Guanidinoacetate methyltransferase (GAMT)

1. Guanidinoacetate methyltransferase (GAMT) catalyzes the creatine biosynthesis

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2. Structure of Guanidinoacetate Methyltransferase (GAMT)

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3. Catalytic mechanism based on the crystal structures and site-directed mutagenesis

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4. N-terminus truncated GAMT has weak protein arginine methyltransferase activity

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5. A dimeric structure of the N-terminus truncated GAMT showing a protein arginine methyltransferase complex

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Publications:

● Komoto, J., Huang, Y., Hu, Y., Takata, Y., Konishi, K., Ogawa, H., Gomi, T., Fujioka, M. & Takusagawa, F. (1999). Crystallization and Preliminary X-ray Diffraction Studies of Guanidinoacetate Methyltransferase from Rat Liver. Acta Crystallogr. D55, 1928-1929.

● Komoto, J., Huang, Y., Takata, Y., Yamada, T., Konishi, K., Ogawa, H., Gomi, T., Fujioka, M. & Takusagawa, F. (2002). Crystal Structure of Guanidinoacetate Methyltransferase from Rat Liver: N-Terminus Truncated Enzyme Represents A Ternary Structure of Protein Arginine Methyltransferase. J. Mol. Biol. 320, 223-235.

● Komoto, J., Takata, Y., Yamada, T., Ogawa, H., Gomi, T., Fujioka, M. & Takusagawa, F. (2003). Monoclinic guanidinoacetate methyltransferase and gadolinium ion-binding characteristics. Acta Crystallogr D Biol Crystallogr. 59, 1589-1596.

● Komoto, J., Yamada, T., Takata, Y., Konishi, K., Gomi, T., Ogawa, H., Fujioka, M. & Takusagawa, F. (2004). Catalytic mechanism of guanidinoacetate methyltransferase: Crystal structures of guanidinoacetate methyltransferase ternary complexes. Biochemistry 43,14385-1494.