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Literature summary for 6.1.1.19 extracted from

  • Guigou, L.; Shalak, V.; Mirande, M.
    The tRNA-interacting factor p43 associates with mammalian arginyl-tRNA synthetase but does not modify its tRNA aminoacylation properties (2004), Biochemistry, 43, 4592-4600.
    View publication on PubMed
Search for more literature for 6.1.1.19

Cloned(Commentary)

Cloned (Comment) Organism
arginyl tRNA synthetase and an N-terminally truncated derivative with a deletion of the 73 N-terminal amino acids, expression in Escherichia coli Cricetulus sp.

Protein Variants

Protein Variants Comment Organism
DELTA1-73 KM-value for tRNAArg is 1.2fold higher than the wild-type value, turnover number is 1.4fold higher Cricetulus sp.

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.00032
-
 tRNAArg 25°C, pH 7.5, native tRNAArg from beef liver, wild type enzyme Cricetulus sp.
0.00039
-
 tRNAArg 25°C, pH 7.5, native tRNAArg from beef liver, mutant enzyme DELTA1-73 Cricetulus sp.

Organism

Organism UniProt Comment Textmining
Cricetulus sp.
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + L-arginine + tRNAArg
-
 Cricetulus sp. AMP + diphosphate + L-arginyl-tRNAArg
-
 ?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.8
-
 tRNAArg 25°C, pH 7.5, native tRNAArg from beef liver, wild type enzyme Cricetulus sp.
2.6
-
 tRNAArg 25°C, pH 7.5, native tRNAArg from beef liver, mutant enzyme DELTA1-73 Cricetulus sp.