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Information on EC 6.1.1.19 - arginine-tRNA ligase and Organism(s) Pyrococcus horikoshii and UniProt Accession O59147

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Pyrococcus horikoshii
UNIPROT: O59147 not found.
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The taxonomic range for the selected organisms is: Pyrococcus horikoshii
The enzyme appears in selected viruses and cellular organisms
Synonyms
arginyl-trna synthetase, argrs, rars2, arg-trna synthetase, arginine-trna synthetase, arginyl-transfer rna synthetase, mtargrs, args2, arginine-trna ligase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Arg-tRNA synthetase
-
Arginine translase
-
-
-
-
Arginine--tRNA ligase
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-
-
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Arginine-tRNA synthetase
-
-
-
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Arginyl transfer ribonucleic acid synthetase
-
-
-
-
Arginyl-transfer RNA synthetase
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-
-
-
Arginyl-tRNA synthetase
-
-
-
-
ArgRS
-
-
-
-
Synthetase, arginyl-transfer ribonucleate
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
esterification
-
-
-
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Aminoacylation
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-
SYSTEMATIC NAME
IUBMB Comments
L-arginine:tRNAArg ligase (AMP-forming)
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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
-
-
-
?
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
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0026 - 0.0038
tRNAArg
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
aminoacylaion assay
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
65
aminoacylaion assay
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
a crystal structure of a complex of Arg-tRNA synthetase, tRNAArgCCU, and the ATP analog ANP is determined to 2.0 A resolution
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
DELTANArgRS
lacking the N-terminal side from the 91st residue
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
on a Ni2+-nitrilotriacetic superflow, a Resource Q, a Hitrap heparin, and a hydroxyapatite column
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
into the TOPO vector and subsequently into the vector pET28c for expression in Escherichia coli BL21DE3codon+ cells
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Konno, M.; Sumida, T.; Uchikawa, E.; Mori, Y.; Yanagisawa, T.; Sekine, S.; Yokoyama, S.; Yokoyama, S.
Modeling of tRNA-assisted mechanism of Arg activation based on a structure of Arg-tRNA synthetase, tRNA, and an ATP analog (ANP)
FEBS J.
276
4763-4779
2009
Pyrococcus horikoshii (O59147), Pyrococcus horikoshii
Manually annotated by BRENDA team