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Information on EC 6.1.1.19 - arginine-tRNA ligase and Organism(s) Thermus thermophilus and UniProt Accession Q93RP5

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This record set is specific for:
Thermus thermophilus
UNIPROT: Q93RP5 not found.
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The taxonomic range for the selected organisms is: Thermus thermophilus
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
Arginine translase
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-
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Arginine--tRNA ligase
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-
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Arginine-tRNA synthetase
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Arginyl transfer ribonucleic acid synthetase
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Arginyl-transfer RNA synthetase
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Arginyl-tRNA synthetase
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-
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ArgRS
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Synthetase, arginyl-transfer ribonucleate
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
esterification
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Aminoacylation
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-
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PATHWAY SOURCE
PATHWAYS
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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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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
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-
-
?
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0098
tRNAArg
adenine at position 20 of the tRNAArg is required for activity, pH 7.5, 65°C
additional information
additional information
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
K116G mutant displays very low activity compared to wild type enzyme
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
Q93RP5_THETH
592
0
66227
TrEMBL
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structure solved by multiple isomorphous replacement
crystallized by the hanging-drop vapour-diffusion method using ethylene glycol as precipitant
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
K116G
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expression of the mutant in Escherichia coli
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purification of the wild type and K116G mutant, expressed in Escherichia coli, by DEAE-Sephacel and PhenylSuperose column chromatography
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
overexpressed in Escherichia coli under the control of the T7 promoter
overexpression in Escherichia coli of wild type and several mutant enzymes
expression of the wild type and K116G mutant in Escherichia coli
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team