Arginyltransferase

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In enzymology, an arginyltransferase (EC 2.3.2.8) is an enzyme that catalyzes the chemical reaction

L-arginyl-tRNA + protein $\rightleftharpoons$ tRNA + L-arginyl-protein

Thus, the two substrates of this enzyme are L-arginyl-tRNA and protein, whereas its two products are tRNA and L-arginyl-protein.

This enzyme belongs to the family of transferases, specifically the aminoacyltransferases. The systematic name of this enzyme class is L-arginyl-tRNA:protein arginyltransferase. Other names in common use include arginine transferase, arginyl-transfer ribonucleate-protein aminoacyltransferase, arginyl-transfer ribonucleate-protein transferase, and arginyl-tRNA protein transferase. It has 2 cofactors: mercaptoethanol, and Cation.

[edit] References

IUBMB entry for 2.3.2.8
BRENDA references for 2.3.2.8 (Recommended.)
PubMed references for 2.3.2.8
PubMed Central references for 2.3.2.8
Google Scholar references for 2.3.2.8
Soffer RL (1970). "Enzymatic modification of proteins. II. Purification and properties of the arginyl transfer ribonucleic acid-protein transferase from rabbit liver cytoplasm". J. Biol. Chem. 245: 731–7. PMID 5416661.
Soffer RL (1973). "Peptide acceptors in the arginine transfer reaction". J. Biol. Chem. 248: 2918–21. PMID 4572514.
Soffer RL, Horinishi H (1969). "Enzymic modification of proteins. I. General characteristics of the arginine-transfer reaction in rabbit liver cytoplasm". J. Mol. Biol. 43: 163–75. doi:10.1016/0022-2836(69)90086-2. PMID 5811819.