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 hide
6.1.1.19
-
RECOMMENDED NAME
GeneOntology No.
arginine-tRNA ligase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + L-arginine + tRNAArg = AMP + diphosphate + L-arginyl-tRNAArg
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Aminoacylation
esterification
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Aminoacyl-tRNA biosynthesis
-
-
arginine metabolism
-
-
tRNA charging
-
-
SYSTEMATIC NAME
IUBMB Comments
L-arginine:tRNAArg ligase (AMP-forming)
-
CAS REGISTRY NUMBER
COMMENTARY hide
37205-35-9
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
strain AB1132 and NP2, two enzyme forms
-
-
Manually annotated by BRENDA team
strain MRE600
-
-
Manually annotated by BRENDA team
strain NCA 1518
-
-
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
Methanothermobacter thermautotrophicum
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
strain SN2
-
-
Manually annotated by BRENDA team
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
strain 836
-
-
Manually annotated by BRENDA team
strain C836
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
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'-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
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
ATP + L-arginine + 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 ACG
AMP + diphosphate + L-arginyl tRNAArg ACG
show the reaction diagram
tRNA substrate from Escherichia coli
-
-
?
ATP + L-arginine + tRNAArg(ACG)
AMP + diphosphate + L-arginyl tRNAArg(ACG)
show the reaction diagram
ATP + L-arginine + tRNAArg(ACG)
AMP + diphosphate + L-arginyl-soybean tRNAArg(ACG)
show the reaction diagram
tRNA from Glycine max
-
-
?
ATP + L-arginine + tRNAArg(ACG)
AMP + diphosphate + L-arginyl-tRNAArg(ACG)
show the reaction diagram
ATP + L-canavanine + tRNAArg
AMP + diphosphate + L-canavanyl-tRNAArg
show the reaction diagram
ATP + L-citrulline + tRNACCCG
AMP + diphosphate + L-citryl-tRNACCCG
show the reaction diagram
-
9% aminoacylation activity at 0.5 mM and 22% aminoacylation activity at 7.5 mM
-
-
?
ATP + L-homoarginine + tRNACCCG
AMP + diphosphate + L-homoarginyl-tRNACCCG
show the reaction diagram
-
9% aminoacylation activity at 0.5 mM and 37% aminoacylation activity at 7.5 mM
-
-
?
ATP + L-thioarginine + tRNAArg
AMP + diphosphate + L-thioarginyl-tRNAArg
show the reaction diagram
ATP + NG-methyl-L-arginine + tRNACCCG
AMP + diphosphate + L-arginyl-tRNACCCG
show the reaction diagram
-
71% aminoacylation activity at 0.5 mM
-
-
?
formycin 5'-triphosphate + L-arginine + tRNAArg
formycin 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
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
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
AMP + diphosphate + L-arginyl-tRNAArg
show the reaction diagram
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
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
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
COMMENTARY hide
LITERATURE
IMAGE
2'-Methoxyadenosine 5'-triphosphate
-
-
2-Aminopurine riboside 5'-triphosphate
-
-
3'-Deoxyadenosine 5'-triphosphate
-
-
6-N-Benzyladenosine 5'-triphosphate
8-azido-ATP
-
-
8-azidoadenosine 5'-triphosphate
-
-
8-bromoadenosine 5'-triphosphate
adenosine 5'-[alpha,beta-methylene]triphosphate
-
-
argininosuccinate
-
-
Arginyl hydroxamate
-
-
citrulline
-
-
diphosphate
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
-
-
K2SO4
-
45 mM
NaCl
50% inhibition at 100 mM, recombinant HIS-/thioredoxin-tagged enzyme
ornithine
-
-
p-hydroxymercuribenzoate
-
tRNA or DTT protects against heat inactivation
Periodate-oxidized tRNA
purine riboside
-
-
purine-riboside 5'-triphosphate
-
-
RNA minihelix
-
-
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
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]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.5
2'-deoxyadenosine 5'-triphosphate
-
NTP-diphosphate exchange
1.3 - 2.5
2-Chloroadenosine 5'-triphosphate
0.5
3'-Deoxyadenosine 5'-triphosphate
-
aminoacylation
0.1
3'-Methoxyadenosine 5'-triphosphate
-
aminoacylation
3 - 3.3
8-azaadenosine 5'-triphosphate
0.0006 - 0.7
Arg
0.186 - 4.3
ATP
0.05
diphosphate
-
ATP-diphosphate exchange
0.0007 - 0.0196
L-arginine
0.0453 - 1.32
L-canavanine
0.00005 - 0.53
tRNAArg
0.00086 - 0.00184
tRNAArg ACG
0.00029 - 0.0041
tRNAArg(ACG)
0.00028
tRNAArgIII
-
aminoacylation
-
0.00018
tRNArg
-
ATP-diphosphate exchange, pH 6.0
-
0.2 - 0.4
tubercidin 5'-triphosphate
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
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.63 - 3.22
Arg
0.28 - 26
ATP
0.215 - 17.9
L-arginine
0.00016 - 26
tRNAArg
0.0017 - 0.105
tRNAArg(ACG)
additional information
additional information
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
6 - 30
ATP
500 - 2800
L-arginine
300 - 1700
tRNAArg
4.8 - 75
tRNAArg(ACG)
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
150 - 180
KCl
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
160
KCl
Escherichia coli
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
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
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8.1 - 8.5
-
-
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 9.5
activity range, pH-profile, overview
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
-
assay at
50
Methanothermobacter thermautotrophicum
-
assay at
65
aminoacylaion assay
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
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
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.4
-
cytoplasmic enzyme, calculated from amino acid sequence
8.8
-
mitochondrial enzyme, calculated from amino acid sequence
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
UNIPROT
Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / 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
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50000
-
gel filtration, enzyme form II
56000 - 63000
-
gel filtration, sedimentation data
59000
-
gel filtration, sucrose density gradient centrifugation
62800
-
gel filtration
63000
-
gel filtration
67000
-
SDS-PAGE, mutant enzyme DELTANhcArgRS
67400
-
theoretical
68000
-
SDS-PAGE
68200
-
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
COMMENTARY hide
LITERATURE
monomer
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
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
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
-
sitting drop vapor diffusion method, using 50 mM HEPES (pH 7.2), 100 mM sodium acetate, 22% (w/v) PEG 3350
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
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
-
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
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20
-
24 h, stable, without glycerol
65
-
stable for 10 min
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
LITERATURE
affected by repeated freeze-thaw cycles
-
complexed arginyl-tRNA synthetase is more stable than the free enzyme
-
degradation of the enzyme during purification may be due to the influence of the immobilized tRNA, and is enhanced by high salt concentrations
-
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
-
reduced glutathione effectively protects the enzyme from thermal inactivation
-
tRNA reduces thermal inactivation
-
zinc or Triton X-100 increases thermal inactivation
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, 50% glycerol, stable for at least 3 months
-
-20C, 50% v/v glycerol, stable for at least 6 months
-
-25C, less than 30% loss of activity after 6 months
-
-75C, stable for at least 3 months
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
72000 MW form
-
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
-
Ni-NTA column chromatography and Source 15Q column chromatography
-
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+-NTA affinity resin column chromatography and Superdex 200 gel filtration
Ni2+-NTA agarose column chromatography
-
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
Methanothermobacter thermautotrophicum
-
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
two active forms which are interconvertible, I and II
-
using chromatography on Ni-nitrilotriacetic acid agarose
-
utilizing the His-tag, the tag is removed by thrombin treatment
-
utilizing the His-tag, the tag is removed by thrombin treatment, furthermore a Source15Q column is used
-
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
-
expressed in Escherichia coli BL21 Codon Plus RP cells
expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli strain MT 102
-
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 26 lethal mutants in 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
Methanothermobacter thermautotrophicum
-
expression of the native and mutant enzymes in Saccharomyces cerevisiae
-
expression of the wild type and K116G mutant in Escherichia coli
-
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
-
overexpression in Escherichia coli of wild type and several mutant enzymes
-
overexpression of the wild type and the argS1 mutant enzymes in Escherichia coli
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
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
D118A
the mutation results in a 2fold increase in binding affinity
D317A
inactive
M460V
-
mutant cannot suppress the effect of the expression of FTOR126, a variant of the wild type tRNAArg
R324A
inactive
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
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
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
-
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
DELTANArgRS
lacking the N-terminal side from the 91st residue
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
additional information
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