Information on EC 6.1.1.19 - arginine-tRNA ligase and Organism(s) Homo sapiens

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


The taxonomic range for the selected organisms is: Homo sapiens

EC NUMBER
COMMENTARY hide
6.1.1.19
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RECOMMENDED NAME
GeneOntology No.
arginine-tRNA ligase
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Aminoacylation
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esterification
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-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
tRNA charging
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arginine metabolism
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Aminoacyl-tRNA biosynthesis
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SYSTEMATIC NAME
IUBMB Comments
L-arginine:tRNAArg ligase (AMP-forming)
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CAS REGISTRY NUMBER
COMMENTARY hide
37205-35-9
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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
ATP + L-arginine + tRNAArg
AMP + diphosphate + L-arginyl-tRNAArg
show the reaction diagram
additional information
?
-
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key role in protein synthesis as part of a multienzyme complex
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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
AMP + diphosphate + L-arginyl-tRNAArg
show the reaction diagram
additional information
?
-
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key role in protein synthesis as part of a multienzyme complex
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-
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Hemin
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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
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.501 - 0.91
ATP
0.0035 - 0.0078
L-arginine
0.00005 - 0.0096
tRNAArg
additional information
additional information
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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 hide
LITERATURE
IMAGE
0.28 - 15.5
ATP
0.41 - 17.9
L-arginine
0.32 - 16.5
tRNAArg
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
6 - 30
ATP
500 - 2800
L-arginine
300 - 1700
tRNAArg
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.286
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wild type enzyme, in 50 mM Tris-HCl (pH 7.5)
0.715
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mutant enzyme DELTANhcArgRS, in 50 mM Tris-HCl (pH 7.5)
additional information
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comparison of aminoacylation activity of Escherichia coli ArgRS and human truncated DELTANhcArgRS in presence of hemin, overview
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
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assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
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assay at
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
UNIPROT
ORGANISM
Homo sapiens;
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
67000
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SDS-PAGE, mutant enzyme DELTANhcArgRS
75000
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SDS-PAGE, wild type enzyme
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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
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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
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
HiTrap Q column chromatography and Superdex 200 gel filtration
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Ni-NTA column chromatography
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Ni-NTA Superflow resin chromatography and dialysis against 20 mM potassium phosphate buffer (pH 7.5)
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Ni2+ column chromatography, Mono-Q column chromatography, and Superdex 200 gel filtration
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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
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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
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deduced amino acid sequence shows 87.7% identity to the CHO enzyme and 37.7% identity to the homologous Escherichia coli enzyme
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expressed in Escherichia coli
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expressed in Escherichia coli BL21(DE3) cells
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expressed in Escherichia coli Rosetta(DE3) cells
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full-length enzyme and mutant DELTA1-72 tagged with green fluorescence protein, expression in 293 T cells, exclusively in cytosol
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
DELTANhcArgRS
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N-terminal 72-amino acid deletion mutant with higher specific activity than the wild type enzyme
RARSL
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the RARSL mutation in the mitochondrial arginyl–tRNA synthetase gene is associated with pontocerebellar hypoplasia