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The taxonomic range for the selected organisms is: Saccharomyces cerevisiae
The enzyme appears in selected viruses and cellular organisms
Synonyms
arginyl-trna synthetase, argrs, rars2, arg-trna synthetase, mtargrs, arginine-trna synthetase, arginyl-transfer rna synthetase, args2, arginine-trna ligase,
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Arginine translase
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Arginine--tRNA ligase
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Arginine-tRNA synthetase
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Arginyl transfer ribonucleic acid synthetase
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Arginyl-transfer RNA synthetase
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Synthetase, arginyl-transfer ribonucleate
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Arginyl-tRNA synthetase
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Arginyl-tRNA synthetase
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ArgRS
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L-arginine:tRNAArg ligase (AMP-forming)
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ATP + L-arginine + tRNAArg
AMP + diphosphate + L-arginyl-tRNAArg
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ATP + L-arginine + tRNAArg
AMP + diphosphate + L-arginyl-tRNAArg
ATP + L-citrulline + tRNACCCG
AMP + diphosphate + L-citryl-tRNACCCG
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9% aminoacylation activity at 0.5 mM and 22% aminoacylation activity at 7.5 mM
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ATP + L-homoarginine + tRNACCCG
AMP + diphosphate + L-homoarginyl-tRNACCCG
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9% aminoacylation activity at 0.5 mM and 37% aminoacylation activity at 7.5 mM
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ATP + NG-methyl-L-arginine + tRNACCCG
AMP + diphosphate + L-arginyl-tRNACCCG
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71% aminoacylation activity at 0.5 mM
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additional information
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NGNG-dimethyl-L-arginine, NGN0G-dimethyl-L-arginine, and NG-nitro-L-arginine cannot be attached to the tRNACCCG by the enzyme
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ATP + L-arginine + tRNAArg
AMP + diphosphate + L-arginyl-tRNAArg
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ATP + L-arginine + tRNAArg
AMP + diphosphate + L-arginyl-tRNAArg
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ATP + L-arginine + tRNAArg
AMP + diphosphate + L-arginyl-tRNAArg
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ATP + L-arginine + tRNAArg
AMP + diphosphate + L-arginyl-tRNAArg
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ATP + L-arginine + tRNAArg
AMP + diphosphate + L-arginyl-tRNAArg
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Arg is 800-8500times more often incorporated into the tRNAArg-C-C-A than noncognate amino acids
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ATP + L-arginine + tRNAArg
AMP + diphosphate + L-arginyl-tRNAArg
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additional information
2-[5-Amino-2-(4-fluoro-phenyl)-6-oxo-6H-pyrimidin-1-yl]-N-(1-benzyl-2-oxo-2-thiazol-2-yl-ethyl)-acetamide
0.011
Arg
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aminoacylation of tRNAArg-C-C-A, Arg
0.022
Arg
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aminoacylation of tRNAArg-C-C-A(3'NH2)
additional information
2-[5-Amino-2-(4-fluoro-phenyl)-6-oxo-6H-pyrimidin-1-yl]-N-(1-benzyl-2-oxo-2-thiazol-2-yl-ethyl)-acetamide
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Km values for different tRNAArg variants
additional information
additional information
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Km values for aminoacylation of various amino acids with tRNAArg-C-C-A and tRNAArg-C-C-A(3'NH2)
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additional information
additional information
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Km values for ATP and L-arginine for 26 mutants
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additional information
additional information
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0.63
Arg
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aminoacylation of tRNAArg-C-C-A(3'NH2)
3.22
Arg
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aminoacylation of tRNAArg-C-C-A
additional information
additional information
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turnover numbers for aminoacylation of various amino acids with tRNAArg-C-C-A and tRNAArg-C-C-A(3'NH2)
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additional information
additional information
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values for different tRNAArg variants
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Uniprot
brenda
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69500
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X-ray diffraction
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monomer
X-ray diffraction
monomer
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X-ray diffraction
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crystallization of a ternary complex formed by arginyl-tRNA synthetase, tRNAArg and L-arginine by the hanging-drop vapour-diffusion method
three different crystal forms crystallized by the hanging-drop vapour-diffusion method
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using the hanging-drop vapour-diffusion method
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additional information
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isolation of 26 mutants by random mutagenesis
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Ni2+-NTA agarose column chromatography
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expression of 26 lethal mutants in Escherichia coli
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Freist, W.; Sternbach, H.; Cramer, F.
Arginyl-tRNA synthetase from yeast. Discrimination between 20 amino acids in aminoacylation of tRNAArg-C-C-A and tRNAArg-C-C-A(3'NH2)
Eur. J. Biochem.
186
535-541
1989
Saccharomyces cerevisiae
brenda
Delagoutte, B.; Keith, G.; Moras, D.; Cavarelli, J.
Crystallization and preliminary X-ray crystallographic analysis of yeast arginyl-tRNA synthetase-yeast tRNAArg complexes
Acta Crystallogr. Sect. D
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492-494
2000
Saccharomyces cerevisiae
brenda
Cavarelli, J.; Delagoutte, B.; Eriani, G.; Gangloff, J.; Moras, D.
L-arginine recognition by yeast arginyl-tRNA synthetase
EMBO J.
17
5438-5448
1998
Saccharomyces cerevisiae
brenda
Delagoutte, B.; Moras, D.; Cavarelli, J.
tRNA aminoacylation by arginyl-tRNA synthetase: induced conformations during substrates binding
EMBO J.
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5599-5610
2000
Saccharomyces cerevisiae (Q05506), Saccharomyces cerevisiae
brenda
Sissler, M.; Giege, R.; Florentz, C.
The RNA sequence context defines the mechanistic routes by which yeast arginyl-tRNA synthetase charges tRNA
RNA
4
647-657
1998
Saccharomyces cerevisiae
brenda
Geslain, R.; Martin, F.; Delagoutte, B.; Cavarelli, J.; Gangloff, J.; Eriani, G.
In vivo selection of lethal mutations reveals two functional domains in arginyl-tRNA synthetase
RNA
6
434-448
2000
Saccharomyces cerevisiae
brenda
Akahoshi, A.; Suzue, Y.; Kitamatsu, M.; Sisido, M.; Ohtsuki, T.
Site-specific incorporation of arginine analogs into proteins using arginyl-tRNA synthetase
Biochem. Biophys. Res. Commun.
414
625-630
2011
Saccharomyces cerevisiae
brenda
6.1.1.19 arginine-tRNA ligase
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