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Literature summary for 6.1.1.19 extracted from

  • Shimada, A.; Nureki, O.; Goto, M.; Takahashi, S.; Yokoyama, S.
    Structural and mutational studies of the recognition of the arginine tRNA-specific major identity element, A20, by arginyl-tRNA synthetase (2001), Proc. Natl. Acad. Sci. USA, 98, 13537-13542.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
overexpression in Escherichia coli of wild type and several mutant enzymes Thermus thermophilus

Crystallization (Commentary)

Crystallization (Comment) Organism
crystal structure solved by multiple isomorphous replacement Thermus thermophilus

Protein Variants

Protein Variants Comment Organism
N79D can use tRNAArg with G20 as substrate Thermus thermophilus
N79E can use tRNAArg with G20 or U20 as substrate Thermus thermophilus
N79K can use tRNAArg with G20 as substrate Thermus thermophilus
N79Q can use tRNAArg with G20 as substrate Thermus thermophilus
N79R can use tRNAArg with G20 or U20 as substrate Thermus thermophilus
Y77A inactive mutant Thermus thermophilus
Y77F slight effect on activity Thermus thermophilus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information Km values for the wild type and mutant enzymes using tRNAArg with different nucleotides at position 20 Thermus thermophilus
0.0098
-
tRNAArg adenine at position 20 of the tRNAArg is required for activity, pH 7.5, 65°C Thermus thermophilus

Organism

Organism UniProt Comment Textmining
Thermus thermophilus Q93RP5
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + L-arginine + tRNAArg
-
Thermus thermophilus AMP + diphosphate + L-arginyl-tRNAArg
-
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