Literature summary for 2.1.4.1 extracted from

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 (2013), Circulation, 128, 1451-1461.

Cloned(Commentary)

Cloned (Comment)	Organism
gene AGAT, recombinant expression in HEK-293 cells	Homo sapiens

Localization	Comment	Organism	GeneOntology No.	Textmining
mitochondrion	-	Homo sapiens	5739	-

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
L-arginine + glycine	Mus musculus	-	L-ornithine + guanidinoacetate	-	?
L-arginine + glycine	Mus musculus C57BL6	-	L-ornithine + guanidinoacetate	-	?

Organism	UniProt	Comment	Textmining
Homo sapiens	P50440	gene AGAT	-
Mus musculus	Q9D964	-	-
Mus musculus C57BL6	Q9D964	-	-

Source Tissue	Comment	Organism	Textmining
brain	-	Homo sapiens	-
brain	-	Mus musculus	-

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
L-arginine + glycine	-	Mus musculus	L-ornithine + guanidinoacetate	-	?
L-arginine + glycine	-	Mus musculus C57BL6	L-ornithine + guanidinoacetate	-	?

Synonyms	Comment	Organism
AGAT	-	Homo sapiens
L-arginine:glycine amidinotransferase	-	Homo sapiens
L-arginine:glycine amidinotransferase	-	Mus musculus

Organism	Comment	Expression
Mus musculus	a guanidinoacetate N-methyltransferase deletion (GAMT-/-) causes gene AGAT upregulation	up

General Information	Comment	Organism
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	Mus musculus
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	Homo sapiens
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	Mus musculus