Biology:Arginyltransferase

From HandWiki
arginyltransferase
Identifiers
EC number2.3.2.8
CAS number37257-24-2
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO

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

L-arginyl-tRNA + protein [math]\displaystyle{ \rightleftharpoons }[/math] 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.

References

  • 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 (4): 731–7. PMID 5416661. 
  • Soffer RL (1973). "Peptide acceptors in the arginine transfer reaction". J. Biol. Chem. 248 (8): 2918–21. PMID 4572514. 
  • "Enzymic modification of proteins. I. General characteristics of the arginine-transfer reaction in rabbit liver cytoplasm". J. Mol. Biol. 43 (1): 163–75. 1969. doi:10.1016/0022-2836(69)90086-2. PMID 5811819.