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Literature summary for 6.1.1.19 extracted from

  • Vellekamp, G.; Sihag, R.K.; Deutscher, M.P.
    Comparison of the complexed and free forms of rat liver arginyl-tRNA synthetase and origin of the free form (1985), J. Biol. Chem., 260, 9843-9847.
    View publication on PubMed
Search for more literature for 6.1.1.19

Inhibitors

Inhibitors Comment Organism Structure
diphosphate 50% inhibition at 0.033 mM (free enzyme), at 0.040 (complexed enzyme) Rattus norvegicus
KCl 50% inhibition: at 150 mM (free enzyme), at 180 mM (complexed enzyme) Rattus norvegicus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0033
-
 Arg complexed enzyme Rattus norvegicus
0.004
-
 tRNAArg free enzyme Rattus norvegicus
0.0045
-
 Arg free enzyme Rattus norvegicus
0.028
-
 tRNAArg complexed enzyme Rattus norvegicus
0.41
-
 ATP free enzyme Rattus norvegicus
0.43
-
 ATP complexed enzyme Rattus norvegicus

Organism

Organism UniProt Comment Textmining
Rattus norvegicus
-
 enzyme exists as a 72000 MW component of the multienzyme aminoacyl-tRNA synthetase complex or as 60000 MW free enzyme form
-

Source Tissue

Source Tissue Comment Organism Textmining
liver
-
 Rattus norvegicus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + L-arginine + tRNAArg
-
 Rattus norvegicus ?
-
 ?

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
-
 Rattus norvegicus

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
150
-
 KCl free enzyme Rattus norvegicus
180
-
 KCl complexed enzyme Rattus norvegicus