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Information on EC 6.1.1.19 - arginine-tRNA ligase
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6.1.1.19 arginine-tRNA ligaseSpecify your search results
Word Map
- 6.1.1.19
- aminoacyl-trna
- synthetases
- aminoacylation
-
arginylation
-
anticodon
-
pontocerebellar
-
aarss
-
isoacceptors
- glnrs
-
atp-ppi
-
multisynthetase
- lysyl-trna
- trnaasp
- l-canavanine
- glutaminyl-trna
- aspartyl-trna
-
isoleucyl
- phenylalanyl-trna
-
glutamyl-prolyl-trna
The enzyme appears in viruses and cellular organisms
Synonyms
arginyl-trna synthetase, argrs, rars2, arg-trna synthetase, arginyl-transfer rna synthetase, mtargrs, arginine-trna synthetase, args2, arginine-trna ligase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Arginine translase
-
-
-
-
Arginine--tRNA ligase
-
-
-
-
Arginine-tRNA synthetase
-
-
-
-
Arginyl transfer ribonucleic acid synthetase
-
-
-
-
Arginyl-transfer RNA synthetase
-
-
-
-
Arginyl-tRNA synthetase
arginyltRNA synthetase
ArgRS
ArgS2
RARS
RRS
Synthetase, arginyl-transfer ribonucleate
-
-
-
-
Arginyl-tRNA synthetase
-
-
-
-
ArgRS
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + L-arginine + tRNAArg = AMP + diphosphate + L-arginyl-tRNAArg
simultaneously with the release of AMP or diphosphate an allosteric rearrangement occurs. Cooperative binding of AMP and diphosphate indicates that aminoacylation reaction and backward reaction are concerted
-
ATP + L-arginine + tRNAArg = AMP + diphosphate + L-arginyl-tRNAArg
random ter-ter mechanism, with addition of the three substrates and release of the products in random order
-
ATP + L-arginine + tRNAArg = AMP + diphosphate + L-arginyl-tRNAArg
mechanism includes the formation of an enzyme-bound aminoacyl-adenylate as an intermediate in the first step followed by transfer of the amino acid to tRNA
-
ATP + L-arginine + tRNAArg = AMP + diphosphate + L-arginyl-tRNAArg
random addition of substrates with all steps in rapid equilibrium except for the interconversion of the central quarternary complexes
-
ATP + L-arginine + tRNAArg = AMP + diphosphate + L-arginyl-tRNAArg
rapid equilibrium random ter ter mechanism
-
ATP + L-arginine + tRNAArg = AMP + diphosphate + L-arginyl-tRNAArg
mechanism includes the formation of an enzyme-bound aminoacyl-adenylate as an intermediate in the first step followed by transfer of the amino acid to tRNA
-
-
ATP + L-arginine + tRNAArg = AMP + diphosphate + L-arginyl-tRNAArg
simultaneously with the release of AMP or diphosphate an allosteric rearrangement occurs. Cooperative binding of AMP and diphosphate indicates that aminoacylation reaction and backward reaction are concerted
-
-
ATP + L-arginine + tRNAArg = AMP + diphosphate + L-arginyl-tRNAArg
rapid equilibrium random ter ter mechanism
-
-
ATP + L-arginine + tRNAArg = AMP + diphosphate + L-arginyl-tRNAArg
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Aminoacylation
esterification
-
-
-
-
Aminoacylation
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
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SYSTEMATIC NAME
IUBMB Comments
L-arginine:tRNAArg ligase (AMP-forming)
-
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CAS REGISTRY NUMBER
COMMENTARY
37205-35-9
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2'-deoxyadenosine 5'-triphosphate + L-arginine + tRNAArg
2'-deoxyadenosine 5'-monophosphate + diphosphate + L-arginyl-tRNAArg
2'-O-methyladenosine 5'-triphosphate + L-arginine + tRNAArg
2'-O-methyladenosine 5'-monophosphate + diphosphate + L-arginyl-tRNAArg
-
-
-
-
?
2-chloroadenosine 5'-triphosphate + L-arginine + tRNAArg
2-chloroadenosine 5'-monophosphate + diphosphate + L-arginyl-tRNAArg
-
-
-
-
?
3'-deoxyadenosine 5'-triphosphate + L-arginine + tRNAArg
3'-deoxyadenosine 5'-monophosphate + diphosphate + L-arginyl-tRNAArg
-
-
-
-
?
3'-methoxyadenosine 5'-triphosphate + L-arginine + tRNAArg
3'-methoxyadenosine 5'-monophosphate + diphosphate + L-arginyl-tRNAArg
-
-
-
-
?
3'-O-methyladenosine 5'-triphosphate + L-arginine + tRNAArg
3'-O-methyladenosine 5'-monophosphate + diphosphate + L-arginyl-tRNAArg
-
-
-
-
?
8-azaadenosine 5'-triphosphate + L-arginine + tRNAArg
8-azaadenosine 5'-monophosphate + diphosphate + L-arginyl-tRNAArg
-
-
-
-
?
ATP + L-arginine + tRNAArg
AMP + diphosphate + L-arginyl tRNAArg
-
-
-
?
ATP + L-arginine + tRNAArg ACG
AMP + diphosphate + L-arginyl tRNAArg ACG
tRNA substrate from Escherichia coli
-
-
?
ATP + L-arginine + tRNAArg(ACG)
AMP + diphosphate + L-arginyl-soybean tRNAArg(ACG)
tRNA from Glycine max
-
-
?
ATP + L-citrulline + tRNACCCG
AMP + diphosphate + L-citryl-tRNACCCG
-
9% aminoacylation activity at 0.5 mM and 22% aminoacylation activity at 7.5 mM
-
-
?
ATP + L-homoarginine + tRNACCCG
AMP + diphosphate + L-homoarginyl-tRNACCCG
-
9% aminoacylation activity at 0.5 mM and 37% aminoacylation activity at 7.5 mM
-
-
?
ATP + NG-methyl-L-arginine + tRNACCCG
AMP + diphosphate + L-arginyl-tRNACCCG
-
71% aminoacylation activity at 0.5 mM
-
-
?
formycin 5'-triphosphate + L-arginine + tRNAArg
formycin 5'-monophosphate + diphosphate + L-arginyl-tRNAArg
-
-
-
-
?
tubercidin 5'-triphosphate + L-arginine + tRNAArg
tubercidin 5'-monophosphate + diphosphate + L-arginyl-tRNAArg
2'-deoxyadenosine 5'-triphosphate + L-arginine + tRNAArg
2'-deoxyadenosine 5'-monophosphate + diphosphate + L-arginyl-tRNAArg
-
-
-
-
?
2'-deoxyadenosine 5'-triphosphate + L-arginine + tRNAArg
2'-deoxyadenosine 5'-monophosphate + diphosphate + L-arginyl-tRNAArg
-
-
-
-
?
ATP + L-arginine + tRNAArg
?
-
the complexed enzyme supplies arginyl-tRNA for the protein synthesis
-
-
?
ATP + L-arginine + tRNAArg
AMP + diphosphate + L-arginyl-tRNAArg
-
-
-
?
ATP + L-arginine + tRNAArg
AMP + diphosphate + L-arginyl-tRNAArg
-
-
-
?
ATP + L-arginine + tRNAArg
AMP + diphosphate + L-arginyl-tRNAArg
-
L-arginine is the best substrate
-
-
?
ATP + L-arginine + tRNAArg
AMP + diphosphate + L-arginyl-tRNAArg
-
-
-
?
ATP + L-arginine + tRNAArg
AMP + diphosphate + L-arginyl-tRNAArg
-
-
-
-
?
ATP + L-arginine + tRNAArg
AMP + diphosphate + L-arginyl-tRNAArg
-
-
-
?
ATP + L-arginine + tRNAArg
AMP + diphosphate + L-arginyl-tRNAArg
-
-
-
?
ATP + L-arginine + tRNAArg
AMP + diphosphate + L-arginyl-tRNAArg
-
-
-
?
ATP + L-arginine + tRNAArg
AMP + diphosphate + L-arginyl-tRNAArg
-
-
-
-
?
ATP + L-arginine + tRNAArg
AMP + diphosphate + L-arginyl-tRNAArg
-
-
-
?
ATP + L-arginine + tRNAArg
AMP + diphosphate + L-arginyl-tRNAArg
-
cytidine in position 35 and G or U in position 36 of the tRNAArg are required for ArgRS activity in Escherichia coli
-
?
ATP + L-arginine + tRNAArg
AMP + diphosphate + L-arginyl-tRNAArg
-
-
-
-
?
ATP + L-arginine + tRNAArg
AMP + diphosphate + L-arginyl-tRNAArg
-
-
-
-
?
ATP + L-arginine + tRNAArg
AMP + diphosphate + L-arginyl-tRNAArg
-
-
-
?
ATP + L-arginine + tRNAArg
AMP + diphosphate + L-arginyl-tRNAArg
-
Bacillus stearothermophilus tRNAArg, E. coli tRNAArg and yeast tRNAArg (poor)
-
-
?
ATP + L-arginine + tRNAArg
AMP + diphosphate + L-arginyl-tRNAArg
-
nucleotides other than ATP are not effective
-
-
?
ATP + L-arginine + tRNAArg
AMP + diphosphate + L-arginyl-tRNAArg
-
Bacillus stearothermophilus tRNAArg, E. coli tRNAArg and yeast tRNAArg (poor)
-
-
?
ATP + L-arginine + tRNAArg
AMP + diphosphate + L-arginyl-tRNAArg
-
nucleotides other than ATP are not effective
-
-
?
ATP + L-arginine + tRNAArg
AMP + diphosphate + L-arginyl-tRNAArg
-
-
-
-
?
ATP + L-arginine + tRNAArg
AMP + diphosphate + L-arginyl-tRNAArg
-
-
-
-
?
ATP + L-arginine + tRNAArg
AMP + diphosphate + L-arginyl-tRNAArg
-
-
-
?
ATP + L-arginine + tRNAArg
AMP + diphosphate + L-arginyl-tRNAArg
-
-
-
?
ATP + L-arginine + tRNAArg
AMP + diphosphate + L-arginyl-tRNAArg
-
the C-terminal extension of the human cytosolic leucyl-tRNA synthetase is indispensable for its interaction with the N-terminal of human cytosolic arginyl-tRNA synthetase in the macromolecular complex
-
-
?
ATP + L-arginine + tRNAArg
AMP + diphosphate + L-arginyl-tRNAArg
-
substrate is Escherichia coli tRNAArg
-
-
?
ATP + L-arginine + tRNAArg
AMP + diphosphate + L-arginyl-tRNAArg
-
-
-
-
?
ATP + L-arginine + tRNAArg
AMP + diphosphate + L-arginyl-tRNAArg
-
-
-
?
ATP + L-arginine + tRNAArg
AMP + diphosphate + L-arginyl-tRNAArg
-
-
-
?
ATP + L-arginine + tRNAArg
AMP + diphosphate + L-arginyl-tRNAArg
-
-
-
?
ATP + L-arginine + tRNAArg
AMP + diphosphate + L-arginyl-tRNAArg
-
-
-
?
ATP + L-arginine + tRNAArg
AMP + diphosphate + L-arginyl-tRNAArg
-
-
-
?
ATP + L-arginine + tRNAArg
AMP + diphosphate + L-arginyl-tRNAArg
-
-
-
?
ATP + L-arginine + tRNAArg
AMP + diphosphate + L-arginyl-tRNAArg
-
-
-
-
?
ATP + L-arginine + tRNAArg
AMP + diphosphate + L-arginyl-tRNAArg
-
-
?
ATP + L-arginine + tRNAArg
AMP + diphosphate + L-arginyl-tRNAArg
-
Arg is 800-8500times more often incorporated into the tRNAArg-C-C-A than noncognate amino acids
-
-
?
ATP + L-arginine + tRNAArg
AMP + diphosphate + L-arginyl-tRNAArg
-
-
-
-
?
ATP + L-arginine + tRNAArg
AMP + diphosphate + L-arginyl-tRNAArg
-
r
-
-
?
ATP + L-arginine + tRNAArg
AMP + diphosphate + L-arginyl-tRNAArg
-
recognizes arginine very specifically
-
-
?
ATP + L-arginine + tRNAArg
AMP + diphosphate + L-arginyl-tRNAArg
-
-
-
-
?
ATP + L-arginine + tRNAArg
AMP + diphosphate + L-arginyl-tRNAArg
-
r
-
-
?
ATP + L-arginine + tRNAArg
AMP + diphosphate + L-arginyl-tRNAArg
-
recognizes arginine very specifically
-
-
?
ATP + L-arginine + tRNAArg
AMP + diphosphate + L-arginyl-tRNAArg
-
-
-
?
ATP + L-arginine + tRNAArg
AMP + diphosphate + L-arginyl-tRNAArg
-
-
?
ATP + L-arginine + tRNAArg
AMP + diphosphate + L-arginyl-tRNAArg
-
-
?
ATP + L-arginine + tRNAArg(ACG)
AMP + diphosphate + L-arginyl tRNAArg(ACG)
tRNA from Escherichia coli
-
-
?
ATP + L-arginine + tRNAArg(ACG)
AMP + diphosphate + L-arginyl tRNAArg(ACG)
tRNA from Glycine max
-
-
?
ATP + L-arginine + tRNAArg(ACG)
AMP + diphosphate + L-arginyl-tRNAArg(ACG)
tRNA from Escherichia coli
-
-
?
ATP + L-arginine + tRNAArg(ACG)
AMP + diphosphate + L-arginyl-tRNAArg(ACG)
tRNA from Glycine max
-
-
?
ATP + L-arginine + tRNAArgIII
AMP + diphosphate + L-arginyl-tRNAArgIII
-
-
-
-
?
ATP + L-arginine + tRNAArgIII
AMP + diphosphate + L-arginyl-tRNAArgIII
-
-
-
-
?
ATP + L-canavanine + tRNAArg
AMP + diphosphate + L-canavanyl-tRNAArg
-
-
-
?
ATP + L-canavanine + tRNAArg
AMP + diphosphate + L-canavanyl-tRNAArg
-
about 25% activity compared to L-arginine
-
-
?
ATP + L-canavanine + tRNAArg
AMP + diphosphate + L-canavanyl-tRNAArg
-
-
-
?
ATP + L-thioarginine + tRNAArg
AMP + diphosphate + L-thioarginyl-tRNAArg
-
-
-
?
ATP + L-thioarginine + tRNAArg
AMP + diphosphate + L-thioarginyl-tRNAArg
-
-
-
?
tubercidin 5'-triphosphate + L-arginine + tRNAArg
tubercidin 5'-monophosphate + diphosphate + L-arginyl-tRNAArg
-
-
-
-
?
tubercidin 5'-triphosphate + L-arginine + tRNAArg
tubercidin 5'-monophosphate + diphosphate + L-arginyl-tRNAArg
-
-
-
-
?
tubercidin 5'-triphosphate + L-arginine + tRNAArg
tubercidin 5'-monophosphate + diphosphate + L-arginyl-tRNAArg
-
-
-
-
?
tubercidin 5'-triphosphate + L-arginine + tRNAArg
tubercidin 5'-monophosphate + diphosphate + L-arginyl-tRNAArg
-
-
-
-
?
additional information
?
-
-
the enzyme is unable to accept D-arginine, L-homoarginine, L-citrulline, L-homocitrulline, L-thiocitrulline, L-lysine and L-albizziine (less than 10% activity compared to L-arginine)
-
-
?
additional information
?
-
-
arginine-dependent ATP-diphosphate exchange
-
-
?
additional information
?
-
-
arginine-dependent ATP-diphosphate exchange
-
-
?
additional information
?
-
-
key role in protein synthesis as part of a multienzyme complex
-
-
?
additional information
?
-
-
arginyl-tRNA synthetase, MtArgRS, directly and stably interacts with seryl-tRNA synthetase, MtSerRS, EC 6.1.1.11, two-hybrid system and surface plasmon resonance analysis, overview. The MtSerRS-MtArgRS complex also contains tRNAArg, consistent with the existence of a stable ribonucleoprotein complex active in aminoacylation. Deletion of the HTH motif, which contributes to the stability of SerRS dimers, significantly weakens the interaction between the two synthetases. Stimulation by MtArgRS peaks at 65°C
-
-
?
additional information
?
-
-
the free enzyme provides arginyl-tRNA for the NH2-terminal arginine modification of proteins by arginyl-tRNA:protein arginyltransferase, EC 2.3.2.8
-
-
?
additional information
?
-
-
NGNG-dimethyl-L-arginine, NGN0G-dimethyl-L-arginine, and NG-nitro-L-arginine cannot be attached to the tRNACCCG by the enzyme
-
-
?
additional information
?
-
-
arginine-dependent ATP-diphosphate exchange
-
-
?
additional information
?
-
-
positions 2, 6, 7, 8, and 9 of the purine moiety and 2' and 3' of the sugar moiety of the ATP molecule are important for catalytic action of the aminoacyl-tRNA synthetase
-
-
?
additional information
?
-
-
arginine-dependent ATP-diphosphate exchange
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + L-arginine + tRNAArg
?
-
the complexed enzyme supplies arginyl-tRNA for the protein synthesis
-
-
?
ATP + L-arginine + tRNAArg
AMP + diphosphate + L-arginyl tRNAArg
-
-
-
?
ATP + L-arginine + tRNAArg
AMP + diphosphate + L-arginyl-tRNAArg
-
-
-
?
ATP + L-arginine + tRNAArg
AMP + diphosphate + L-arginyl-tRNAArg
-
-
-
?
ATP + L-arginine + tRNAArg
AMP + diphosphate + L-arginyl-tRNAArg
-
L-arginine is the best substrate
-
-
?
ATP + L-arginine + tRNAArg
AMP + diphosphate + L-arginyl-tRNAArg
-
-
-
-
?
ATP + L-arginine + tRNAArg
AMP + diphosphate + L-arginyl-tRNAArg
-
-
-
?
ATP + L-arginine + tRNAArg
AMP + diphosphate + L-arginyl-tRNAArg
-
-
-
?
ATP + L-arginine + tRNAArg
AMP + diphosphate + L-arginyl-tRNAArg
-
-
-
?
ATP + L-arginine + tRNAArg
AMP + diphosphate + L-arginyl-tRNAArg
-
the C-terminal extension of the human cytosolic leucyl-tRNA synthetase is indispensable for its interaction with the N-terminal of human cytosolic arginyl-tRNA synthetase in the macromolecular complex
-
-
?
ATP + L-arginine + tRNAArg
AMP + diphosphate + L-arginyl-tRNAArg
-
-
-
-
?
ATP + L-arginine + tRNAArg
AMP + diphosphate + L-arginyl-tRNAArg
-
-
-
?
ATP + L-arginine + tRNAArg
AMP + diphosphate + L-arginyl-tRNAArg
-
-
-
?
ATP + L-arginine + tRNAArg
AMP + diphosphate + L-arginyl-tRNAArg
-
-
-
?
ATP + L-arginine + tRNAArg
AMP + diphosphate + L-arginyl-tRNAArg
-
-
-
-
?
additional information
?
-
-
key role in protein synthesis as part of a multienzyme complex
-
-
?
additional information
?
-
-
arginyl-tRNA synthetase, MtArgRS, directly and stably interacts with seryl-tRNA synthetase, MtSerRS, EC 6.1.1.11, two-hybrid system and surface plasmon resonance analysis, overview. The MtSerRS-MtArgRS complex also contains tRNAArg, consistent with the existence of a stable ribonucleoprotein complex active in aminoacylation. Deletion of the HTH motif, which contributes to the stability of SerRS dimers, significantly weakens the interaction between the two synthetases. Stimulation by MtArgRS peaks at 65°C
-
-
?
additional information
?
-
-
the free enzyme provides arginyl-tRNA for the NH2-terminal arginine modification of proteins by arginyl-tRNA:protein arginyltransferase, EC 2.3.2.8
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Co2+
-
CoCl2, complete activation at a concentration of 5 mM in excess of the total ATP concentration, 24% as effective as Mg2+
Fe2+
-
FeCl2, complete activation at a concentration of 5 mM in excess of the total ATP concentration, 29% as effective as Mg2+
Mg2+
Mn2+
-
MnCl2, complete activation at a concentration of 5 mM in excess of the total ATP concentration, 49% as effective as Mg2+
Mg2+
-
MgCl2, complete activation at a concentration of 5 mM in excess of the total ATP concentration
Mg2+
-
MgCl2, optimal concentration in aminoacylation: 7 mM , when ATP concentration is 10 mM
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NaCl
50% inhibition at 100 mM, recombinant HIS-/thioredoxin-tagged enzyme
diphosphate
-
50% inhibition at 0.033 mM (free enzyme), at 0.040 (complexed enzyme)
hemin
-
hemin is a protoporphyrin containing a ferric iron in the center. ArgRS Cys115 acts as a specific axial ligand of hemin binding that is located in the Add1 domain, but hemin binding to Cys115 is not responsible for the inhibition of enzymatic activity. Hemin inhibits the catalytic activity of full-length and N-terminal 72-amino acid-truncated hcArgRSs by blocking amino acid activation. Hemin induces oligomerization of both the isolated Add1 domain and the wild type enzyme, which might account for the inhibition of catalytic activity. Km values for tRNAArg, arginine, and ATP in the presence of hemin are not altered, but kcat values dramatically decrease compared with those in the absence of hemin, kinetic analysis, overview
hemin
hemin induces a dimeric form of the enzyme that is thus rendered enzymatically dead as it is unable to recognize its cognate tRNAarg
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1,2-Diaminoethane
-
supports aminoacylation in presence of crude tRNA not in presence of resolved tRNA
1,2-diaminopropane
-
supports aminoacylation in presence of crude tRNA not in presence of resolved tRNA
1,3-Diamino-2-hydroxypropane
-
supports aminoacylation in presence of crude tRNA not in presence of resolved tRNA
1,3-diaminopropane
-
supports aminoacylation in presence of crude tRNA not in presence of resolved tRNA
polyamines
-
stimulate the formation of arginyl-tRNAArg, the stimulation being more significant at sub-optimal Mg2+ concentrations
-
spermidine
-
supports aminoacylation in presence of crude tRNA not in presence of resolved tRNA
spermine
-
supports aminoacylation in presence of crude tRNA not in presence of resolved tRNA
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
arginine-trna ligase deficiency
Phenotypes and genotypes of mitochondrial aminoacyl-tRNA synthetase deficiencies from a single neurometabolic clinic.
Brain Diseases
A novel mutation in the promoter of RARS2 causes pontocerebellar hypoplasia in two siblings.
Brain Diseases
A patient with pontocerebellar hypoplasia type 6: Novel RARS2 mutations, comparison to previously published patients and clinical distinction from PEHO syndrome.
Brain Diseases
Pontocerebellar hypoplasia type 6 caused by mutations in RARS2: definition of the clinical spectrum and molecular findings in five patients.
Brain Diseases
RARS2 mutations cause early onset epileptic encephalopathy without ponto-cerebellar hypoplasia.
Brain Diseases
RARS2 Mutations: Is Pontocerebellar Hypoplasia Type 6 a Mitochondrial Encephalopathy?
Brain Diseases
[Early onset epileptic encephalopathy caused by mitochondrial arginyl-tRNA synthetase gene deficiency: report of two cases and literature review].
Brain Edema
Knockdown of Arginyl-tRNA Synthetase Attenuates Ischemia-Induced Cerebral Cortex Injury in Rats After Middle Cerebral Artery Occlusion.
Carcinoma, Hepatocellular
Neoplastic transformation-linked alterations in arginyl-tRNA synthetase activity.
Cardiomyopathies
Neuropathologic Characterization of Pontocerebellar Hypoplasia Type 6 Associated With Cardiomyopathy and Hydrops Fetalis and Severe Multisystem Respiratory Chain Deficiency due to Novel RARS2 Mutations.
Drug Resistant Epilepsy
[Early onset epileptic encephalopathy caused by mitochondrial arginyl-tRNA synthetase gene deficiency: report of two cases and literature review].
Epilepsies, Myoclonic
A term neonate with early myoclonic encephalopathy caused by RARS2 gene variants: a case report.
Epilepsies, Myoclonic
Expanding spectrum of RARS2 gene disorders: Myoclonic epilepsy, mental retardation, spasticity, and extrapyramidal features.
Gastroenteritis
Identification of a gamma interferon-activated inhibitor of translation-like RNA motif at the 3' end of the transmissible gastroenteritis coronavirus genome modulating innate immune response.
Hydrops Fetalis
Neuropathologic Characterization of Pontocerebellar Hypoplasia Type 6 Associated With Cardiomyopathy and Hydrops Fetalis and Severe Multisystem Respiratory Chain Deficiency due to Novel RARS2 Mutations.
Infarction, Middle Cerebral Artery
Knockdown of Arginyl-tRNA Synthetase Attenuates Ischemia-Induced Cerebral Cortex Injury in Rats After Middle Cerebral Artery Occlusion.
Intellectual Disability
Expanding spectrum of RARS2 gene disorders: Myoclonic epilepsy, mental retardation, spasticity, and extrapyramidal features.
Intellectual Disability
Novel mutations in WWOX, RARS2, and C10orf2 genes in consanguineous Arab families with intellectual disability.
Ischemic Stroke
Knockdown of Arginyl-tRNA Synthetase Attenuates Ischemia-Induced Cerebral Cortex Injury in Rats After Middle Cerebral Artery Occlusion.
Leukemia, Lymphocytic, Chronic, B-Cell
miR-15a and miR-16-1 down-regulation in pituitary adenomas.
Malaria
Dimerization of Arginyl-tRNA Synthetase by Free Heme Drives Its Inactivation in Plasmodium falciparum.
Microcephaly
A term neonate with early myoclonic encephalopathy caused by RARS2 gene variants: a case report.
Microcephaly
RARS2 mutations cause early onset epileptic encephalopathy without ponto-cerebellar hypoplasia.
Microcephaly
Subdural effusions and lack of early pontocerebellar hypoplasia in siblings with RARS2 mutations.
Microcephaly
[Early onset epileptic encephalopathy caused by mitochondrial arginyl-tRNA synthetase gene deficiency: report of two cases and literature review].
Mitochondrial Diseases
Neuropathologic Characterization of Pontocerebellar Hypoplasia Type 6 Associated With Cardiomyopathy and Hydrops Fetalis and Severe Multisystem Respiratory Chain Deficiency due to Novel RARS2 Mutations.
Mitochondrial Diseases
Novel homozygous RARS2 mutation in two siblings without pontocerebellar hypoplasia - further expansion of the phenotypic spectrum.
Mitochondrial Encephalomyopathies
Cerebellar hypoplasia and brainstem thinning associated with severe white matter and basal ganglia abnormalities in a child with an mtDNA deletion.
Myoclonic Epilepsies, Progressive
Expanding spectrum of RARS2 gene disorders: Myoclonic epilepsy, mental retardation, spasticity, and extrapyramidal features.
nadh:ubiquinone reductase (h+-translocating) deficiency
Mitochondrial disease and epilepsy.
Neurodegenerative Diseases
RARS2 mutations cause early onset epileptic encephalopathy without ponto-cerebellar hypoplasia.
Neurologic Manifestations
Expanding spectrum of RARS2 gene disorders: Myoclonic epilepsy, mental retardation, spasticity, and extrapyramidal features.
pantoate-beta-alanine ligase (amp-forming) deficiency
Phenotypes and genotypes of mitochondrial aminoacyl-tRNA synthetase deficiencies from a single neurometabolic clinic.
Seizures
A term neonate with early myoclonic encephalopathy caused by RARS2 gene variants: a case report.
Seizures
Expanding spectrum of RARS2 gene disorders: Myoclonic epilepsy, mental retardation, spasticity, and extrapyramidal features.
Seizures
Subdural effusions and lack of early pontocerebellar hypoplasia in siblings with RARS2 mutations.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
0.207
ATP
pH 7.5, 30°C, recombinant HIS-/thioredoxin-tagged enzyme
0.501
ATP
-
pH 7.5, 37°C, recombinant, truncated DELTANhcArgRS, absence of hemin
0.529
ATP
-
pH 7.5, 37°C, recombinant, truncated DELTANhcArgRS, presence of hemin
0.001
L-arginine
-
ATP-diphosphate exchange reaction, pH 8, 55°C
0.0022
L-arginine
assay method, aminoacylation of transcript tRNA with [14C]-labelled amino acid
0.003
L-arginine
assay method, aminoacylation of [32P]-labelled transcript tRNA
0.0065
L-arginine
-
pH 7.5, 37°C, recombinant, truncated DELTANhcArgRS, absence of hemin
0.0074
L-arginine
-
ATP-diphosphate exchange reaction, pH 8, 37°C
0.0078
L-arginine
assay method, aminoacylation of [32P]-labelled transcript tRNA
0.0078
L-arginine
-
pH 7.5, 37°C, recombinant, truncated DELTANhcArgRS, presence of hemin
0.0137
L-arginine
-
aminoacylation reaction, 4-fluorotryptophan-labeled enzyme
0.0164
L-arginine
pH 7.5, 30°C, recombinant HIS-/thioredoxin-tagged enzyme
0.0196
L-arginine
assay method, aminoacylation of transcript tRNA with [14C]-labelled amino acid
0.0453
L-canavanine
assay method, aminoacylation of transcript tRNA with [14C]-labelled amino acid
0.0454
L-canavanine
assay method, aminoacylation of [32P]-labelled transcript tRNA
1.32
L-canavanine
assay method, aminoacylation of [32P]-labelled transcript tRNA
0.0002
tRNAArg
-
substrate from E. coli, , ATP-diphosphate exchange, pH 6.0
0.00032
tRNAArg
-
25°C, pH 7.5, native tRNAArg from beef liver, wild type enzyme
0.00039
tRNAArg
-
25°C, pH 7.5, native tRNAArg from beef liver, mutant enzyme DELTA1-73
0.0036
tRNAArg
-
substrate from E. coli, , ATP-diphosphate exchange, pH 7.4
0.00477
tRNAArg
-
pH 7.5, 50°C, recombinant MtArgRS in presence of recombinant MtSerRS
0.0081
tRNAArg
-
pH 7.5, 37°C, recombinant, truncated DELTANhcArgRS, presence of hemin, Escherichia coli tRNAArg
0.0096
tRNAArg
-
pH 7.5, 37°C, recombinant, truncated DELTANhcArgRS, absence of hemin, Escherichia coli tRNAArg
0.0098
tRNAArg
adenine at position 20 of the tRNAArg is required for activity, pH 7.5, 65°C
0.45
tRNAArg
-
25°C, pH 7.5, tRNAArg from Saccharomyces cerevisiae, aminoacylation
0.00184
tRNAArg ACG
pH 7.5, 30°C, recombinant HIS-/thioredoxin-tagged enzyme
-
0.00029
tRNAArg(ACG)
tRNA from Escherichia coli, pH and temperature not specified in the publication
-
0.0014
tRNAArg(ACG)
tRNA from Glycine max, pH and temperature not specified in the publication
-
0.0017
tRNAArg(ACG)
tRNA from Glycine max, pH and temperature not specified in the publication
-
0.0022
tRNAArg(ACG)
tRNA from Escherichia coli, pH and temperature not specified in the publication
-
0.0024
tRNAArg(ACG)
tRNA from Escherichia coli, pH and temperature not specified in the publication
-
0.0041
tRNAArg(ACG)
tRNA from Glycine max. pH and temperature not specified in the publication
-
0.2
tubercidin 5'-triphosphate
-
formycin 5'-triphosphate, 2'-deoxyadenosine 5'-triphosphate, 3'-O-methyladenosine 5'-triphosphate
0.4
tubercidin 5'-triphosphate
-
3'-methoxyadenosine 5'-triphosphate, , NTP-diphosphate exchange
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
-
Km values for different tRNAArg variants
additional information
additional information
-
Km values for aminoacylation of various amino acids with tRNAArg-C-C-A and tRNAArg-C-C-A(3'NH2)
-
additional information
additional information
-
effect on the Km of several variations of the tRNAArg sequence
-
additional information
additional information
-
Km values for ATP and L-arginine for 26 mutants
-
additional information
additional information
-
Km values for ATP and L-arginine for several mutants and revertants
-
additional information
additional information
Km values for the wild type and mutant enzymes using tRNAArg with different nucleotides at position 20
-
additional information
additional information
-
Km values for the wild type and mutant enzymes using tRNAArg with different nucleotides at position 20
-
additional information
additional information
-
addition of MtArgRS to MtSerRS leads to an almost 4fold increase in the catalytic efficiency of serine attachment to tRNA, also under conditions of elevated temperature and osmolarity, but has no effect on the activity of MtArgRS, steady-state kinetic analyses, overview
-
additional information
additional information
-
Km values for tRNAArg, arginine, and ATP in the presence of hemin are not altered, but kcat values dramatically decrease compared with those in the absence of hemin, kinetic analysis, overview
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.215
L-arginine
pH 7.5, 30°C, recombinant HIS-/thioredoxin-tagged enzyme
3.8
L-arginine
-
pH 7.5, 37°C, recombinant, truncated DELTANhcArgRS, presence of hemin
17.9
L-arginine
-
pH 7.5, 37°C, recombinant, truncated DELTANhcArgRS, absence of hemin
0.0045
tRNAArg
-
25°C, pH 7.5, tRNAArg from Saccharomyces cerevisiae, aminoacylation
0.034
tRNAArg
-
pH 7.5, 50°C, recombinant MtArgRS in presence of recombinant MtSerRS
2.5
tRNAArg
-
pH 7.5, 37°C, recombinant, truncated DELTANhcArgRS, presence of hemin, Escherichia coli tRNAArg
2.6
tRNAArg
-
25°C, pH 7.5, native tRNAArg from beef liver, mutant enzyme DELTA1-73
16.5
tRNAArg
-
pH 7.5, 37°C, recombinant, truncated DELTANhcArgRS, absence of hemin, Escherichia coli tRNAArg
0.0017
tRNAArg(ACG)
tRNA from Escherichia coli, pH and temperature not specified in the publication
-
0.02
tRNAArg(ACG)
tRNA from Glycine max. pH and temperature not specified in the publication
-
0.03
tRNAArg(ACG)
tRNA from Escherichia coli, pH and temperature not specified in the publication
-
0.04
tRNAArg(ACG)
tRNA from Glycine max, pH and temperature not specified in the publication
-
0.055
tRNAArg(ACG)
tRNA from Escherichia coli, pH and temperature not specified in the publication
-
0.105
tRNAArg(ACG)
tRNA from Glycine max, pH and temperature not specified in the publication
-
additional information
additional information
-
turnover numbers for aminoacylation of various amino acids with tRNAArg-C-C-A and tRNAArg-C-C-A(3'NH2)
-
additional information
additional information
-
effect on the turnover number of several variations of the tRNAArg sequence
-
additional information
additional information
-
values for ATP and L-arginine for several mutants and revertants
-
additional information
additional information
-
values for different tRNAArg variants
-
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
500
L-arginine
-
pH 7.5, 37°C, recombinant, truncated DELTANhcArgRS, presence of hemin
2800
L-arginine
-
pH 7.5, 37°C, recombinant, truncated DELTANhcArgRS, absence of hemin
300
tRNAArg
-
pH 7.5, 37°C, recombinant, truncated DELTANhcArgRS, presence of hemin, Escherichia coli tRNAArg
1700
tRNAArg
-
pH 7.5, 37°C, recombinant, truncated DELTANhcArgRS, absence of hemin, Escherichia coli tRNAArg
4.8
tRNAArg(ACG)
tRNA from Glycine max. pH and temperature not specified in the publication
-
5.5
tRNAArg(ACG)
tRNA from Escherichia coli, pH and temperature not specified in the publication
-
14
tRNAArg(ACG)
tRNA from Escherichia coli, pH and temperature not specified in the publication
-
22.7
tRNAArg(ACG)
tRNA from Glycine max, pH and temperature not specified in the publication
-
25.2
tRNAArg(ACG)
tRNA from Escherichia coli, pH and temperature not specified in the publication
-
75
tRNAArg(ACG)
tRNA from Glycine max, pH and temperature not specified in the publication
-
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
activity of recombinant tagged and detagged enzyme
additional information
-
activity of recombinant tagged and detagged enzyme
additional information
-
incorporation of 4-fluorotryptophan has little effect on activity
additional information
-
mutant W162A displays 23% of the activity compared to the native enzyme
additional information
-
recombinant enzyme tagged with 10 tandem histidine residues at the N-terminus exhibits similar activity than the wild type enzyme, C-terminal tag inactivates the enzyme
additional information
-
comparison of aminoacylation activity of Escherichia coli ArgRS and human truncated DELTANhcArgRS in presence of hemin, overview
additional information
-
K116G mutant displays very low activity compared to wild type enzyme
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
55
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
35
-
35°C: about 50% of maximal activity, 70°C: rapid drop of activity above
additional information
additional information
-
tRNA protects from heat inactivation above 1 mg/ml
additional information
-
Arg and tRNA show synergistic protection at Arg concentrations of 0.1 mM or more, the presence of ATP is absolutely required to induce synergistic protection at lower Arg concentrations
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
enzyme exists as a high MW component of the multienzyme aminoacyl-tRNA synthetase complex and a low MW free enzyme
-
-
brenda
-
263, 269, 270, 275, 276, 280, 285, 649631, 649854, 650287, 651112, 653023, 671281, 672397, 701542, 702060
-
-
brenda
2 mutant enzymes with reduced affinity for Arg, a mutant with reduced affinity for arginine-tRNAArg and reduced aminoacylation in vivo for two of the five isoaccepting species of tRNAArg
-
-
brenda
enzyme exists as a 72000 MW component of the multienzyme aminoacyl-tRNA synthetase complex or as 60000 MW free enzyme form
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
physiological function
the rrt-1 gene, encoding arginyl-tRNA synthetase, acutely controls hypoxic sensitivity
physiological function
-
the free form of human cytoplasmic arginyl-tRNA synthetase participates in ubiquitin-dependent protein degradation by offering arginyl-tRNAArg to arginyl-tRNA transferase, ATE1, overview
physiological function
-
the enzyme participates in conferring L-canavanine resistance
physiological function
the mRNA encoding the N-terminal extension region of the enzyme has the capacity to independently recruit the E. coli ribosome
Show AA Sequence and Transmembrane Helices (54070 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
43000
-
x * 43000 (alpha, catalytic subunit) + x * 78000, (beta, exhibits no significant activity), SDS-PAGE
58000
60000
64700
-
x * 64700, mitochondrial enzyme, calculated from amino acid sequence
72000
76700
-
x * 76700, cytoplasmic enzyme, calculated from amino acid sequence
78000
-
x * 43000 (alpha, catalytic subunit) + x * 78000, (beta, exhibits no significant activity), SDS-PAGE
72000
-
x * 72000, component of the multienzyme aminoacyl-tRNA synthetase complex, the 12000 MW NH2-terminal extension makes this form much more hydrophobic than the smaller one, SDS-PAGE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
additional information
?
-
x * 64700, mitochondrial enzyme, calculated from amino acid sequence
?
-
x * 43000 (alpha, catalytic subunit) + x * 78000, (beta, exhibits no significant activity), SDS-PAGE
?
-
x * 72000, component of the multienzyme aminoacyl-tRNA synthetase complex, the 12000 MW NH2-terminal extension makes this form much more hydrophobic than the smaller one, SDS-PAGE
additional information
-
cognate tRNA induces dimerization
-
additional information
-
enzyme is part of a high molecular mass aminoacyl-tRNA synthetase complex, which has a coherent structure that can be visualized by electron microscopy
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
lipoprotein
-
high molecular weight aminoacyl-tRNA synthetase complex contains lipid. Delipidation does not affect the size or activity of the complex, but a variety of functional and structural properties of individual synthetases in the complex are altered: sensitivity to salts plus detergents, temperature inactivation, hydrophobicity, sensitivity to protease digestion
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapour diffusion method in complex form with tRNAArg at pH 5.6 using ammonium sulfate as a precipitating agent
-
sitting drop vapor diffusion method, using 50 mM HEPES (pH 7.2), 100 mM sodium acetate, 22% (w/v) PEG 3350
apo, L-arginine-complexed, and L-canavanine-complexed forms of the cytoplasmic free enzyme isoform, hanging drop vapor diffusion method, using 0.085 mM sodium citrate tribasic dehydrate (pH 5.7), 24% (w/v) polyethylene glycol 4000, 0.17 M ammonium acetate, and 15% (v/v) glycerol
multisynthetase complex subcomplex comprising arginyl-tRNA synthetase, glutaminyl-tRNA synthetase, and the auxiliary factor aminoacyl tRNA synthetase complex-interacting multifunctional protein 1, hanging drop vapor diffusion method, using 5-10% (w/v) methylpentenediol, 0.1 M Tris HCl (pH 7.4), 0.2 M NaCl
a crystal structure of a complex of Arg-tRNA synthetase, tRNAArgCCU, and the ATP analog ANP is determined to 2.0 A resolution
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
-
crystallized by the hanging-drop vapour-diffusion method using ethylene glycol as precipitant
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C599Y
-
expression in Saccharomices cerevisiae, shows reduced activity and stability
DELTA1-73
-
KM-value for tRNAArg is 1.2fold higher than the wild-type value, turnover number is 1.4fold higher
argS MA5002
-
mutant argS MA5002 differs from the wild-type ArgRS structural gene by one mutation, a substitution of an Arg by a Ser at position 134. It exhibits a 4times to 6times as low activity and a 5times as high Km value for ATP as the wild-type enzyme in aminoacylation and ATP-diphosphate exchange, Km values for Arg and tRNAArg remain unaltered
M460V
-
mutant cannot suppress the effect of the expression of FTOR126, a variant of the wild type tRNAArg
Y313A
the mutation results in a merely 2fold reduction in binding affinity
Y524D
-
mutant cannot suppress the effect of the expression of FTOR126, a variant of the wild type tRNAArg
DELTANhcArgRS
-
N-terminal 72-amino acid deletion mutant with higher specific activity than the wild type enzyme
RARSL
-
the RARSL mutation in the mitochondrial arginyltRNA synthetase gene is associated with pontocerebellar hypoplasia
additional information
additional information
-
2 mutant enzymes with reduced affinity for Arg, one mutant with reduced affinity for arginine-tRNAArg and reduced aminoacylation in vivo for two of the five isoaccepting species of tRNAArg
additional information
-
biosynthetic preparation of an enzyme where Trp are replaced by 4-fluorotryptophane
additional information
-
isolation of 26 mutants by random mutagenesis
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
74.5
-
50% inactivation, when the temperature is raised gradually at the rate of 1°C/min
additional information
-
tRNA reduces thermal inactivation, reduced glutathione effectively protects the enzyme from thermal inactivation, zinc or Triton X-100 increases thermal inactivation
37
-
20 min, 25% loss of activity of high MW form, 50% loss of activity of low MW form
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
degradation of the enzyme during purification may be due to the influence of the immobilized tRNA, and is enhanced by high salt concentrations
-
presence of ribosomes or of high concentrations of albumin oppose the conformational change of arginyl-tRNA synthetase which results in a loss of activity when the enzyme is incubated at low concentrations
-
reduced glutathione effectively protects the enzyme from thermal inactivation
-
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
affinity column chromatography, ion-exchange column chromatography, and Superdex 200 gel filtration
DEAE-Sepharose CL-6B column chromatography, hydroxylapatite chromatography, Sepharose CL-2B column chromatography, and Sephacryl S-300 gel filtration
-
Ni-NTA column chromatography and Source15Q column chromatography
Ni-NTA Superflow resin chromatography and dialysis against 20 mM potassium phosphate buffer (pH 7.5)
-
Ni2+ column chromatography, Mono-Q column chromatography, and Superdex 200 gel filtration
Ni2+-NTA affinity resin column chromatography and Superdex 200 gel filtration
on a Ni2+-nitrilotriacetic superflow, a Resource Q, a Hitrap heparin, and a hydroxyapatite column
partial purification of recombinant enzymes using DEAE-Sepharose and Blue-Sepharose column chromatography
-
purification of a His-tagged recombinant enzyme using Ni-nitrilotriacetic acid agarose affinity chromatography
-
purification of the native and mutant enzymes expressed in Saccharomices cerevisiae, using Q-Sepharose and S-Sepharose chromatography
-
purification of the wild type and K116G mutant, expressed in Escherichia coli, by DEAE-Sephacel and PhenylSuperose column chromatography
-
recombinant GST-tagged MtArgRS from Escherichia coli strain BL21(DE3) by glutathione affinity chromatograophy. GST-MtArgRS shows the ability to co-purify with His-tagged MtSerRS by nickel affinity chromatography, co-elution of the two enzymes during gel filtration
-
recombinant His-tagged wild-type full-length and truncated mutant enzymes from Escherichia coli strain BL21-CodonPlus (DE3)-RIL by nickel affinity chromatography and gel filtration
-
soluble recombinant N-terminally HIS-/thioredoxin-tagged enzyme from Escherichia coli strain BL21 by metal affinity chromatography, tag cleavage by thrombin
utilizing the His-tag, the tag is removed by thrombin treatment, furthermore a Source15Q column is used
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
arginyl tRNA synthetase and an N-terminally truncated derivative with a deletion of the 73 N-terminal amino acids, expression in Escherichia coli
-
construction of pMFT7H6-hcArgRS by inserting the full-length hcArgRS gene into the gap between NcoI and BamH1 of vector pMFT7H6. Expression of His-tagged wild-type full-length and truncated mutant enzymes in Escherichia coli strain BL21-CodonPlus (DE3)-RIL
-
deduced amino acid sequence shows 87.7% identity to the CHO enzyme and 37.7% identity to the homologous Escherichia coli enzyme
-
expressed in Escherichia coli BL21 Codon Plus RP cells
expressed in Escherichia coli BL21(DE3) cells
expression in Escherichia coli of a His-tagged recombinant enzyme, the enzyme has 73% homology with respect to Bacillus subtilis ArgRS, and 22% with respect to Escherichia coli
-
expression of GST-tagged MtArgRS in Escherichia coli strain BL21(DE3), co-expression of MtArgRS with seryl-tRNA synthetase, MtSerRS, EC 6.1.1.11, from in the Saccharomyces cerevisiae two-hybrid system using yeast strain MaV203
-
full-length enzyme and mutant DELTA1-72 tagged with green fluorescence protein, expression in 293 T cells, exclusively in cytosol
-
gene argS, DNA and amino acid sequence determination and analysis, expression of N-terminally HIS-/thioredoxin-tagged enzyme in Escherichia coli strain BL21
into the TOPO vector and subsequently into the vector pET28c for expression in Escherichia coli BL21DE3codon+ cells
into the vector pET32a for expression in Escherichia coli BL21 cells
overexpressed in Escherichia coli under the control of the T7 promoter
overexpression in Escherichia coli of wild type and several mutant enzymes
overexpression of the wild type and the argS1 mutant enzymes in Escherichia coli
-
into the vector pET32a for expression in Escherichia coli BL21 cells
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
at 24 h, the expression levels of enzyme protein and mRNA in ischemic penumbral tissues are lower than those in normal tissue
ischemic preconditioning can inhibit the increased enzyme activity and down-regulate enzyme expression of ischemia-insulted neurons
prolonged ischemia insult can induce an escalating activity of the enzyme and leads to enzyme over-expression in primary cultured neurons
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Norcum, M.T.
Isolation and electron microscopic characterization of the high molecular mass aminoacyl-tRNA synthetase complex from murine erythroleukemia cells
J. Biol. Chem.
264
15043-15051
1989
Mus musculus
brenda
Sivaram, P.; Vellekamp, G.; Deutscher, M.P.
A role for lipids in the functional and structural properties of the rat liver aminoacyl-tRNA synthetase complex
J. Biol. Chem.
263
18891-18896
1988
Rattus norvegicus
brenda
Thiebe, R.
Arginyl-tRNA synthetase from brewer's yeast. Purification, properties, and steady-state mechanism
Eur. J. Biochem.
130
517-524
1983
Saccharomyces pastorianus, Saccharomyces pastorianus C836
brenda
Girjes, A.A.; Hobson, K.; Chen, P.; Lavin, M.F.
Cloning and chracterization of cDNA encoding a human arginyl-tRNA synthetase
Gene
27
347-350
1995
Homo sapiens
brenda
Huang, S.; Deutscher, M.P.
The NH2-terminal extension of rat liver arginyl-tRNA synthetase is responsible for its hydrophobic properties
Biochem. Biophys. Res. Commun.
180
702-708
1991
Rattus norvegicus
brenda
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
Berbec, H.; Paszkowska, A.
Comparison of the thermolability and hydrophobic properties of high- and low-molecular-weight forms of rabbit liver arginyl-tRNA synthetase
Mol. Cell. Biochem.
86
125-133
1989
Oryctolagus cuniculus
brenda
Berg, B.H.
Degradation of the arginyl-tRNA synthetase protein during purification by affinity chromatography on immobilized total tRNA and immobilized tRNA, specific for arginyl-tRNA synthetase
Biochem. Mol. Biol. Int.
31
219-228
1993
Mus musculus
brenda
Eriani, G.; Dirheimer, G.; Gangloff, J.
Structure-function relationship of arginyl-tRNA synthetase from Escherichia coli: isolation and characterization of the argS mutation MA5002
Nucleic Acids Res.
18
1475-1479
1990
Escherichia coli
brenda
Sivaram, P.; Deutscher, M.P.
Existence of two forms of rat liver arginyl-tRNA synthetase suggests channeling of aminoacyl-tRNA for protein synthesis
Proc. Natl. Acad. Sci. USA
87
3665-3669
1990
Rattus norvegicus
brenda
Parfait, R.; Grosjean, H.
Arginyl-transfer ribonucleic-acid synthetase from Bacillus stearothermophilus. Purification, properties and mechanism of action
Eur. J. Biochem.
30
242-249
1972
Geobacillus stearothermophilus, Geobacillus stearothermophilus NCA 1518
brenda
Yem, D.W.; Williams, L.S.
Evidence for the existence of two arginyl-transfer ribonucleic acid synthetase activities in Escherichia coli
J. Bacteriol.
113
891-894
1973
Escherichia coli, Escherichia coli AB1132
brenda
Williams, A.L.; Williams, L.S.
Control of arginine biosynthesis in Escherichia coli: characteriation of arginyl-transfer ribonucleic acid synthetase mutants
J. Bacteriol.
113
1433-1441
1973
Escherichia coli
brenda
Parfait, R.
Arginyl-tRNA synthetase from Bacillus stearothermophilus: heat inactivation and substrate induced protection
FEBS Lett.
29
323-325
1973
Geobacillus stearothermophilus
brenda
Williams, A.L.; Yem, D.W.; McGinnis, E.; Williams, L.S.
Control of arginine biosynthesis in Escherichia coli: inhibition of arginyl-transfer ribonucleic acid synthetase activity
J. Bacteriol.
115
228-234
1973
Escherichia coli
brenda
Craine, J.E; Peterkofsky, A.
Studies of arginyl-tRNA synthetase from Escherichia coli B. Dual role of metals in enzyme catalysis
J. Biol. Chem.
251
241-246
1976
Escherichia coli, Escherichia coli B / ATCC 11303
brenda
Godeau, J.M.
Arginyl-tRNA synthetase from Bacillus stearothermophilus: subunit structure of enzyme
FEBS Lett.
62
190-193
1976
Geobacillus stearothermophilus
brenda
Gangloff, J.; Schutz, A.; Dirheimer, G.
Arginyl-tRNA synthetase from baker's yeast. Purification and some properties
Eur. J. Biochem.
65
177-182
1976
Saccharomyces pastorianus, Saccharomyces pastorianus 836
brenda
Freist, W.; Sternbach, H.; von der Haar, F.; Cramer, F.
Threonyl-tRNA, lysyl-tRNA and arginyl-tRNA synthetases from baker's yeast. Substrate specificity with regard to ATP analogues
Eur. J. Biochem.
84
499-502
1978
Saccharomyces pastorianus
brenda
Carias, J.R.; Mouricout, M.; Quintard, B.; Thomes, J.C.; Julien, R.
Leucyl-tRNA and arginyl-tRNA synthetases of wheat germ. Inactivation and ribosome effects
Eur. J. Biochem.
87
583-590
1978
Triticum aestivum
brenda
Gerlo, E.; Charlier, J.
Irreversible inactivation of arginyl-tRNA ligase by periodate-oxidized tRNA
FEBS Lett.
99
25-28
1979
Escherichia coli
brenda
Charlier, J.; Gerlo, E.
Arginyl-tRNA synthetase from Escherichia coli K12. Purification, properties, and sequence of substrate addition
Biochemistry
18
3171-3178
1979
Escherichia coli
brenda
Godeau, J.M.
Arginyl-transfer ribonucleic acid synthetase of Bacillus stearothermophilus. Purification and kinetic analysis
Eur. J. Biochem.
103
169-177
1980
Geobacillus stearothermophilus, Geobacillus stearothermophilus NCA 1518
brenda
Freist, W.; Sternbach, H.; Cramer,F.
Arginyl-tRNA synthetase from baker's yeast. Order of substrate addition and action of ATP analogs in aminoacylation reaction. Influence of pyrophosphate on the catalytic mechanism
Eur. J. Biochem.
119
477-482
1981
Saccharomyces pastorianus
brenda
Gerlo, E.; Freist, W.; Charlier, J.
Arginyl-tRNA synthetase from Escherichia coli K12: specificity with regard to ATP analogs and their magnesium complexes
Hoppe-Seyler's Z. Physiol. Chem.
363
365-373
1982
Escherichia coli
brenda
Deutscher, M.P.; Ni, R.C.
Purification of a low molecular weight form of rat liver arginyl-tRNA synthetase
J. Biol. Chem.
257
6003-6006
1982
Rattus norvegicus
brenda
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
J. Biol. Chem.
260
9843-9847
1985
Rattus norvegicus
brenda
Char, S.; Gopinathan, K.P.
Arginyl-tRNA synthetase from Mycobacterium smegmatis SN2: purification and kinetic mechanism
J. Biochem.
100
349-357
1986
Mycolicibacterium smegmatis, Mycolicibacterium smegmatis SN2
brenda
Airas, R.K.
Differences in the magnesium dependences of the class I and class II aminoacyl-tRNA synthetases from Escherichia coli
Eur. J. Biochem.
240
223-231
1996
Escherichia coli
brenda
Glinski, R.L.; Gainey, P.C.; Mawhinney, T.P.; Hilderman, R.H.
Evidence that lysyl- and/or arginyl-tRNA synthetases from rat liver contain carbohydrate
Biochem. Biophys. Res. Commun.
88
1052-1061
1979
Rattus norvegicus
brenda
Van Dang, C.; Mawhinney, T.P.; Hilderman, R.H.
Characterization of a homogeneous arginyl- and lysyl-tRNA synthetase complex isolated from rat liver. Arginyl- and lysyl-tRNA synthetases contain carbohydrates
Biochemistry
21
4891-4895
1982
Rattus norvegicus
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
56
492-494
2000
Saccharomyces cerevisiae
brenda
Shimada, A.; Nureki, O.; Dohmae, N.; Takio, K.; Yokoyama, S.
Gene cloning, expression, crystallization and preliminary X-ray analysis of Thermus thermophilus arginyl-tRNA synthetase
Acta Crystallogr. Sect. D
57
272-275
2001
Thermus thermophilus (Q93RP5), Thermus thermophilus
brenda
Yao, Y.N.; Zhang, Q.S.; Yan, X.Z.; Zhu, G.; Wang, E.D.
Escherichia coli tRNA(4)(Arg)(UCU) induces a constrained conformation of the crucial Omega-loop of arginyl-tRNA synthetase
Biochem. Biophys. Res. Commun.
313
129-134
2004
Escherichia coli
brenda
Li, J.; Yao, Y.N.; Liu, M.F.; Wang, E.D.
Arginyl-tRNA synthetase with signature sequence KMSK from Bacillus stearothermophilus
Biochem. J.
376
773-779
2003
Geobacillus stearothermophilus
brenda
Liu, M.; Huang, Y.; Wu, J.; Wang, E.; Wang, Y.
Effect of cysteine residues on the activity of arginyl-tRNA synthetase from Escherichia coli
Biochemistry
38
11006-11011
1999
Escherichia coli
brenda
Zhang, Q.S.; Wang, E.D.; Wang, Y.L.
The role of tryptophan residues in Escherichia coli arginyl-tRNA synthetase
Biochim. Biophys. Acta
1387
136-142
1998
Escherichia coli
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.
19
5599-5610
2000
Saccharomyces cerevisiae (Q05506), Saccharomyces cerevisiae
brenda
Kiga, D.; Sakamoto, K.; Sato, S.; Hirao, I.; Yokoyama, S.
Shifted positioning of the anticodon nucleotide residues of amber suppressor tRNA species by Escherichia coli arginyl-tRNA synthetase
Eur. J. Biochem.
268
6207-6213
2001
Escherichia coli
brenda
Sekine, S.; Shimada, A.; Nureki, O.; Cavarelli, J.; Moras, D.; Vassylyev, D.G.; Yokoyama, S.
Crucial role of the high-loop lysine for the catalytic activity of arginyl-tRNA synthetase
J. Biol. Chem.
276
3723-3726
2001
Thermus thermophilus
brenda
Lazard, M.; Agou, F.; Kerjan, P.; Mirande, M.
The tRNA-dependent activation of arginine by arginyl-tRNA synthetase requires inter-domain communication
J. Mol. Biol.
302
991-1004
2000
Cricetulus griseus
brenda
Zhang, Q.S.; Shen, L.; Wang, E.D.; Wang, Y.L.
Biosynthesis and characterization of 4-fluorotryptophan-labeled Escherichia coli arginyl-tRNA synthetase
J. Protein Chem.
18
187-192
1999
Escherichia coli
brenda
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
Proc. Natl. Acad. Sci. USA
98
13537-13542
2001
Thermus thermophilus (Q93RP5), Thermus thermophilus
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
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
Biochemistry
43
4592-4600
2004
Cricetulus sp.
brenda
Guigou, L.; Mirande, M.
Determinants in tRNA for activation of arginyl-tRNA synthetase: evidence that tRNA flexibility is required for the induced-fit mechanism
Biochemistry
44
16540-16548
2005
Cricetulus sp.
brenda
Ling, C.; Yao, Y.N.; Zheng, Y.G.; Wei, H.; Wang, L.; Wu, X.F.; Wang, E.D.
The C-terminal appended domain of human cytosolic leucyl-tRNA synthetase is indispensable in its interaction with arginyl-tRNA synthetase in the multi-tRNA synthetase complex
J. Biol. Chem.
280
34755-34763
2005
Homo sapiens
brenda
Edvardson, S.; Shaag, A.; Kolesnikova, O.; Gomori, J.M.; Tarassov, I.; Einbinder, T.; Saada, A.; Elpeleg, O.
Deleterious mutation in the mitochondrial arginyl-transfer RNA synthetase gene is associated with pontocerebellar hypoplasia
Am. J. Hum. Genet.
81
857-862
2007
Homo sapiens
brenda
Zhou, M.; Azzi, A.; Xia, X.; Wang, E.D.; Lin, S.X.
Crystallization and preliminary X-ray diffraction analysis of E. coli arginyl-tRNA synthetase in complex form with a tRNAArg
Amino Acids
32
479-482
2007
Escherichia coli
brenda
Nehme, B.; Ganga, M.A.; Lonvaud-Funel, A.
The arginine deiminase locus of Oenococcus oeni includes a putative arginyl-tRNA synthetase ArgS2 at its 3-end
Appl. Microbiol. Biotechnol.
70
590-597
2006
Oenococcus oeni (Q5Y930), Oenococcus oeni, Oenococcus oeni IOEB 8406 (Q5Y930)
brenda
Zheng, Y.G.; Wei, H.; Ling, C.; Xu, M.G.; Wang, E.D.
Two forms of human cytoplasmic arginyl-tRNA synthetase produced from two translation initiations by a single mRNA
Biochemistry
45
1338-1344
2006
Homo sapiens
brenda
Airas, R.K.
Analysis of the kinetic mechanism of arginyl-tRNA synthetase
Biochim. Biophys. Acta
1764
307-319
2006
Escherichia coli, Escherichia coli MRE 600
brenda
Hogg, J.; Schiefermayr, E.; Schiltz, E.; Igloi, G.L.
Expression and properties of arginyl-tRNA synthetase from jack bean (Canavalia ensiformis)
Protein Expr. Purif.
61
163-167
2008
Canavalia ensiformis (B2G3G6), Canavalia ensiformis
brenda
Eichert, A.; Schreiber, A.; Fuerste, J.P.; Perbandt, M.; Betzel, C.; Erdmann, V.A.; Foerster, C.
Escherichia coli tRNA(Arg) acceptor-stem isoacceptors: comparative crystallization and preliminary X-ray diffraction analysis
Acta Crystallogr. Sect. F
65
98-101
2009
Escherichia coli
brenda
Eichert, A.; Perbandt, M.; Oberthuer, D.; Schreiber, A.; Fuerste, J.P.; Betzel, C.; Erdmann, V.A.; Foerster, C.
Crystal structure of the E. coli tRNA(Arg) aminoacyl stem isoacceptor RR-1660 at 2.0 A resolution
Biochem. Biophys. Res. Commun.
385
84-87
2009
Escherichia coli
brenda
Igloi, G.L.; Schiefermayr, E.
Amino acid discrimination by arginyl-tRNA synthetases as revealed by an examination of natural specificity variants
FEBS J.
276
1307-1318
2009
Canavalia ensiformis (B2G3G6), Canavalia ensiformis, Glycine max (B6ETP1), Glycine max
brenda
Konno, M.; Sumida, T.; Uchikawa, E.; Mori, Y.; Yanagisawa, T.; Sekine, S.; Yokoyama, S.; Yokoyama, S.
Modeling of tRNA-assisted mechanism of Arg activation based on a structure of Arg-tRNA synthetase, tRNA, and an ATP analog (ANP)
FEBS J.
276
4763-4779
2009
Pyrococcus horikoshii (O59147), Pyrococcus horikoshii
brenda
Anderson, L.L.; Mao, X.; Scott, B.A.; Crowder, C.M.
Survival from hypoxia in C. elegans by inactivation of aminoacyl-tRNA synthetases
Science
323
630-633
2009
Caenorhabditis elegans (Q19825)
brenda
Yang, F.; Xia, X.; Lei, H.Y.; Wang, E.D.
Hemin binds to human cytoplasmic arginyl-tRNA synthetase and inhibits its catalytic activity
J. Biol. Chem.
285
39437-39446
2010
Homo sapiens
brenda
Godinic-Mikulcic, V.; Jaric, J.; Hausmann, C.D.; Ibba, M.; Weygand-Durasevic, I.
An archaeal tRNA-synthetase complex that enhances aminoacylation under extreme conditions
J. Biol. Chem.
286
3396-3404
2011
Methanothermobacter thermautotrophicus
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
Aldinger, C.A.; Leisinger, A.K.; Igloi, G.L.
The influence of identity elements on the aminoacylation of tRNAArg by plant and Escherichia coli arginyl-tRNA synthetases
FEBS J.
279
3622-3638
2012
Escherichia coli (B1XHE4), Canavalia ensiformis (B2G3G6), Glycine max (B6ETP1), Glycine max
brenda
Leisinger, A.K.; Janzen, D.H.; Hallwachs, W.; Igloi, G.L.
Amino acid discrimination by the nuclear encoded mitochondrial arginyl-tRNA synthetase of the larva of a bruchid beetle (Caryedes brasiliensis) from northwestern Costa Rica
Insect Biochem. Mol. Biol.
43
1172-1180
2013
Caryedes brasiliensis
brenda
Bi, K.; Zheng, Y.; Gao, F.; Dong, J.; Wang, J.; Wang, Y.; Gong, W.
Crystal structure of E. coli arginyl-tRNA synthetase and ligand binding studies revealed key residues in arginine recognition
Protein Cell
5
151-159
2014
Escherichia coli (P11875), Escherichia coli
brenda
Kim, H.S.; Cha, S.Y.; Jo, C.H.; Han, A.; Hwang, K.Y.
The crystal structure of arginyl-tRNA synthetase from Homo sapiens
FEBS Lett.
588
2328-2334
2014
Homo sapiens (P54136), Homo sapiens
brenda
Yang, F.; Ji, Q.Q.; Ruan, L.L.; Ye, Q.; Wang, E.D.
The mRNA of human cytoplasmic arginyl-tRNA synthetase recruits prokaryotic ribosomes independently
J. Biol. Chem.
289
20953-20959
2014
Homo sapiens (P54136), Homo sapiens
brenda
Xu, H.; Malinin, N.L.; Awasthi, N.; Schwarz, R.E.; Schwarz, M.A.
The N terminus of pro-endothelial monocyte-activating polypeptide II (EMAP II) regulates its binding with the C terminus, arginyl-tRNA synthetase, and neurofilament light protein
J. Biol. Chem.
290
9753-9766
2015
Homo sapiens (P54136), Homo sapiens
brenda
Fu, R.; Fan, Y.Z.; Fan, Y.C.; Zhao, H.Y.
Expression of arginyl-tRNA synthetase in rats with focal cerebral ischemia
J. Huazhong Univ. Sci. Technol. Med. Sci.
34
172-175
2014
Rattus norvegicus (P40329)
brenda
Shen, Y.; Zhao, H.Y.; Wang, H.J.; Wang, W.L.; Zhang, L.Z.; Fu, R.
Ischemic preconditioning inhibits over-expression of arginyl-tRNA synthetase gene Rars in ischemia-injured neurons
J. Huazhong Univ. Sci. Technol. Med. Sci.
36
554-557
2016
Rattus norvegicus (P40329)
brenda
Fu, Y.; Kim, Y.; Jin, K.S.; Kim, H.S.; Kim, J.H.; Wang, D.; Park, M.; Jo, C.H.; Kwon, N.H.; Kim, D.; Kim, M.H.; Jeon, Y.H.; Hwang, K.Y.; Kim, S.; Cho, Y.
Structure of the ArgRS-GlnRS-AIMP1 complex and its implications for mammalian translation
Proc. Natl. Acad. Sci. USA
111
15084-15089
2014
Homo sapiens (P54136)
brenda
Jain, V.; Yogavel, M.; Sharma, A.
Dimerization of arginyl-tRNA synthetase by free heme drives its inactivation in Plasmodium falciparum
Structure
24
1476-1487
2016
Plasmodium falciparum (Q8I5M2), Plasmodium falciparum
brenda
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