show the reaction diagram
-
-
-
-
r
canavanine + ornithine
arginine + canaline
show the reaction diagram
Felis domestica
-
-
-
-
r
canavanine + ornithine
arginine + canaline
show the reaction diagram
Lacerta sp.
-
-
-
-
r
canavanine + ornithine
arginine + canaline
show the reaction diagram
-
-
-
-
r
canavanine + ornithine
arginine + canaline
show the reaction diagram
P50442
-
-
-
r
canavanine + ornithine
arginine + canaline
show the reaction diagram
Rattus norvegicus Sprague-Dawley
-
-
-
-
r
canavanine + ornithine
arginine + canaline
show the reaction diagram
Rattus norvegicus Wistar
-
-
-
-
r
glycine + guanidinoacetate
guanidinoacetate + glycine
show the reaction diagram
-
-
-
-
r
guanidinoacetate + canaline
glycine + canavine
show the reaction diagram
-
-
-
-
?
guanidinoacetate + hydroxylamine
hydroxyguanidine + glycine
show the reaction diagram
-
-
-
-
?
guanidinoacetate + hydroxylamine
hydroxyguanidine + glycine
show the reaction diagram
-
-
-
-
?
guanidinoacetate + hydroxylamine
hydroxyguanidine + glycine
show the reaction diagram
-
-
-
-
?
guanidinoacetate + ornithine
glycine + arginine
show the reaction diagram
-
-
-
-
?
guanidinoacetate + ornithine
glycine + arginine
show the reaction diagram
-
-
-
-
?
homoarginine + glycine
homoornithine + guanidinoacetate
show the reaction diagram
-
-
-
-
r
homoarginine + glycine
homoornithine + guanidinoacetate
show the reaction diagram
-
-
-
-
r
homoarginine + glycine
homoornithine + guanidinoacetate
show the reaction diagram
-
-
-
-
r
homoarginine + glycine
homoornithine + guanidinoacetate
show the reaction diagram
Rattus norvegicus Sprague-Dawley
-
-
-
-
r
hydroxyguanidine + glycine
hydroxylamine + guanidinoacetate
show the reaction diagram
-
-
-
-
?
hydroxylamine + glycine
L-ornithine + hydroxyguanidine
show the reaction diagram
B0LI36, -
-
-
-
?
hydroxylamine + glycine
L-ornithine + hydroxyguanidine
show the reaction diagram
B0LI36, -
-
-
-
?
L-alanine + glycine
?
show the reaction diagram
-
-
-
-
?
L-aminobutyric acid + glycine
?
show the reaction diagram
-
-
-
-
?
L-arginine + glycine
L-ornithine + guanidinoacetate
show the reaction diagram
-
-
-
-
r
L-arginine + glycine
L-ornithine + guanidinoacetate
show the reaction diagram
Q9I9K9
-
-
-
r
L-arginine + glycine
L-ornithine + guanidinoacetate
show the reaction diagram
-
-
-
-
?
L-arginine + glycine
L-ornithine + guanidinoacetate
show the reaction diagram
-
-
-
-
r
L-arginine + glycine
L-ornithine + guanidinoacetate
show the reaction diagram
-
-
-
-
r
L-arginine + glycine
L-ornithine + guanidinoacetate
show the reaction diagram
P50440
-
-
-
r
L-arginine + glycine
L-ornithine + guanidinoacetate
show the reaction diagram
-
-
-
-
r
L-arginine + glycine
L-ornithine + guanidinoacetate
show the reaction diagram
-
-
-
-
?
L-arginine + glycine
L-ornithine + guanidinoacetate
show the reaction diagram
-
-
-
-
r
L-arginine + glycine
L-ornithine + guanidinoacetate
show the reaction diagram
-
-
-
-
r
L-arginine + glycine
L-ornithine + guanidinoacetate
show the reaction diagram
-
-
-
-
r
L-arginine + glycine
L-ornithine + guanidinoacetate
show the reaction diagram
-
-
-
-
r
L-arginine + glycine
L-ornithine + guanidinoacetate
show the reaction diagram
-
-
-
-
r
L-arginine + glycine
L-ornithine + guanidinoacetate
show the reaction diagram
-
-
-
-
r
L-arginine + glycine
L-ornithine + guanidinoacetate
show the reaction diagram
Felis domestica
-
-
-
-
r
L-arginine + glycine
L-ornithine + guanidinoacetate
show the reaction diagram
Lacerta sp.
-
-
-
-
r
L-arginine + glycine
L-ornithine + guanidinoacetate
show the reaction diagram
-
-
-
-
r
L-arginine + glycine
L-ornithine + guanidinoacetate
show the reaction diagram
P50442
-
-
-
?
L-arginine + glycine
L-ornithine + guanidinoacetate
show the reaction diagram
Q0GU46
-
-
-
?
L-arginine + glycine
L-ornithine + guanidinoacetate
show the reaction diagram
B0LI36, -
-
-
-
?
L-arginine + glycine
L-ornithine + guanidinoacetate
show the reaction diagram
-
-
-
-
?
L-arginine + glycine
L-ornithine + guanidinoacetate
show the reaction diagram
P50440
first reaction in the de novo biosynthesis of creatine
-
-
r
L-arginine + glycine
L-ornithine + guanidinoacetate
show the reaction diagram
-
first reaction in the de novo biosynthesis of creatine
-
-
r
L-arginine + glycine
L-ornithine + guanidinoacetate
show the reaction diagram
P50442
first reaction in the de novo biosynthesis of creatine
-
-
r
L-arginine + glycine
L-ornithine + guanidinoacetate
show the reaction diagram
-
first reaction in the de novo biosynthesis of creatine
-
-
r
L-arginine + glycine
L-ornithine + guanidinoacetate
show the reaction diagram
-
nitrogen metabolism, putrescine biosynthesis
-
-
r
L-arginine + glycine
L-ornithine + guanidinoacetate
show the reaction diagram
-
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
-
-
?
L-arginine + glycine
L-ornithine + guanidinoacetate
show the reaction diagram
B0LI36, -
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
-
-
?
L-arginine + glycine
L-ornithine + guanidinoacetate
show the reaction diagram
Rattus norvegicus Sprague-Dawley
-
-
-
-
r
L-arginine + glycine
L-ornithine + guanidinoacetate
show the reaction diagram
Rattus norvegicus Wistar
-
-
-
-
r
L-arginine + glycine
L-ornithine + guanidinoacetate
show the reaction diagram
B0LI36, -
-
-
-
?
L-arginine + glycine
L-ornithine + guanidinoacetate
show the reaction diagram
B0LI36, -
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
-
-
?
L-arginine + glycine
L-ornithine + guanidinoacetate
show the reaction diagram
-
-
-
-
?
L-norvaline + glycine
?
show the reaction diagram
-
-
-
-
?
L-ornithine + guanidinoacetate
L-arginine + glycine
show the reaction diagram
-
-
-
-
r
L-ornithine + guanidinoacetate
L-arginine + glycine
show the reaction diagram
Q9I9K9
-
-
-
r
L-ornithine + guanidinoacetate
L-arginine + glycine
show the reaction diagram
-
-
-
-
r
L-ornithine + guanidinoacetate
L-arginine + glycine
show the reaction diagram
-
-
-
-
r
L-ornithine + guanidinoacetate
L-arginine + glycine
show the reaction diagram
P50440
-
-
-
r
L-ornithine + guanidinoacetate
L-arginine + glycine
show the reaction diagram
-
-
-
-
r
L-ornithine + guanidinoacetate
L-arginine + glycine
show the reaction diagram
P50442
-
-
-
r
L-ornithine + guanidinoacetate
L-arginine + glycine
show the reaction diagram
-
-
-
-
r
additional information
?
-
-
L-glutamic acid, L-aspartic acid and histidine are no substrates
-
-
-
additional information
?
-
-
possible amidino group acceptors gamma-aminobutyric acid, beta-alanine, hydroxylamine
-
-
-
additional information
?
-
-
homoarginine, alpha-amino-gamma-guanidinobutyric acid and alpha-amino-beta-guanidinopropionic acid are not substrates
-
-
-
additional information
?
-
-
lysine will not substitute for ornithine
-
-
-
additional information
?
-
B0LI36, -
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
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
Rattus norvegicus Sprague-Dawley
-
L-glutamic acid, L-aspartic acid and histidine are no substrates
-
-
-
additional information
?
-
B0LI36, -
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
-
-
-
additional information
?
-
-
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
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
L-arginine + glycine
L-ornithine + guanidinoacetate
show the reaction diagram
-
-
-
-
r
L-arginine + glycine
L-ornithine + guanidinoacetate
show the reaction diagram
Q9I9K9
-
-
-
r
L-arginine + glycine
L-ornithine + guanidinoacetate
show the reaction diagram
-
-
-
-
?
L-arginine + glycine
L-ornithine + guanidinoacetate
show the reaction diagram
-
-
-
-
r
L-arginine + glycine
L-ornithine + guanidinoacetate
show the reaction diagram
-
-
-
-
r
L-arginine + glycine
L-ornithine + guanidinoacetate
show the reaction diagram
P50440
-
-
-
r
L-arginine + glycine
L-ornithine + guanidinoacetate
show the reaction diagram
-
-
-
-
r
L-arginine + glycine
L-ornithine + guanidinoacetate
show the reaction diagram
-
-
-
-
?
L-arginine + glycine
L-ornithine + guanidinoacetate
show the reaction diagram
-
-
-
-
r
L-arginine + glycine
L-ornithine + guanidinoacetate
show the reaction diagram
-
-
-
-
r
L-arginine + glycine
L-ornithine + guanidinoacetate
show the reaction diagram
-
-
-
-
r
L-arginine + glycine
L-ornithine + guanidinoacetate
show the reaction diagram
-
-
-
-
r
L-arginine + glycine
L-ornithine + guanidinoacetate
show the reaction diagram
-
-
-
-
r
L-arginine + glycine
L-ornithine + guanidinoacetate
show the reaction diagram
-
-
-
-
r
L-arginine + glycine
L-ornithine + guanidinoacetate
show the reaction diagram
Felis domestica
-
-
-
-
r
L-arginine + glycine
L-ornithine + guanidinoacetate
show the reaction diagram
Lacerta sp.
-
-
-
-
r
L-arginine + glycine
L-ornithine + guanidinoacetate
show the reaction diagram
-
-
-
-
r
L-arginine + glycine
L-ornithine + guanidinoacetate
show the reaction diagram
P50442
-
-
-
?
L-arginine + glycine
L-ornithine + guanidinoacetate
show the reaction diagram
Q0GU46
-
-
-
?
L-arginine + glycine
L-ornithine + guanidinoacetate
show the reaction diagram
B0LI36, -
-
-
-
?
L-arginine + glycine
L-ornithine + guanidinoacetate
show the reaction diagram
-
-
-
-
?
L-arginine + glycine
L-ornithine + guanidinoacetate
show the reaction diagram
P50440
first reaction in the de novo biosynthesis of creatine
-
-
r
L-arginine + glycine
L-ornithine + guanidinoacetate
show the reaction diagram
-
first reaction in the de novo biosynthesis of creatine
-
-
r
L-arginine + glycine
L-ornithine + guanidinoacetate
show the reaction diagram
P50442
first reaction in the de novo biosynthesis of creatine
-
-
r
L-arginine + glycine
L-ornithine + guanidinoacetate
show the reaction diagram
-
first reaction in the de novo biosynthesis of creatine
-
-
r
L-arginine + glycine
L-ornithine + guanidinoacetate
show the reaction diagram
-
nitrogen metabolism, putrescine biosynthesis
-
-
r
L-arginine + glycine
L-ornithine + guanidinoacetate
show the reaction diagram
-
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
-
-
?
L-arginine + glycine
L-ornithine + guanidinoacetate
show the reaction diagram
Rattus norvegicus Sprague-Dawley
-
-
-
-
r
L-arginine + glycine
L-ornithine + guanidinoacetate
show the reaction diagram
Rattus norvegicus Wistar
-
-
-
-
r
L-arginine + glycine
L-ornithine + guanidinoacetate
show the reaction diagram
B0LI36, -
-
-
-
?
L-arginine + glycine
L-ornithine + guanidinoacetate
show the reaction diagram
-
-
-
-
?
L-ornithine + guanidinoacetate
L-arginine + glycine
show the reaction diagram
-
-
-
-
r
L-ornithine + guanidinoacetate
L-arginine + glycine
show the reaction diagram
Q9I9K9
-
-
-
r
L-ornithine + guanidinoacetate
L-arginine + glycine
show the reaction diagram
-
-
-
-
r
L-ornithine + guanidinoacetate
L-arginine + glycine
show the reaction diagram
-
-
-
-
r
L-ornithine + guanidinoacetate
L-arginine + glycine
show the reaction diagram
P50440
-
-
-
r
L-ornithine + guanidinoacetate
L-arginine + glycine
show the reaction diagram
-
-
-
-
r
L-ornithine + guanidinoacetate
L-arginine + glycine
show the reaction diagram
P50442
-
-
-
r
L-ornithine + guanidinoacetate
L-arginine + glycine
show the reaction diagram
-
-
-
-
r
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
2-thio-6-aminouracil
-
plus ferricyanide, strong inhibition
2-thio-6-oxopurine
-
plus ferricyanide, strong inhibition
2-Thiouracil
-
plus ferricyanide, strong inhibition
2-thiouracil-5-carboxylic acid
-
plus ferricyanide, strong inhibition
5,5'-dithiobis-2-nitrobenzoate
-
-
CO2
-
in presence of amidino group donor
Creatine
P50440
represses enzyme expression
dithiobiuret
-
plus ferricyanide, strong inhibition
glycine
-
inhibits in presence of low amounts of arginine
guanidine hydrochloride
-
-
HOC3-
-
-
-
L-norvaline
-
good competitive inhibitor
L-ornithine
-
-
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
NH4+
P50442
NH4+-induced decrease in creatine and guanidinoacetate probably occurs through inhibition of AGAT enzymatic activity
ornithine
-
above 1 mg per ml guanidinoacetate-ornithine transamidination is inhibited
ornithine
-
competitive inhibition
ornithine
-
-
ornithine
-
competitive inhibition
p-chloromercuribenzoate
-
-
thiolhistidine
-
plus ferricyanide, strong inhibition
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
cysteine
-
relative activity 103%
thiolhistidine
-
relative activity 102%
Thiourea
-
relative activity 104%
thyroxine
-
induces enzyme expression
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
57.4
-
3-aminopropionic acid
-
alpha-transamidinase
57.5
-
3-aminopropionic acid
-
beta-transamidinase
24.9
-
4-aminobutyric acid
-
beta-transamidinase
27.2
-
4-aminobutyric acid
-
alpha-transamidinase
23.5
-
5-Aminovaleric acid
-
beta-transamidinase
23.9
-
5-Aminovaleric acid
-
alpha-transamidinase
1.8
-
arginine
-
-
2.27
-
arginine
-
-
2.3
-
arginine
-
-
2.4
-
arginine
-
beta-transamidinase
2.5
-
arginine
-
-
2.8
-
arginine
-
alpha-transamidinase
3.8
-
arginine
-
-
9.21
-
arginine
-
-
14
-
arginine
-
-
14.3
-
arginine
-
-
163
-
ethanolamine
-
-
171
-
ethanolamine
-
beta-transamidinase
174
-
ethanolamine
-
alpha-transamidinase
450
-
ethanolamine
-
beta-transamidinase
0.89
-
glycine
-
-
2.3
-
glycine
-
-
2.5
-
glycine
-
-
3
-
glycine
-
alpha-transamidinase
3.1
-
glycine
-
beta-transamidinase
5
-
glycine
-
alpha-and beta-transamidinase
6.9
-
glycine
-
pH 8.5, 30C
18
-
glycine
-
-
3.5
-
L-arginine
-
pH 8.5, 30C
23
-
lysine
-
alpha-transamidinase
0.011
-
ornithine
-
-
392
-
Taurine
-
alpha-transamidinase
23.5
-
lysine
-
beta-transamidinase
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
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
875
-
glycine
-
per active site, pH 8.5, 30C
875
-
L-arginine
-
per active site, pH 8.5, 30C
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.25
-
L-ornithine
-
pH 8.5, 30C
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.0004
-
-
Ehrlich ascites carcinoma cell; sarcoma
0.000485
-
-
S180 cell
0.00097
-
-
kidney of sarcoma-bearing mice
0.00099
-
-
kidney of normal mice
0.211
-
-
kidney
1.057
-
-
pancreas
1.25
-
-
-
23.33
-
-
-
additional information
-
-
specific activity 3400 cpm per mg of protein
additional information
-
-
in vitro assay for enzyme activity based on stable-isotope-labeled substrates L-(guanidino-15N2)arginine and U-(13C,15N)glycine
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
7
7.5
-
-
7
-
-
recombinant mutant F245N/S247M
7.2
-
-
-
7.4
-
-
-
7.4
-
-
synthesis of guanidinoacetic acid
7.4
-
-
assay at
7.4
-
-
assay at
7.5
-
-
-
8
-
-
recombinant mutants F245N and S247M
8.3
-
-
synthesis of 4-guanidinobutyric acid
8.4
-
-
synthesis of homoarginine
8.5
-
-
recombinant wild-type CyrA
8.6
-
-
synthesis of 5-guanidinovaleric acid
9.2
-
-
synthesis of 3-guanidinopropionic acid, 2-guanidinoethanol and 2-guanidinoethanesulfonic acid
9.5
-
-
-
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6
9
-
-
6.2
8.2
-
-
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
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
30
-
-
recombinant mutant F245N
35
-
-
recombinant wild-type CyrA and mutant F245N/S247M
37
-
-
-
37
-
-
assay at
40
-
-
recombinant mutant S247M
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
30
45
-
different optima for wild-type and mutant CyrAs, above 40C activity decreases rapidly for all enzymes, including the S247M variant, which shows 18% of maximal activity at 45C
32
40
-
20% of maximal activity at 40C, maximal activity at 32C
pI VALUE
pI VALUE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5.1
-
-
sequence calculation, native enzyme
5.6
-
-
sequence calculation, His6-tagged enzyme
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
Felis domestica, Oryctolagus cuniculus
-
-
Manually annotated by BRENDA team
Rattus norvegicus Sprague-Dawley
-
;
-
Manually annotated by BRENDA team
-
microcapillary endothelial cell, adult brain
Manually annotated by BRENDA team
-
ependymal epithelium, adult brain, developing embryonic brain
Manually annotated by BRENDA team
-
developing embryonic brain
Manually annotated by BRENDA team
Q9IAJ6
marginal zone, high level in dorsal region
Manually annotated by BRENDA team
-
developing embryonic brain
Manually annotated by BRENDA team
Bos taurus, Lacerta sp.
-
-
Manually annotated by BRENDA team
-
developing embryonic brain
Manually annotated by BRENDA team
Q9IAJ6
hypaxial
Manually annotated by BRENDA team
-
developing embryonic brain
Manually annotated by BRENDA team
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
46000
-
-
preprotein, size predicted from cDNA
52000
56000
-
wild-type enzyme AT, mutant ATdelta11, mutant ATdeltaM302, gel filtration
57000
-
-
in vitro synthesized preprotein, SDS-PAGE
82600
-
-
alpha-transamidinase, sedimentation equilibrium
83000
-
-
gel filtration
83300
-
-
beta-transamidinase, sedimentation equilibrium
89000
-
-
gel filtration, equilibrium sedimentation
89200
-
-
mutant ATDELTA11, calculated molecular mass
90000
-
-
mutant ATDELTAM302, sedimentation analysis
90100
-
-
mutant ATDELTA11, sedimentation analysis
91600
-
-
mutant ATDELTAM302, calculated molecular mass
91800
-
-
wild-type enzyme AT, calculated molecular mass
98000
-
-
dimeric CyrA, gel filtration
100000
-
-
sucrose density gradient sedimentation
100000
-
-
gel filtration
100000
-
-
-
185000
-
-
tetrameric CyrA, gel filtration
240000
-
-
-
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 50000, about, SDS-PAGE
?
-
x * 50000, about, SDS-PAGE
-
dimer
-
2 * 44000, SDS-PAGE
dimer
-
2 * 42000, alpha-transamidinase, SDS-PAGE, 2 * 44000, beta-transamidinase, SDS-PAGE
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
-
tetramer
-
-
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
-
monomer
-
-
additional information
-
structure-function-stability relationship, overview
additional information
-
structure-function-stability relationship, overview
-
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
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
-
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6.5
-
-
purified recombinant enzyme, maximally stable at
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
44.5
-
-
an inactivated form of this enzyme retains an appreciable amount of secondary structure elements even on heating to 94C, but loses its tertiary structure at low temperature of 44.5C resulting in a state reminiscent of a molten globule. The presence of 500 mm NaCl decreases Tmax at pH 7.5 from 54C to 49C
100
-
-
inactivation by incubation for 5 min
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 54C compared to 48C, 51.5C and 49.5C for F245N, S247M, and F245N/S247M, respectively
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
4C, 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
-
-18C, homogenized tissues stored during 1 month without any loss of enzyme activity
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
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
-
2 fractions of enzyme, designated alpha- and beta transamidase individually purified
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
for sequencing and synthesizing of RNA probes for in situ hybridizations
Q0GU46
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)
-
cDNA clone isolated
-, Q9I9K9
cDNA, nucleotide sequence determined, cloned and expressed in Escherichia coli BL21(DE3)-pLysS
P50440
cDNA, nucleotide sequence determined
-
cDNA, nucleotide sequence determined
-
cDNA, nucleotide sequence determined
-
EXPRESSION
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
high expression in malignant cells
-
weak expression in notochord of embryo, in embryo no expression in neural tube and lateral plate mesoderm, weak expression at larval stage in endoderm
Q9IAJ6
high expression patterns at gastrulation in dorsal region; in embryo high expression in somite and endodermal mass; at larval stage high expression in somites
Q9IAJ6
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
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
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
-
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
F245N/S247M
-
site-directed mutagenesis, exchange analogously to the human L-arginine:glycine amidinotransferase, h-AGAT
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
F245N/S247M
-
site-directed mutagenesis, exchange analogously to the human L-arginine:glycine amidinotransferase, h-AGAT
-
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
-
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
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
-
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
P50442
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