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Literature summary extracted from

  • Ciechanover, A.; Ferber, S.; Ganoth, D.; Elias, S.; Avram, H.; Arfin, S.
    Purification and characterization of arginyl-tRNA-protein transferase from rabbit reticulocytes. Its involvement in post-translational modification and degradation of acidic NH2 termini substrates of the ubiquitin pathway (1988), J. Biol. Chem., 263, 11155-11167.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.3.2.8 Di- and tripeptides most potent inhibitor is Glu-Val-Phe, inhibits transfer of arginine to acceptor proteins Oryctolagus cuniculus
2.3.2.8 L-Glu-L-Val-L-Phe
-
 Oryctolagus cuniculus

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.3.2.8 360000
-
 multienzyme complex of several molecules of arginyl-tRNA synthetase and arginyl-tRNA-protein transferase, gel filtration Oryctolagus cuniculus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.3.2.8 L-arginyl-tRNAArg + acceptor protein Oryctolagus cuniculus possibly involved in degradation of proteins with acidic NH2-termini tRNAArg + L-arginyl-[acceptor protein]
-
 ?
2.3.2.8 L-arginyl-tRNAArg + acceptor protein Oryctolagus cuniculus catalyzes post-translational ribosome-independent modification of certain acceptor proteins tRNAArg + L-arginyl-[acceptor protein]
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.3.2.8 Oryctolagus cuniculus
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.3.2.8 partial Oryctolagus cuniculus

Source Tissue

EC Number Source Tissue Comment Organism Textmining
2.3.2.8 reticulocyte
-
 Oryctolagus cuniculus
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
2.3.2.8 0.0047
-
-
 Oryctolagus cuniculus
2.3.2.8 1.3
-
-
 Oryctolagus cuniculus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.3.2.8 L-arginyl-tRNAArg + acceptor protein
-
 Oryctolagus cuniculus tRNAArg + L-arginyl-[acceptor protein]
-
 ?
2.3.2.8 L-arginyl-tRNAArg + acceptor protein possibly involved in degradation of proteins with acidic NH2-termini Oryctolagus cuniculus tRNAArg + L-arginyl-[acceptor protein]
-
 ?
2.3.2.8 L-arginyl-tRNAArg + acceptor protein catalyzes post-translational ribosome-independent modification of certain acceptor proteins Oryctolagus cuniculus tRNAArg + L-arginyl-[acceptor protein]
-
 ?
2.3.2.8 L-arginyl-tRNAArg + albumin from bovine serum Oryctolagus cuniculus tRNAArg + L-arginyl-albumin
-
 ?
2.3.2.8 L-arginyl-tRNAArg + alpha lactalbumin bovine Oryctolagus cuniculus tRNAArg + L-arginyl-[lactalbumin]
-
 ?
2.3.2.8 L-arginyl-tRNAArg + immunoglobulin kappa-light chain of immunoglobulin Oryctolagus cuniculus tRNAArg + L-arginyl-[immunoglobulin]
-
 ?
2.3.2.8 L-arginyl-tRNAArg + trypsin inhibitor from soybean Oryctolagus cuniculus tRNAArg + L-arginyl-[trypsin inhibitor]
-
 ?

Subunits

EC Number Subunits Comment Organism
2.3.2.8 More multienzyme complex of several molecules of arginyl-tRNA synthetase and arginyl-tRNA-protein transferase Oryctolagus cuniculus

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
2.3.2.8 0.02
-
 Glu-Val-Phe
-
 Oryctolagus cuniculus