Gamt cDNA ORF clone, Rattus norvegicus(Norway rat)

Mild guanidinoacetate increase under partial guanidinoacetate methyltransferase deficiency strongly affects brain cell development.
Hanna-El-Daher L, B?ard E, Henry H, Tenenbaum L, Braissant O
Neurobiology of disease7914-27(2015 Jul)

Creatine synthesis and transport during rat embryogenesis: spatiotemporal expression of AGAT, GAMT and CT1.
Braissant O, Henry H, Villard AM, Speer O, Wallimann T, Bachmann C
BMC developmental biology59(2005 May)

Catalytic mechanism of guanidinoacetate methyltransferase: crystal structures of guanidinoacetate methyltransferase ternary complexes.
Komoto J, Yamada T, Takata Y, Konishi K, Ogawa H, Gomi T, Fujioka M, Takusagawa F
Biochemistry43(45)14385-94(2004 Nov)

Severely altered guanidino compound levels, disturbed body weight homeostasis and impaired fertility in a mouse model of guanidinoacetate N-methyltransferase (GAMT) deficiency.
Schmidt A, Marescau B, Boehm EA, Renema WK, Peco R, Das A, Steinfeld R, Chan S, Wallis J, Davidoff M, Ullrich K, Waldsch?tz R, Heerschap A, De Deyn PP, Neubauer S, Isbrandt D
Human molecular genetics13(9)905-21(2004 May)

Monoclinic guanidinoacetate methyltransferase and gadolinium ion-binding characteristics.
Komoto J, Takata Y, Yamada T, Konishi K, Ogawa H, Gomi T, Fujioka M, Takusagawa F
Acta crystallographica. Section D, Biological crystallography59(Pt 9)1589-96(2003 Sep)

3D organotypic brain cell cultures showed that GAMT deficiency with significant residual enzymatic activity does not lead to creatine deficiency but generates sufficient guanidinoacetate to irreversibly affect developing brain
Title: Mild guanidinoacetate increase under partial guanidinoacetate methyltransferase deficiency strongly affects brain cell development.

results suggest that de novo synthesis of creatine(Cr) by AGAT and GAMT, as well as cellular Cr uptake by CT1, are essential during embryonic development
Title: Creatine synthesis and transport during rat embryogenesis: spatiotemporal expression of AGAT, GAMT and CT1.

On the basis of the crystal structure of GAMT-S-adenosyl-L-homocysteine (SAH)+ guanidinoacetate (GAA) and the model structure of GAMT-S-adenosylmethionine (SAM)+ GAA, a possible catalytic mechanism of the methyl transfer reaction of GAMT is proposed.
Title: Catalytic mechanism of guanidinoacetate methyltransferase: crystal structures of guanidinoacetate methyltransferase ternary complexes.

x-ray crstallography studies explain why the Y136F mutant enzyme retains considerable catalytic activity while the Y136V mutant enzyme loses the catalytic activity.
Title: Monoclinic guanidinoacetate methyltransferase and gadolinium ion-binding characteristics.

Crystal structure of guanidinoacetate methyltransferase from rat liver
Title: Crystal structure of guanidinoacetate methyltransferase from rat liver: a model structure of protein arginine methyltransferase.