Information on EC 2.1.4.1 - glycine amidinotransferase

New: Word Map on EC 2.1.4.1
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Mark a special word or phrase in this record:
Search Reference ID:
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)


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

EC NUMBER
COMMENTARY hide
2.1.4.1
-
RECOMMENDED NAME
GeneOntology No.
glycine amidinotransferase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
L-arginine + glycine = L-ornithine + guanidinoacetate
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
amidine group transfer
transamidination
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Arginine and proline metabolism
-
-
creatine biosynthesis
-
-
glycine metabolism
-
-
Glycine, serine and threonine metabolism
-
-
guadinomine B biosynthesis
-
-
Metabolic pathways
-
-
SYSTEMATIC NAME
IUBMB Comments
L-arginine:glycine amidinotransferase
Canavanine can act instead of arginine.
CAS REGISTRY NUMBER
COMMENTARY hide
9027-35-4
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
cow
-
-
Manually annotated by BRENDA team
Jack bean
-
-
Manually annotated by BRENDA team
Felis domestica
cat
-
-
Manually annotated by BRENDA team
soybean
-
-
Manually annotated by BRENDA team
Lacerta sp.
lizard
-
-
Manually annotated by BRENDA team
lamprey
-
-
Manually annotated by BRENDA team
-
-
-
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
rabbit
-
-
Manually annotated by BRENDA team
frog
-
-
Manually annotated by BRENDA team
Rattus norvegicus Sprague-Dawley
strain Sprague-Dawley
-
-
Manually annotated by BRENDA team
strain Wistar
-
-
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
metabolism
physiological function
-
creatine synthesis
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
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 + 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
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 + glycine
guanidinoacetate + canaline
show the reaction diagram
canavanine + hydroxylamine
canaline + hydroxyguanidine
show the reaction diagram
canavanine + ornithine
arginine + canaline
show the reaction diagram
glycine + guanidinoacetate
guanidinoacetate + glycine
show the reaction diagram
guanidinoacetate + canaline
glycine + canavine
show the reaction diagram
guanidinoacetate + glycine
?
show the reaction diagram
guanidinoacetate + hydroxylamine
hydroxyguanidine + glycine
show the reaction diagram
guanidinoacetate + ornithine
glycine + arginine
show the reaction diagram
homoarginine + glycine
homoornithine + guanidinoacetate
show the reaction diagram
hydroxyguanidine + glycine
hydroxylamine + guanidinoacetate
show the reaction diagram
-
-
-
-
?
hydroxylamine + glycine
L-ornithine + hydroxyguanidine
show the reaction diagram
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
L-norvaline + glycine
?
show the reaction diagram
-
-
-
-
?
L-ornithine + guanidinoacetate
L-arginine + glycine
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
L-arginine + glycine
L-ornithine + guanidinoacetate
show the reaction diagram
L-ornithine + guanidinoacetate
L-arginine + glycine
show the reaction diagram
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-thio-6-aminouracil
2-thio-6-oxopurine
2-Thiouracil
2-thiouracil-5-carboxylic acid
5,5'-dithiobis-2-nitrobenzoate
-
-
Creatine
represses enzyme expression
dithiobiuret
glycine
-
inhibits in presence of low amounts of arginine
guanidine hydrochloride
-
-
Hg2+
-
-
HOC3-
-
-
-
L-norvaline
L-ornithine
NH4+
NH4+-induced decrease in creatine and guanidinoacetate probably occurs through inhibition of AGAT enzymatic activity
Ni2+
-
-
ornithine
p-chloromercuribenzoate
thiolhistidine
Zn2+
-
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
cysteine
thiolhistidine
Thiourea
thyroxine
-
induces enzyme expression
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
57.4 - 57.5
3-aminopropionic acid
24.9 - 27.2
4-aminobutyric acid
23.5 - 23.9
5-Aminovaleric acid
1.8 - 14.3
arginine
163 - 450
ethanolamine
0.89 - 18
glycine
3.5
L-arginine
-
pH 8.5, 30C
23 - 23.5
lysine
0.011
ornithine
-
-
392
taurine
-
alpha-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]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
875
glycine
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.25
L-ornithine
-
pH 8.5, 30C
0.253
ornithine
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
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
23.33
-
-
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7
-
recombinant mutant F245N/S247M
7 - 7.5
-
-
7.2
-
-
7.5
-
-
8
-
recombinant mutants F245N and S247M
8.3
-
synthesis of 4-guanidinobutyric acid
8.4
-
synthesis of homoarginine
8.6
-
synthesis of 5-guanidinovaleric acid
9.2
-
synthesis of 3-guanidinopropionic acid, 2-guanidinoethanol and 2-guanidinoethanesulfonic acid
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
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
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
-
recombinant mutant F245N
35
-
recombinant wild-type CyrA and mutant F245N/S247M
40
-
recombinant mutant S247M
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
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
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.1
-
sequence calculation, native enzyme
5.6
-
sequence calculation, His6-tagged enzyme
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
adult brain
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
marginal zone, high level in dorsal region
Manually annotated by BRENDA team
-
developing embryonic brain
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
-
developing embryonic brain
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
-
S180 cells
Manually annotated by BRENDA team
-
developing embryonic brain
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
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
185000
-
tetrameric CyrA, gel filtration
240000
-
-
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
-
-
tetramer
additional information
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
-
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5
-
purified recombinant enzyme, maximally stable at
719453
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
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
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-18C, homogenized tissues stored during 1 month without any loss of enzyme activity
-
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
-
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
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
cDNA clone isolated
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 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)
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
high expression in malignant cells
-
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
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
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
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine