IUBMB Enzyme Nomenclature

EC 2.1.4.1

Accepted name: glycine amidinotransferase

Reaction: L-arginine + glycine = L-ornithine + guanidinoacetate

For diagram of reaction click here.

Other name(s): arginine-glycine amidinotransferase; arginine-glycine transamidinase; glycine transamidinase

Systematic name: L-arginine:glycine amidinotransferase

Comments: Canavanine can act instead of arginine. Formerly EC 2.6.2.1.

Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, PDB, CAS registry number: 9027-35-4

References:

1. Borsook, H. and Dubnoff, J.W. The formation of glycocyamine in animal tissues. J. Biol. Chem. 138 (1941) 389-403.

2. Conconi, F. and Grazi, E. Transamidinase of hog kidney. I. Purification and properties. J. Biol. Chem. 240 (1965) 2461-2464.

3. McGuire, D.M., Tormanen, C.D., Segal, I.S. and van Pilsum, J.F. The effect of growth hormone and thyroxine on the amount of L-arginine:glycine amidinotransferase in kidneys of hypophysectomized rats, purification and some properties of rat kidney transamidinase. J. Biol. Chem. 255 (1980) 1152-1159.

4. Ratner, S. Transamidination. In: Boyer, P.D., Lardy, H. and Myrbäck, K. (Eds.), The Enzymes, 2nd ed., vol. 6, Academic Press, New York, 1962, pp. 267-275.

5. Ratner, S. and Rochovansky, O. Biosynthesis of guanidinoacetic acid. I. Purification and properties of transamidinase. Arch. Biochem. Biophys. 63 (1956) 277-295.

6. Ratner, S. and Rochovansky, O. Biosynthesis of guanidinoacetic acid. II. Mechanism of amidine group transfer. Arch. Biochem. Biophys. 63 (1956) 296-315.

7. Walker, J.B. Biosynthesis of arginine from canavanine and ornithine in kidney. J. Biol. Chem. 218 (1956) 549-556.

8. Walker, J.B. Studies on the mechanism of action of kidney transamidinase. J. Biol. Chem. 224 (1957) 57-66.

[EC 2.1.4.1 created 1961 as EC 2.6.2.1, transferred 1965 to EC 2.1.4.1]


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