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Information on EC 2.1.4.1 - glycine amidinotransferase and Organism(s) Homo sapiens and UniProt Accession P50440
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2.1.4.1 glycine amidinotransferaseIUBMB Comments
Canavanine can act instead of arginine.
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Word Map
- 2.1.4.1
- creatine
- guanidinoacetate
- homoarginine
-
slc6a8
- harg
- phosphocreatine
- medicine
-
creatine-deficient
-
transamidination
The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
l-arginine:glycine amidinotransferase, glycine amidinotransferase, arginine:glycine amidinotransferase, arginine-glycine amidinotransferase, glycine aminotransferase, arginine-glycine transamidinase, glycine transamidinase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
arginine-glycine amidinotransferase
-
-
-
-
arginine-glycine transamidinase
-
-
-
-
glycine transamidinase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
amidine group transfer
-
-
-
-
transamidination
-
-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
-
-, -, -
SYSTEMATIC NAME
IUBMB Comments
L-arginine:glycine amidinotransferase
Canavanine can act instead of arginine.
CAS REGISTRY NUMBER
COMMENTARY
9027-35-4
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
arginine + 3-aminopropionic acid
3-guanidinopropionic acid + ornithine
-
-
-
-
?
arginine + 4-aminobutyric acid
4-guanidinobutyric acid + ornithine
-
-
-
-
?
arginine + delta-aminovaleric acid
delta-guanidinovaleric acid + ornithine
-
-
-
-
?
arginine + gamma-aminobutyric acid
gamma-guanidinobutyric acid + ornithine
-
-
-
-
?
canavanine + glycine
guanidinoacetate + canaline
-
-
-
-
r
additional information
?
-
-
homoarginine, alpha-amino-gamma-guanidinobutyric acid and alpha-amino-beta-guanidinopropionic acid are not substrates
-
-
?
L-arginine + glycine
L-ornithine + guanidinoacetate
first reaction in the de novo biosynthesis of creatine
-
-
r
L-arginine + glycine
L-ornithine + guanidinoacetate
first reaction in the de novo biosynthesis of creatine
-
-
r
canavanine + ornithine
arginine + canaline
-
-
-
-
r
L-arginine + glycine
L-ornithine + guanidinoacetate
-
-
-
-
r
L-arginine + glycine
L-ornithine + guanidinoacetate
-
-
-
-
r
L-arginine + glycine
L-ornithine + guanidinoacetate
-
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
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
L-arginine + glycine
L-ornithine + guanidinoacetate
first reaction in the de novo biosynthesis of creatine
-
-
r
L-arginine + glycine
L-ornithine + guanidinoacetate
first reaction in the de novo biosynthesis of creatine
-
-
r
L-arginine + glycine
L-ornithine + guanidinoacetate
-
-
-
-
r
L-arginine + glycine
L-ornithine + guanidinoacetate
-
-
-
-
r
L-arginine + glycine
L-ornithine + guanidinoacetate
-
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
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
in vitro assay for enzyme activity based on stable-isotope-labeled substrates L-(guanidino-15N2)arginine and U-(13C,15N)glycine
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
cytosolic enzyme, DDBJ/EMBL/GenBank database, cDNA sequence
SwissProt
mitochondrial enzyme, DDBJ/EMBL/GenBank database, cDNA sequence
SwissProt
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). GATM_HUMAN
423
0
48455
Swiss-Prot
Mitochondrion (Reliability: 2)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
52000 - 56000
-
wild-type enzyme AT, mutant ATdelta11, mutant ATdeltaM302, gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
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°
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
-
in vitro assay for enzyme activity in lymphocytes based on stable-isotope-labeled substrates L-(guanidino-15N2)arginine and U-(13C,15N)glycine
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
cDNA, nucleotide sequence determined, cloned and expressed in Escherichia coli BL21(DE3)-pLysS
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
-
Dubach, U.C.
Transamidinase
Methods Enzym. Anal. , 3rd Ed. (Bergmeyer, H. U. , ed. )
1
740-743
1974
Homo sapiens, Rattus norvegicus, Sus scrofa
-
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
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
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
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
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), Sus scrofa, Rattus norvegicus (P50442)
-
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
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
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
-
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
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
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
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
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
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)
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