Information on EC 6.1.1.19 - Arginine-tRNA ligase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea

EC NUMBER
COMMENTARY
6.1.1.19
-
RECOMMENDED NAME
GeneOntology No.
Arginine-tRNA ligase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
ATP + L-arginine + tRNAArg = AMP + diphosphate + L-arginyl-tRNAArg
show the reaction diagram
-
-
-
-
ATP + L-arginine + tRNAArg = AMP + diphosphate + L-arginyl-tRNAArg
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
rapid equilibrium random ter ter mechanism
-
ATP + L-arginine + tRNAArg = AMP + diphosphate + L-arginyl-tRNAArg
show the reaction diagram
random addition of substrates with all steps in rapid equilibrium except for the interconversion of the central quarternary complexes
Escherichia coli K12
-
-
ATP + L-arginine + tRNAArg = AMP + diphosphate + L-arginyl-tRNAArg
show the reaction diagram
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
Geobacillus stearothermophilus NCA 1518
-
-
ATP + L-arginine + tRNAArg = AMP + diphosphate + L-arginyl-tRNAArg
show the reaction diagram
rapid equilibrium random ter ter mechanism
Mycobacterium smegmatis SN2
-
-
ATP + L-arginine + tRNAArg = AMP + diphosphate + L-arginyl-tRNAArg
show the reaction diagram
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
Saccharomyces carlsbergensis C836
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Aminoacylation
-
-
-
-
Aminoacylation
-
-
Aminoacylation
B2G3G6, -
-
Aminoacylation
B6ETP1, -
-
Aminoacylation
O59147, -
-
Aminoacylation
Q19825
-
esterification
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
Aminoacyl-tRNA biosynthesis
-
tRNA charging
-
SYSTEMATIC NAME
IUBMB Comments
L-Arginine:tRNAArg ligase (AMP-forming)
-
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Arg-tRNA synthetase
O59147
-
Arginine translase
-
-
-
-
Arginine--tRNA ligase
-
-
-
-
Arginine-tRNA synthetase
-
-
-
-
Arginyl transfer ribonucleic acid synthetase
-
-
-
-
Arginyl-transfer RNA synthetase
-
-
-
-
Arginyl-tRNA synthetase
-
-
-
-
Arginyl-tRNA synthetase
Q19825
-
Arginyl-tRNA synthetase
B2G3G6
-
Arginyl-tRNA synthetase
-
-
Arginyl-tRNA synthetase
B6ETP1
-
Arginyl-tRNA synthetase
-
-
Arginyl-tRNA synthetase
-
-
Arginyl-tRNA synthetase
Q5Y930
-
Arginyl-tRNA synthetase
Oenococcus oeni IOEB 8406
Q5Y930
-
-
arginyltRNA synthetase
-
-
arginyltRNA synthetase
Escherichia coli MRE600
-
-
-
arginyltRNA synthetase
-
-
ArgRS
-
-
-
-
ArgRS
Escherichia coli MRE600
-
-
-
ArgRS
O59147
-
ArgS2
Q5Y930
-
ArgS2
Oenococcus oeni IOEB 8406
Q5Y930
-
-
RARS2
-
-
Synthetase, arginyl-transfer ribonucleate
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
37205-35-9
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
gene argS
UniProt
Manually annotated by BRENDA team
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
-
-
Manually annotated by BRENDA team
strain AB1132 and NP2, two enzyme forms
-
-
Manually annotated by BRENDA team
strain B
-
-
Manually annotated by BRENDA team
strain K12
-
-
Manually annotated by BRENDA team
strain K12; strain K12 mutant argS MA5002
-
-
Manually annotated by BRENDA team
strain MRE600
-
-
Manually annotated by BRENDA team
Escherichia coli AB1132
strain AB1132 and NP2, two enzyme forms
-
-
Manually annotated by BRENDA team
Escherichia coli K12
strain K12
-
-
Manually annotated by BRENDA team
Escherichia coli K12
strain K12; strain K12 mutant argS MA5002
-
-
Manually annotated by BRENDA team
Escherichia coli MRE600
strain MRE600
-
-
Manually annotated by BRENDA team
Geobacillus stearothermophilus NCA 1518
strain NCA 1518
-
-
Manually annotated by BRENDA team
strain SN2
-
-
Manually annotated by BRENDA team
Mycobacterium smegmatis SN2
strain SN2
-
-
Manually annotated by BRENDA team
strain IOEB 8406
TrEMBL
Manually annotated by BRENDA team
Oenococcus oeni IOEB 8406
strain IOEB 8406
TrEMBL
Manually annotated by BRENDA team
enzyme exists as a high MW component of the multienzyme aminoacyl-tRNA synthetase complex and a low MW free enzyme
-
-
Manually annotated by BRENDA team
enzyme exists as a 72000 MW component of the multienzyme aminoacyl-tRNA synthetase complex or as 60000 MW free enzyme form
-
-
Manually annotated by BRENDA team
Saccharomyces carlsbergensis 836
strain 836
-
-
Manually annotated by BRENDA team
Saccharomyces carlsbergensis C836
strain C836
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
physiological function
Q19825
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
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2'-deoxyadenosine 5'-triphosphate + L-arginine + tRNAArg
2'-deoxyadenosine 5'-monophosphate + diphosphate + L-arginyl-tRNAArg
show the reaction diagram
-
-
-
-
-
2'-deoxyadenosine 5'-triphosphate + L-arginine + tRNAArg
2'-deoxyadenosine 5'-monophosphate + diphosphate + L-arginyl-tRNAArg
show the reaction diagram
Escherichia coli, Escherichia coli K12
-
-
-
-
-
2'-O-methyladenosine 5'-triphosphate + L-arginine + tRNAArg
2'-O-methyladenosine 5'-monophosphate + diphosphate + L-arginyl-tRNAArg
show the reaction diagram
-
-
-
-
-
2-chloroadenosine 5'-triphosphate + L-arginine + tRNAArg
2-chloroadenosine 5'-monophosphate + diphosphate + L-arginyl-tRNAArg
show the reaction diagram
Escherichia coli, Escherichia coli K12
-
-
-
-
-
3'-deoxyadenosine 5'-triphosphate + L-arginine + tRNAArg
3'-deoxyadenosine 5'-monophosphate + diphosphate + L-arginyl-tRNAArg
show the reaction diagram
-
-
-
-
-
3'-methoxyadenosine 5'-triphosphate + L-arginine + tRNAArg
3'-methoxyadenosine 5'-monophosphate + diphosphate + L-arginyl-tRNAArg
show the reaction diagram
-
-
-
-
-
3'-O-methyladenosine 5'-triphosphate + L-arginine + tRNAArg
3'-O-methyladenosine 5'-monophosphate + diphosphate + L-arginyl-tRNAArg
show the reaction diagram
-
-
-
-
-
8-azaadenosine 5'-triphosphate + L-arginine + tRNAArg
8-azaadenosine 5'-monophosphate + diphosphate + L-arginyl-tRNAArg
show the reaction diagram
Escherichia coli, Escherichia coli K12
-
-
-
-
-
ATP + L-arginine + tRNAArg
AMP + diphosphate + L-arginyl-tRNAArg
show the reaction diagram
-
-
-
?
ATP + L-arginine + tRNAArg
AMP + diphosphate + L-arginyl-tRNAArg
show the reaction diagram
-
-
-
-
-
ATP + L-arginine + tRNAArg
AMP + diphosphate + L-arginyl-tRNAArg
show the reaction diagram
-
-
-
-
-
ATP + L-arginine + tRNAArg
AMP + diphosphate + L-arginyl-tRNAArg
show the reaction diagram
Q93RP5, -
-
-
?
ATP + L-arginine + tRNAArg
AMP + diphosphate + L-arginyl-tRNAArg
show the reaction diagram
-
-
-
?
ATP + L-arginine + tRNAArg
AMP + diphosphate + L-arginyl-tRNAArg
show the reaction diagram
-
-
-
-
-
ATP + L-arginine + tRNAArg
AMP + diphosphate + L-arginyl-tRNAArg
show the reaction diagram
-
-
-
?
ATP + L-arginine + tRNAArg
AMP + diphosphate + L-arginyl-tRNAArg
show the reaction diagram
-
-
-
?
ATP + L-arginine + tRNAArg
AMP + diphosphate + L-arginyl-tRNAArg
show the reaction diagram
-
-
-
?
ATP + L-arginine + tRNAArg
AMP + diphosphate + L-arginyl-tRNAArg
show the reaction diagram
-
-
-
-
?
ATP + L-arginine + tRNAArg
AMP + diphosphate + L-arginyl-tRNAArg
show the reaction diagram
-
-
-
-
?
ATP + L-arginine + tRNAArg
AMP + diphosphate + L-arginyl-tRNAArg
show the reaction diagram
-
-
-
?
ATP + L-arginine + tRNAArg
AMP + diphosphate + L-arginyl-tRNAArg
show the reaction diagram
-
-
-
?
ATP + L-arginine + tRNAArg
AMP + diphosphate + L-arginyl-tRNAArg
show the reaction diagram
Q05506
-
-
?
ATP + L-arginine + tRNAArg
AMP + diphosphate + L-arginyl-tRNAArg
show the reaction diagram
-
-
-
?
ATP + L-arginine + tRNAArg
AMP + diphosphate + L-arginyl-tRNAArg
show the reaction diagram
-
-
-
-
-
ATP + L-arginine + tRNAArg
AMP + diphosphate + L-arginyl-tRNAArg
show the reaction diagram
-
-
-
?
ATP + L-arginine + tRNAArg
AMP + diphosphate + L-arginyl-tRNAArg
show the reaction diagram
-
-
-
-
?
ATP + L-arginine + tRNAArg
AMP + diphosphate + L-arginyl-tRNAArg
show the reaction diagram
-
-
-
-
?
ATP + L-arginine + tRNAArg
AMP + diphosphate + L-arginyl-tRNAArg
show the reaction diagram
-
-
-
?
ATP + L-arginine + tRNAArg
AMP + diphosphate + L-arginyl-tRNAArg
show the reaction diagram
B2G3G6, -
-
-
-
?
ATP + L-arginine + tRNAArg
AMP + diphosphate + L-arginyl-tRNAArg
show the reaction diagram
O59147, -
-
-
-
?
ATP + L-arginine + tRNAArg
AMP + diphosphate + L-arginyl-tRNAArg
show the reaction diagram
Q19825
-
-
-
?
ATP + L-arginine + tRNAArg
AMP + diphosphate + L-arginyl-tRNAArg
show the reaction diagram
B6ETP1, -
-
-
-
?
ATP + L-arginine + tRNAArg
AMP + diphosphate + L-arginyl-tRNAArg
show the reaction diagram
-
r
-
-
-
ATP + L-arginine + tRNAArg
AMP + diphosphate + L-arginyl-tRNAArg
show the reaction diagram
-
Bacillus stearothermophilus tRNAArg, E. coli tRNAArg and yeast tRNAArg (poor)
-
-
-
ATP + L-arginine + tRNAArg
AMP + diphosphate + L-arginyl-tRNAArg
show the reaction diagram
-
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
show the reaction diagram
-
recognizes arginine very specifically
-
-
-
ATP + L-arginine + tRNAArg
AMP + diphosphate + L-arginyl-tRNAArg
show the reaction diagram
-
nucleotides other than ATP are not effective
-
-
-
ATP + L-arginine + tRNAArg
AMP + diphosphate + L-arginyl-tRNAArg
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
substrate is Escherichia coli tRNAArg
-
-
?
ATP + L-arginine + tRNAArg
AMP + diphosphate + L-arginyl-tRNAArg
show the reaction diagram
Saccharomyces carlsbergensis 836
-
-
-
-
-
ATP + L-arginine + tRNAArg
AMP + diphosphate + L-arginyl-tRNAArg
show the reaction diagram
Saccharomyces carlsbergensis C836
-
r, recognizes arginine very specifically
-
-
-
ATP + L-arginine + tRNAArg
AMP + diphosphate + L-arginyl-tRNAArg
show the reaction diagram
Escherichia coli K12
-
-
-
-
-
ATP + L-arginine + tRNAArg
AMP + diphosphate + L-arginyl-tRNAArg
show the reaction diagram
Escherichia coli MRE600
-
-
-
-
?
ATP + L-arginine + tRNAArg
AMP + diphosphate + L-arginyl-tRNAArg
show the reaction diagram
Geobacillus stearothermophilus NCA 1518
-
Bacillus stearothermophilus tRNAArg, E. coli tRNAArg and yeast tRNAArg (poor), nucleotides other than ATP are not effective
-
-
-
ATP + L-arginine + tRNAArg
AMP + diphosphate + L-arginyl-tRNAArg
show the reaction diagram
Geobacillus stearothermophilus NCA 1518
-
-
-
-
-
ATP + L-arginine + tRNAArg
?
show the reaction diagram
-
-
-
-
-
ATP + L-arginine + tRNAArg
?
show the reaction diagram
-
the complexed enzyme supplies arginyl-tRNA for the protein synthesis
-
-
-
ATP + L-arginine + tRNAArg
AMP + diphosphate + L-arginyl tRNAArg
show the reaction diagram
B2G3G6, -
-
-
-
?
ATP + L-arginine + tRNAArg ACG
AMP + diphosphate + L-arginyl tRNAArg ACG
show the reaction diagram
B2G3G6, -
tRNA substrate from Escherichia coli
-
-
?
ATP + L-canavanine + tRNAArg
AMP + diphosphate + L-canavanyl-tRNAArg
show the reaction diagram
B2G3G6, -
-
-
-
?
ATP + L-canavanine + tRNAArg
AMP + diphosphate + L-canavanyl-tRNAArg
show the reaction diagram
B6ETP1, -
-
-
-
?
ATP + L-thioarginine + tRNAArg
AMP + diphosphate + L-thioarginyl-tRNAArg
show the reaction diagram
B2G3G6, -
-
-
-
?
ATP + L-thioarginine + tRNAArg
AMP + diphosphate + L-thioarginyl-tRNAArg
show the reaction diagram
B6ETP1, -
-
-
-
?
tubercidin 5'-triphosphate + L-arginine + tRNAArg
tubercidin 5'-monophosphate + diphosphate + L-arginyl-tRNAArg
show the reaction diagram
-
-
-
-
-
tubercidin 5'-triphosphate + L-arginine + tRNAArg
tubercidin 5'-monophosphate + diphosphate + L-arginyl-tRNAArg
show the reaction diagram
-
-
-
-
-
tubercidin 5'-triphosphate + L-arginine + tRNAArg
tubercidin 5'-monophosphate + diphosphate + L-arginyl-tRNAArg
show the reaction diagram
Mycobacterium smegmatis, Mycobacterium smegmatis SN2
-
-
-
-
-
tubercidin 5'-triphosphate + L-arginine + tRNAArg
tubercidin 5'-monophosphate + diphosphate + L-arginyl-tRNAArg
show the reaction diagram
Escherichia coli K12
-
-
-
-
-
formycin 5'-triphosphate + L-arginine + tRNAArg
formycin 5'-monophosphate + diphosphate + L-arginyl-tRNAArg
show the reaction diagram
-
-
-
-
-
additional information
?
-
-
arginine-dependent ATP-diphosphate exchange
-
-
-
additional information
?
-
-
arginine-dependent ATP-diphosphate exchange
-
-
-
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
?
-
-
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
?
-
-
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 65C
-
-
-
additional information
?
-
Saccharomyces carlsbergensis 836
-
arginine-dependent ATP-diphosphate exchange
-
-
-
additional information
?
-
Escherichia coli K12
-
arginine-dependent ATP-diphosphate exchange
-
-
-
additional information
?
-
Geobacillus stearothermophilus NCA 1518
-
arginine-dependent ATP-diphosphate exchange
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + L-arginine + tRNAArg
AMP + diphosphate + L-arginyl-tRNAArg
show the reaction diagram
-
-
-
-
?
ATP + L-arginine + tRNAArg
AMP + diphosphate + L-arginyl-tRNAArg
show the reaction diagram
-
-
-
-
?
ATP + L-arginine + tRNAArg
AMP + diphosphate + L-arginyl-tRNAArg
show the reaction diagram
-
-
-
-
?
ATP + L-arginine + tRNAArg
AMP + diphosphate + L-arginyl-tRNAArg
show the reaction diagram
B2G3G6, -
-
-
-
?
ATP + L-arginine + tRNAArg
AMP + diphosphate + L-arginyl-tRNAArg
show the reaction diagram
O59147, -
-
-
-
?
ATP + L-arginine + tRNAArg
AMP + diphosphate + L-arginyl-tRNAArg
show the reaction diagram
Q19825
-
-
-
?
ATP + L-arginine + tRNAArg
AMP + diphosphate + L-arginyl-tRNAArg
show the reaction diagram
B6ETP1, -
-
-
-
?
ATP + L-arginine + tRNAArg
AMP + diphosphate + L-arginyl-tRNAArg
show the reaction diagram
-
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
?
show the reaction diagram
-
the complexed enzyme supplies arginyl-tRNA for the protein synthesis
-
-
-
ATP + L-arginine + tRNAArg
AMP + diphosphate + L-arginyl tRNAArg
show the reaction diagram
B2G3G6, -
-
-
-
?
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
?
-
-
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 65C
-
-
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
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+
K+
-
50 mM is required for full activity
Mg2+
-
required
Mg2+
-
MgCl2, complete activation at a concentration of 5 mM in excess of the total ATP concentration; required
Mg2+
-
MgCl2, optimal concentration in aminoacylation: 7 mM , when ATP concentration is 10 mM
Mg2+
-
optimal concentration is 6 mM; required
Mg2+
-
requires one Mg2+ for the activation reaction (MgATP2-)
Mg2+
-
dependent
Mg2+
B2G3G6, -
-
Mg2+
-
-
Mn2+
-
MnCl2, complete activation at a concentration of 5 mM in excess of the total ATP concentration, 49% as effective as Mg2+
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
2'-Methoxyadenosine 5'-triphosphate
-
-
2-Aminopurine riboside 5'-triphosphate
-
-
3'-Deoxyadenosine 5'-triphosphate
-
-
6-N-Benzyladenosine 5'-triphosphate
-
-
6-N-Benzyladenosine 5'-triphosphate
-
-
8-azido-ATP
-
-
8-azidoadenosine 5'-triphosphate
-
-
8-bromoadenosine 5'-triphosphate
-
-
8-bromoadenosine 5'-triphosphate
-
-
adenosine 5'-[alpha,beta-methylene]triphosphate
-
-
argininosuccinate
-
-
Arginyl hydroxamate
-
-
citrulline
-
-
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
Homoarginine
-
-
KCl
-
50% inhibition: at 150 mM (free enzyme), at 180 mM (complexed enzyme)
NaCl
B2G3G6, -
50% inhibition at 100 mM, recombinant HIS-/thioredoxin-tagged enzyme
ornithine
-
-
p-hydroxymercuribenzoate
-
tRNA or DTT protects against heat inactivation
Periodate-oxidized tRNA
-
mixed type non-competitive, irreversible
-
Periodate-oxidized tRNA
-
-
-
purine riboside
-
-
purine-riboside 5'-triphosphate
-
-
RNA minihelix
-
-
-
RNAi
Q19825
-
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
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
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
1.5
-
2'-Deoxyadenosine 5'-triphosphate
-
NTP-diphosphate exchange
1.3
-
2-Chloroadenosine 5'-triphosphate
-
NTP-diphosphate exchange
0.5
-
3'-Deoxyadenosine 5'-triphosphate
-
aminoacylation
0.1
-
3'-Methoxyadenosine 5'-triphosphate
-
aminoacylation
3
-
8-azaadenosine 5'-triphosphate
-
aminoacylation
3.3
-
8-azaadenosine 5'-triphosphate
-
NTP-diphosphate exchange
0.0015
-
Arg
-
aminoacylation
0.0019
-
Arg
-
aminoacylation
0.0033
-
Arg
-
complexed enzyme
0.0045
-
Arg
-
free enzyme
0.009
-
Arg
-
aminoacylation, native enzyme
0.011
-
Arg
-
aminoacylation of tRNAArg-C-C-A, Arg
0.011
-
Arg
-
aminoacylation and ATP-diphosphate exchange, mutant enzyme
0.022
-
Arg
-
aminoacylation of tRNAArg-C-C-A(3'NH2)
0.11
-
Arg
-
ATP-diphosphate exchange
0.15
-
Arg
-
ATP-diphosphate exchange, native enzyme
0.15
-
Arg
-
2'-deoxyadenosine 5'-triphosphate, , aminoacylation
0.7
-
Arg
-
aminoacylation, native enzyme
0.186
-
ATP
B2G3G6, -
pH 7.5, 30C, recombinant detagged enzyme
0.19
-
ATP
-
aminoacylation reaction, pH 8, 25C
0.207
-
ATP
B2G3G6, -
pH 7.5, 30C, recombinant HIS-/thioredoxin-tagged enzyme
0.24
-
ATP
-
aminoacylation reaction, pH 8, 37C
0.3
-
ATP
-
aminoacylation
0.3
-
ATP
-
2'-O-methyladenosine 5'-triphosphate
0.41
-
ATP
-
free enzyme
0.43
-
ATP
-
complexed enzyme
0.501
-
ATP
-
pH 7.5, 37C, recombinant, truncated DELTANhcArgRS, absence of hemin
0.529
-
ATP
-
pH 7.5, 37C, recombinant, truncated DELTANhcArgRS, presence of hemin
0.54
-
ATP
-
aminoacylation
0.671
-
ATP
-
37C, pH 7.5, arginylation, mutant enzyme DELTA1-72
0.84
-
ATP
-
mutant W162A, pH 7.4, 37C
0.9
-
ATP
-
pH 7.4, 37C
0.9
-
ATP
-
aminoacylation reaction
0.91
-
ATP
-
37C, pH 7.5, arginylation, full-length enzyme
1
-
ATP
-
aminoacylation reaction, pH 8, 55C
1.2
-
ATP
-
aminoacylation
1.29
-
ATP
-
ATP-diphosphate exchange reaction, pH 8, 55C
1.3
-
ATP
-
aminoacylation reaction, pH 8, 37C
1.31
-
ATP
-
ATP-diphosphate exchange reaction, pH 8, 37C
1.35
-
ATP
-
aminoacylation reaction, 4-fluorotryptophan-labeled enzyme
1.4
-
ATP
-
ATP-diphosphate exchange
1.9
-
ATP
-
NTP-diphosphate exchange
2
-
ATP
-
ATP-diphosphate exchange, native enzyme
4.3
-
ATP
-
aminoacylation, mutant enzyme
0.05
-
diphosphate
-
ATP-diphosphate exchange
0.0007
-
L-arginine
-
ATP-diphosphate exchange reaction, pH 8, 25C
0.001
-
L-arginine
-
ATP-diphosphate exchange reaction, pH 8, 55C
0.0013
-
L-arginine
-
aminoacylation reaction, pH 8, 25C
0.0022
-
L-arginine
B6ETP1, -
assay method, aminoacylation of transcript tRNA with [14C]-labelled amino acid
0.0023
-
L-arginine
-
ATP-diphosphate exchange reaction, pH 8, 37C
0.0024
-
L-arginine
-
aminoacylation reaction, pH 8, 37C
0.003
-
L-arginine
B6ETP1, -
assay method, aminoacylation of [32P]-labelled transcript tRNA
0.0035
-
L-arginine
-
37C, pH 7.5, arginylation, full-length enzyme
0.0048
-
L-arginine
-
37C, pH 7.5, arginylation, mutant enzyme DELTA1-72
0.0057
-
L-arginine
-
aminoacylation reaction, pH 8, 37C
0.0065
-
L-arginine
-
pH 7.5, 37C, recombinant, truncated DELTANhcArgRS, absence of hemin
0.0073
-
L-arginine
-
mutant W162A, pH 7.4, 37C
0.0074
-
L-arginine
-
ATP-diphosphate exchange reaction, pH 8, 37C
0.0078
-
L-arginine
B2G3G6, -
assay method, aminoacylation of [32P]-labelled transcript tRNA
0.0078
-
L-arginine
-
pH 7.5, 37C, recombinant, truncated DELTANhcArgRS, presence of hemin
0.0094
-
L-arginine
-
aminoacylation reaction, pH 8, 55C
0.012
-
L-arginine
-
pH 7.4, 37C
0.012
-
L-arginine
-
aminoacylation reaction
0.0137
-
L-arginine
-
aminoacylation reaction, 4-fluorotryptophan-labeled enzyme
0.0164
-
L-arginine
B2G3G6, -
pH 7.5, 30C, recombinant HIS-/thioredoxin-tagged enzyme
0.0196
-
L-arginine
B2G3G6, -
pH 7.5, 30C, recombinant detagged enzyme
0.0196
-
L-arginine
B2G3G6, -
assay method, aminoacylation of transcript tRNA with [14C]-labelled amino acid
0.0453
-
L-canavanine
B6ETP1, -
assay method, aminoacylation of transcript tRNA with [14C]-labelled amino acid
0.0454
-
L-canavanine
B6ETP1, -
assay method, aminoacylation of [32P]-labelled transcript tRNA
0.00005
0.0006
tRNAArg
-
pH 7.4
0.00005
-
tRNAArg
-
37C, pH 7.5, arginylation, full-length enzyme
0.000098
-
tRNAArg
-
37C, pH 7.5, arginylation, mutant enzyme DELTA1-72
0.0001
0.0002
tRNAArg
-
-
0.0002
-
tRNAArg
-
substrate from E. coli, , ATP-diphosphate exchange, pH 6.0
0.00031
-
tRNAArg
-
aminoacylation
0.00032
-
tRNAArg
-
25C, pH 7.5, native tRNAArg from beef liver, wild type enzyme
0.00039
-
tRNAArg
-
25C, pH 7.5, native tRNAArg from beef liver, mutant enzyme DELTA1-73
0.00044
-
tRNAArg
-
argS1 mutant, pH 7.5, 37C
0.001
-
tRNAArg
-
pH 7.5, 37C
0.0017
-
tRNAArg
-
aminoacylation reaction, pH 8, 37C
0.0019
-
tRNAArg
-
transfer RNA isoacceptor for arginine UCU
0.0023
-
tRNAArg
-
mutant W162A, pH 7.4, 37C
0.0025
-
tRNAArg
-
pH 7.4, ATP-diphosphate exchange
0.0025
-
tRNAArg
-
Arg, , ATP-diphosphate exchange
0.0025
-
tRNAArg
-
transfer RNA isoacceptor for arginine UCU
0.0025
-
tRNAArg
-
pH 7.4, 37C
0.0025
-
tRNAArg
-
aminoacylation reaction
0.0026
-
tRNAArg
O59147, -
tRNAArgCCU, wild-type ArgRS
0.0029
-
tRNAArg
-
aminoacylation reaction, pH 8, 55C
0.003
-
tRNAArg
-
aminoacylation, native enzyme
0.003
-
tRNAArg
-
aminoacylation reaction, 4-fluorotryptophan-labeled enzyme
0.0032
-
tRNAArg
-
aminoacylation reaction, pH 8, 25C
0.0036
-
tRNAArg
-
substrate from E. coli, , ATP-diphosphate exchange, pH 7.4
0.0038
-
tRNAArg
O59147, -
tRNAArgCCU, mutant DELTANArgRS
0.004
-
tRNAArg
-
free enzyme
0.0042
-
tRNAArg
-
aminoacylation, mutant enzyme
0.0044
-
tRNAArg
-
aminoacylation reaction, pH 8, 37C
0.00466
-
tRNAArg
-
pH 7.5, 50C, recombinant MtArgRS
0.00477
-
tRNAArg
-
pH 7.5, 50C, recombinant MtArgRS in presence of recombinant MtSerRS
0.0081
-
tRNAArg
-
pH 7.5, 37C, recombinant, truncated DELTANhcArgRS, presence of hemin, Escherichia coli tRNAArg
0.0096
-
tRNAArg
-
pH 7.5, 37C, 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, 65C
0.028
-
tRNAArg
-
complexed enzyme
0.45
-
tRNAArg
-
25C, pH 7.5, tRNAArg from Saccharomyces cerevisiae, aminoacylation
0.53
-
tRNAArg
-
25C, pH 7.5, mammalian tRNAArg, aminoacylation
0.00086
-
tRNAArg ACG
B2G3G6, -
pH 7.5, 30C, recombinant detagged enzyme
-
0.00184
-
tRNAArg ACG
B2G3G6, -
pH 7.5, 30C, recombinant HIS-/thioredoxin-tagged enzyme
-
0.00028
-
tRNAArgIII
-
aminoacylation
-
0.00018
-
tRNArg
-
ATP-diphosphate exchange, pH 6.0
-
0.2
-
Tubercidin 5'-triphosphate
-
formycin 5'-triphosphate, 2'-deoxyadenosine 5'-triphosphate, 3'-O-methyladenosine 5'-triphosphate
0.2
-
Tubercidin 5'-triphosphate
-
tubercidine 5'-triphosphate, , aminoacylation
0.4
-
Tubercidin 5'-triphosphate
-
3'-methoxyadenosine 5'-triphosphate, , NTP-diphosphate exchange
0.4
-
Tubercidin 5'-triphosphate
-
ATP
2.5
-
2-Chloroadenosine 5'-triphosphate
-
aminoacylation
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
1.32
-
L-canavanine
B2G3G6, -
assay method, aminoacylation of [32P]-labelled transcript tRNA
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 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 ATP and L-arginine for 26 mutants
-
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
-
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
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.63
-
Arg
-
aminoacylation of tRNAArg-C-C-A(3'NH2)
3.22
-
Arg
-
aminoacylation of tRNAArg-C-C-A
0.28
-
ATP
-
37C, pH 7.5, arginylation, full-length enzyme
0.77
-
ATP
-
37C, pH 7.5, arginylation, mutant enzyme DELTA1-72
3.4
-
ATP
-
pH 7.5, 37C, recombinant, truncated DELTANhcArgRS, presence of hemin
5.6
-
ATP
-
mutant W162A, pH 7.4, 37C
15.5
-
ATP
-
pH 7.5, 37C, recombinant, truncated DELTANhcArgRS, absence of hemin
26
-
ATP
-
pH 7.4, 37C
0.215
-
L-arginine
B2G3G6, -
pH 7.5, 30C, recombinant HIS-/thioredoxin-tagged enzyme
0.337
-
L-arginine
B2G3G6, -
pH 7.5, 30C, recombinant detagged enzyme
0.41
-
L-arginine
-
37C, pH 7.5, arginylation, full-length enzyme
0.97
-
L-arginine
-
37C, pH 7.5, arginylation, mutant enzyme DELTA1-72
3.8
-
L-arginine
-
pH 7.5, 37C, recombinant, truncated DELTANhcArgRS, presence of hemin
0.00016
-
tRNAArg
-
25C, pH 7.5, mammalian tRNAArg, aminoacylation
0.0045
-
tRNAArg
-
25C, pH 7.5, tRNAArg from Saccharomyces cerevisiae, aminoacylation
0.026
-
tRNAArg
-
pH 7.5, 50C, recombinant MtArgRS
0.034
-
tRNAArg
-
pH 7.5, 50C, recombinant MtArgRS in presence of recombinant MtSerRS
0.32
-
tRNAArg
-
37C, pH 7.5, arginylation, full-length enzyme
0.36
-
tRNAArg
-
wild type enzyme, in 50 mM Tris-HCl (pH 7.5)
0.8
-
tRNAArg
-
mutant enzyme DELTANhcArgRS, in 50 mM Tris-HCl (pH 7.5)
0.81
-
tRNAArg
-
37C, pH 7.5, arginylation, mutant enzyme DELTA1-72
1.8
-
tRNAArg
-
25C, pH 7.5, native tRNAArg from beef liver, wild type enzyme
2
8
tRNAArg
-
transfer RNA isoacceptor for arginine UCU
2.5
-
tRNAArg
-
pH 7.5, 37C, recombinant, truncated DELTANhcArgRS, presence of hemin, Escherichia coli tRNAArg
2.6
-
tRNAArg
-
25C, pH 7.5, native tRNAArg from beef liver, mutant enzyme DELTA1-73
2.8
-
tRNAArg
-
argS1 mutant, pH 7.5, 37C
16.5
-
tRNAArg
-
pH 7.5, 37C, recombinant, truncated DELTANhcArgRS, absence of hemin, Escherichia coli tRNAArg
17
-
tRNAArg
-
pH 7.5, 37C
21.9
-
tRNAArg
-
transfer RNA isoacceptor for arginine UCU
26
-
tRNAArg
-
transfer RNA isoacceptor for arginine UCU
17.9
-
L-arginine
-
pH 7.5, 37C, recombinant, truncated DELTANhcArgRS, absence of hemin
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
-
-
-
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
-
kcat/KM VALUE [1/mMs-1]
kcat/KM VALUE [1/mMs-1] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
6
-
ATP
-
pH 7.5, 37C, recombinant, truncated DELTANhcArgRS, presence of hemin
22040
30
-
ATP
-
pH 7.5, 37C, recombinant, truncated DELTANhcArgRS, absence of hemin
22040
500
-
L-arginine
-
pH 7.5, 37C, recombinant, truncated DELTANhcArgRS, presence of hemin
12093
2800
-
L-arginine
-
pH 7.5, 37C, recombinant, truncated DELTANhcArgRS, absence of hemin
12093
300
-
tRNAArg
-
pH 7.5, 37C, recombinant, truncated DELTANhcArgRS, presence of hemin, Escherichia coli tRNAArg
17501
1700
-
tRNAArg
-
pH 7.5, 37C, recombinant, truncated DELTANhcArgRS, absence of hemin, Escherichia coli tRNAArg
17501
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
150
-
KCl
-
free enzyme
180
-
KCl
-
complexed enzyme
IC50 VALUE [mM]
IC50 VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.000609
-
-
-
0.286
-
-
wild type enzyme, in 50 mM Tris-HCl (pH 7.5)
0.715
-
-
mutant enzyme DELTANhcArgRS, in 50 mM Tris-HCl (pH 7.5)
4.984
-
-
-
additional information
-
-
-
additional information
-
-
-
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
-
-
K116G mutant displays very low activity compared to wild type enzyme
additional information
-
-
activity for different mutants
additional information
-
-
incorporation of 4-fluorotryptophan has little effect on activity
additional information
-
B2G3G6, -
activity of recombinant tagged and detagged enzyme
additional information
-
B2G3G6, -
L-arginine, aminoacylation 100%; L-canavanine, aminoacylation 15%; L-thioarginine, aminoacylation 90%
additional information
-
B6ETP1, -
L-arginine, aminoacylation 100%; L-canavanine, aminoacylation 45%; L-thioarginine, aminoacylation 82%
additional information
-
-
comparison of aminoacylation activity of Escherichia coli ArgRS and human truncated DELTANhcArgRS in presence of hemin, overview
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
7.5
-
-
aminoacylation
7.5
-
B2G3G6, -
aminoacylation assay
7.5
-
B6ETP1, -
aminoacylation assay
7.5
-
O59147, -
aminoacylaion assay
7.5
-
-
assay at
8.1
8.5
-
-
8.2
-
B2G3G6, -
about
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6.5
9.5
B2G3G6, -
activity range, pH-profile, overview
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
30
-
B2G3G6, -
assay at
30
-
B2G3G6, -
aminoacylation assay
30
-
B6ETP1, -
aminoacylation assay
37
-
-
assay at
55
-
-
activity three-fold higher than at 37C
65
-
O59147, -
aminoacylaion assay
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
35
-
-
35C: about 50% of maximal activity, 70C: rapid drop of activity above
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; tRNA protects from heat inactivation above 1 mg/ml
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
Campylobacter jejuni subsp. jejuni serotype O:2 (strain NCTC 11168)
Escherichia coli (strain K12)
Klebsiella pneumoniae subsp. pneumoniae (strain ATCC 700721 / MGH 78578)
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
50000
-
-
gel filtration, enzyme form II
56000
63000
-
gel filtration, sedimentation data
58000
-
-
gel filtration
58000
-
-
gel filtration
59000
-
-
gel filtration, sucrose density gradient centrifugation
62800
-
-
gel filtration
63000
-
-
gel filtration
67000
-
-
SDS-PAGE, mutant enzyme DELTANhcArgRS
67400
-
B2G3G6, -
theoretical
68000
-
-
SDS-PAGE
68200
-
B6ETP1, -
theoretical
69500
-
-
X-ray diffraction
70000
73000
-
sucrose density gradient centrifugation
70000
-
-
gel filtration
73000
-
-
electrophoresis in variably cross-linked gels
75000
-
-
SDS-PAGE, wild type enzyme
80000
-
-
gel filtration, enzyme form I
240000
-
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 60000, free enzyme; 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
?
-
x * 43000 (alpha, catalytic subunit) + x * 78000, (beta, exhibits no significant activity), SDS-PAGE
monomer
-
1 * 72000, SDS-PAGE
monomer
-
1 * 74000, SDS-PAGE
monomer
-
1 * 70000, PAGE after dissociation
monomer
-
1 * 60000, SDS-PAGE
monomer
-
1 * 59000, SDS-PAGE
monomer
-
1 * 60000, SDS-PAGE
monomer
-
1 * 55000, SDS-PAGE
monomer
-
1 * 62800, SDS-PAGE
monomer
-
X-ray diffraction
monomer
Escherichia coli K12
-
1 * 60000, SDS-PAGE
-
monomer
Geobacillus stearothermophilus NCA 1518
-
1 * 59000, SDS-PAGE
-
monomer
Mycobacterium smegmatis SN2
-
1 * 55000, SDS-PAGE
-
monomer
Saccharomyces carlsbergensis 836
-
1 * 74000, SDS-PAGE
-
monomer
Saccharomyces carlsbergensis C836
-
1 * 72000, SDS-PAGE
-
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
additional information
-
cognate tRNA induces dimerization
additional information
Geobacillus stearothermophilus NCA 1518
-
cognate tRNA induces dimerization
-
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
glycoprotein
-
3.5% carbohydrate: mannose and N-acetylglucosamine
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
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
different tRNA acceptor stem helices are crystalized
-
hanging drop vapour diffusion method in complex form with tRNAArg at pH 5.6 using ammonium sulfate as a precipitating agent
-
the tRNAArg microhelices RR-1660 and RR-1662 are crystalized
-
a crystal structure of a complex of Arg-tRNA synthetase, tRNAArgCCU, and the ATP analog ANP is determined to 2.0 A resolution
O59147, -
crystallization of a ternary complex formed by arginyl-tRNA synthetase, tRNAArg and L-arginine by the hanging-drop vapour-diffusion method
Q05506
three different crystal forms crystallized by the hanging-drop vapour-diffusion method
-
using the hanging-drop vapour-diffusion method
-
crystal structure solved by multiple isomorphous replacement
-
crystallized by the hanging-drop vapour-diffusion method using ethylene glycol as precipitant
-
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
20
-
-
24 h, stable, without glycerol
37
-
-
20 min, 25% loss of activity of high MW form, 50% loss of activity of low MW form
37
-
-
stable for 6 h
65
-
-
stable for 10 min
70
-
-
stable up to
74.5
-
-
50% inactivation, when the temperature is raised gradually at the rate of 1C/min
additional information
-
-
tRNA reduces thermal inactivation, reduced glutathione effectively protects the enzyme from thermal inactivation, zinc or Triton X-100 increases thermal inactivation
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
affected by repeated freeze-thaw cycles
-
degradation of the enzyme during purification may be due to the influence of the immobilized tRNA, and is enhanced by high salt concentrations
-
complexed arginyl-tRNA synthetase is more stable than the free enzyme
-
reduced glutathione effectively protects the enzyme from thermal inactivation
-
tRNA reduces thermal inactivation
-
zinc or Triton X-100 increases thermal inactivation
-
not affected by four freeze-thaw cycles
-
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
-
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-20C, 50% v/v glycerol, stable for at least 6 months
-
-25C, less than 30% loss of activity after 6 months
-
-20C, 50% glycerol, stable for at least 3 months
-
-75C, stable for at least 3 months
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
soluble recombinant N-terminally HIS-/thioredoxin-tagged enzyme from Escherichia coli strain BL21 by metal affinity chromatography, tag cleavage by thrombin
B2G3G6, -
utilizing the His-tag, the tag is removed by thrombin treatment
B2G3G6, -
purification of the native and mutant enzymes expressed in Saccharomices cerevisiae, using Q-Sepharose and S-Sepharose chromatography
-
DEAE-Sepharose CL-6B column chromatography
-
DEAE-Sepharose CL-6B column chromatography, hydroxylapatite chromatography, Sepharose CL-2B column chromatography, and Sephacryl S-300 gel filtration
-
partial purification of recombinant enzymes using DEAE-Sepharose and Blue-Sepharose column chromatography
-
using chromatography on Ni-nitrilotriacetic acid agarose
-
purification of a His-tagged recombinant enzyme using Ni-nitrilotriacetic acid agarose affinity chromatography
-
utilizing the His-tag, the tag is removed by thrombin treatment, furthermore a Source15Q column is used
B6ETP1, -
Ni-NTA Superflow resin chromatography and dialysis against 20 mM potassium phosphate buffer (pH 7.5)
-
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
-
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
-
on a Ni2+-nitrilotriacetic superflow, a Resource Q, a Hitrap heparin, and a hydroxyapatite column
O59147, -
72000 MW form
-
two active forms which are interconvertible, I and II
-
purification of the wild type and K116G mutant, expressed in Escherichia coli, by DEAE-Sephacel and PhenylSuperose column chromatography
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
gene argS, DNA and amino acid sequence determination and analysis, expression of N-terminally HIS-/thioredoxin-tagged enzyme in Escherichia coli strain BL21
B2G3G6, -
into the vector pET32a for expression in Escherichia coli BL21 cells
B2G3G6, -
expression of the native and mutant enzymes in Saccharomyces cerevisiae
-
arginyl tRNA synthetase and an N-terminally truncated derivative with a deletion of the 73 N-terminal amino acids, expression in Escherichia coli
-
expressed in Escherichia coli strain MT 102
-
overexpression in Escherichia coli
-
overexpression of the wild type and the argS1 mutant enzymes in Escherichia coli
-
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
-
into the vector pET32a for expression in Escherichia coli BL21 cells
B6ETP1, -
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
-
full-length enzyme and mutant DELTA1-72 tagged with green fluorescence protein, expression in 293 T cells, exclusively in cytosol
-
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
-
into the TOPO vector and subsequently into the vector pET28c for expression in Escherichia coli BL21DE3codon+ cells
O59147, -
expression of 26 lethal mutants in Escherichia coli
-
expression of the wild type and K116G mutant in Escherichia coli
-
overexpressed in Escherichia coli under the control of the T7 promoter
-
overexpression in Escherichia coli of wild type and several mutant enzymes
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
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
C320A
-
slight effect on activity
C537A
-
slight effect on activity
W162A
-
expression in Escherichia coli, 23% of wild-type activity
W172A
-
expression in Escherichia coli
W228A
-
expression in Escherichia coli
W349A
-
expression in Escherichia coli
W446A
-
expression in Escherichia coli
Y524D
-
mutant cannot suppress the effect of the expression of FTOR126, a variant of the wild type tRNAArg
argS MA5002
Escherichia coli K12
-
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
-
G136K
-
inactive enzyme
K382A
-
half as active as the native enzyme
K385A
-
inactive enzyme
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
K116G
-
expression of the mutant in Escherichia coli
N79D
-
can use tRNAArg with G20 as substrate
N79E
-
can use tRNAArg with G20 or U20 as substrate
N79K
-
can use tRNAArg with G20 as substrate
N79Q
-
can use tRNAArg with G20 as substrate
N79R
-
can use tRNAArg with G20 or U20 as substrate
Y77A
-
inactive mutant
Y77F
-
slight effect on activity
M460V
-
mutant cannot suppress the effect of the expression of FTOR126, a variant of the wild type tRNAArg
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
DELTANArgRS
O59147, -
lacking the N-terminal side from the 91st residue
additional information
-
isolation of 26 mutants by random mutagenesis