Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 2.1.4.1 - glycine amidinotransferase and Organism(s) Mus musculus and UniProt Accession Q9D964

for references in articles please use BRENDA:EC2.1.4.1
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
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.
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Mus musculus
UNIPROT: Q9D964
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
hide
The taxonomic range for the selected organisms is: Mus musculus
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
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
L-arginine:glycine amidinotransferase
-
arginine-glycine amidinotransferase
-
-
-
-
arginine-glycine transamidinase
-
-
-
-
arginine:glycine amidinotransferase
-
-
glycine transamidinase
-
-
-
-
L-arginine:glycine amidinotransferase
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
amidine group transfer
-
-
-
-
transamidination
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
L-arginine:glycine amidinotransferase
Canavanine can act instead of arginine.
CAS REGISTRY NUMBER
COMMENTARY hide
9027-35-4
-
SUBSTRATE
PRODUCT                       
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
-
-
-
?
arginine + glycine
?
show the reaction diagram
-
assay at pH 7.4, 37°C
-
-
?
arginine + taurine
2-guanidinoethanesulfonic acid + ornithine
show the reaction diagram
-
-
-
-
?
canavanine + ornithine
arginine + canaline
show the reaction diagram
-
-
-
-
r
L-arginine + glycine
L-ornithine + guanidinoacetate
show the reaction diagram
NATURAL SUBSTRATE
NATURAL PRODUCT
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-arginine + glycine
L-ornithine + guanidinoacetate
show the reaction diagram
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0004
0.000485
-
S180 cell
0.00097
-
kidney of sarcoma-bearing mice
0.00099
-
kidney of normal mice
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.4
-
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
-
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
S180 cells
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
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
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
physiological function
-
creatine synthesis
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
GATM_MOUSE
423
0
48297
Swiss-Prot
Mitochondrion (Reliability: 2)
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
a guanidinoacetate N-methyltransferase deletion (GAMT-/-) causes gene AGAT upregulation
high expression in malignant cells
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team