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Information on EC 6.1.1.19 - arginine-tRNA ligase and Organism(s) Homo sapiens and UniProt Accession P54136

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Homo sapiens
UNIPROT: P54136 not found.
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The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
Synonyms
arginyl-trna synthetase, argrs, rars2, arg-trna synthetase, mtargrs, arginine-trna synthetase, arginyl-transfer rna synthetase, args2, arginine-trna ligase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Arginyl-tRNA synthetase
-
Arginine translase
-
-
-
-
Arginine--tRNA ligase
-
-
-
-
Arginine-tRNA synthetase
-
-
-
-
Arginyl transfer ribonucleic acid synthetase
-
-
-
-
Arginyl-transfer RNA synthetase
-
-
-
-
Arginyl-tRNA synthetase
arginyl–tRNA synthetase
-
-
ArgRS
RARS2
-
-
Synthetase, arginyl-transfer ribonucleate
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
esterification
-
-
-
-
Aminoacylation
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-
SYSTEMATIC NAME
IUBMB Comments
L-arginine:tRNAArg ligase (AMP-forming)
-
CAS REGISTRY NUMBER
COMMENTARY hide
37205-35-9
-
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
ATP + L-arginine + tRNAArg
AMP + diphosphate + L-arginyl-tRNAArg
show the reaction diagram
additional information
?
-
-
key role in protein synthesis as part of a multienzyme complex
-
-
?
NATURAL SUBSTRATE
NATURAL 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
ATP + L-arginine + tRNAArg
AMP + diphosphate + L-arginyl-tRNAArg
show the reaction diagram
additional information
?
-
-
key role in protein synthesis as part of a multienzyme complex
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
-
-
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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
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
-
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
-
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
-
wild type enzyme, in 50 mM Tris-HCl (pH 7.5)
0.715
-
mutant enzyme DELTANhcArgRS, in 50 mM Tris-HCl (pH 7.5)
additional information
-
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
-
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
-
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
the mRNA encoding the N-terminal extension region of the enzyme has the capacity to independently recruit the E. coli ribosome
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
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
SYRC_HUMAN
660
0
75379
Swiss-Prot
other Location (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
67000
-
SDS-PAGE, mutant enzyme DELTANhcArgRS
75000
-
SDS-PAGE, wild type enzyme
SUBUNIT
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
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
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
DELTANhcArgRS
-
N-terminal 72-amino acid deletion mutant with higher specific activity than the wild type enzyme
RARSL
-
the RARSL mutation in the mitochondrial arginyl–tRNA synthetase gene is associated with pontocerebellar hypoplasia
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
HiTrap Q column chromatography and Superdex 200 gel filtration
Ni-NTA column chromatography
Ni2+ column chromatography, Mono-Q column chromatography, and Superdex 200 gel filtration
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
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli Rosetta(DE3) cells
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
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team