The Enzyme Database

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EC 2.1.4.1     
Accepted name: glycine amidinotransferase
Reaction: L-arginine + glycine = L-ornithine + guanidinoacetate
For diagram of creatine biosynthesis, 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.
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. [PMID: 14304853]
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. [PMID: 6766137]
4.  Ratner, S. Transamidination. In: Boyer, P.D., Lardy, H. and Myrbäck, K. (Eds), The Enzymes, 2nd edn, 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. [PMID: 13355454]
6.  Ratner, S. and Rochovansky, O. Biosynthesis of guanidinoacetic acid. II. Mechanism of amidine group transfer. Arch. Biochem. Biophys. 63 (1956) 296–315. [PMID: 13355455]
7.  Walker, J.B. Biosynthesis of arginine from canavanine and ornithine in kidney. J. Biol. Chem. 218 (1956) 549–556. [PMID: 13278360]
8.  Walker, J.B. Studies on the mechanism of action of kidney transamidinase. J. Biol. Chem. 224 (1957) 57–66. [PMID: 13398387]
[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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