Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 6.1.1.19 - arginine-tRNA ligase and Organism(s) Rattus norvegicus and UniProt Accession P40329

for references in articles please use BRENDA:EC6.1.1.19
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Rattus norvegicus
UNIPROT: P40329 not found.
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
hide
The taxonomic range for the selected organisms is: Rattus norvegicus
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
-
-
-
-
ArgRS
-
-
-
-
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
?
show the reaction diagram
additional information
?
-
-
the free enzyme provides arginyl-tRNA for the NH2-terminal arginine modification of proteins by arginyl-tRNA:protein arginyltransferase, EC 2.3.2.8
-
-
?
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
?
show the reaction diagram
-
the complexed enzyme supplies arginyl-tRNA for the protein synthesis
-
-
?
additional information
?
-
-
the free enzyme provides arginyl-tRNA for the NH2-terminal arginine modification of proteins by arginyl-tRNA:protein arginyltransferase, EC 2.3.2.8
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
diphosphate
-
50% inhibition at 0.033 mM (free enzyme), at 0.040 (complexed enzyme)
KCl
-
50% inhibition: at 150 mM (free enzyme), at 180 mM (complexed enzyme)
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0033 - 0.0045
Arg
0.41 - 0.43
ATP
0.004 - 0.028
tRNAArg
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
-
-
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
150 - 180
KCl
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
SYRC_RAT
660
0
75810
Swiss-Prot
other Location (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
240000
-
gel filtration
56000 - 63000
-
gel filtration, sedimentation data
60000
72000
-
x * 72000, component of the multienzyme aminoacyl-tRNA synthetase complex, the 12000 MW NH2-terminal extension makes this form much more hydrophobic than the smaller one, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 70000, SDS-PAGE
monomer
-
1 * 60000, SDS-PAGE
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
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 50% glycerol, stable for at least 3 months
-
-75°C, stable for at least 3 months
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
72000 MW form
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
at 24 h, the expression levels of enzyme protein and mRNA in ischemic penumbral tissues are lower than those in normal tissue
ischemic preconditioning can inhibit the increased enzyme activity and down-regulate enzyme expression of ischemia-insulted neurons
prolonged ischemia insult can induce an escalating activity of the enzyme and leads to enzyme over-expression in primary cultured neurons
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Sivaram, P.; Vellekamp, G.; Deutscher, M.P.
A role for lipids in the functional and structural properties of the rat liver aminoacyl-tRNA synthetase complex
J. Biol. Chem.
263
18891-18896
1988
Rattus norvegicus
Manually annotated by BRENDA team
Huang, S.; Deutscher, M.P.
The NH2-terminal extension of rat liver arginyl-tRNA synthetase is responsible for its hydrophobic properties
Biochem. Biophys. Res. Commun.
180
702-708
1991
Rattus norvegicus
Manually annotated by BRENDA team
Sivaram, P.; Deutscher, M.P.
Existence of two forms of rat liver arginyl-tRNA synthetase suggests channeling of aminoacyl-tRNA for protein synthesis
Proc. Natl. Acad. Sci. USA
87
3665-3669
1990
Rattus norvegicus
Manually annotated by BRENDA team
Deutscher, M.P.; Ni, R.C.
Purification of a low molecular weight form of rat liver arginyl-tRNA synthetase
J. Biol. Chem.
257
6003-6006
1982
Rattus norvegicus
Manually annotated by BRENDA team
Vellekamp, G.; Sihag, R.K.; Deutscher, M.P.
Comparison of the complexed and free forms of rat liver arginyl-tRNA synthetase and origin of the free form
J. Biol. Chem.
260
9843-9847
1985
Rattus norvegicus
Manually annotated by BRENDA team
Glinski, R.L.; Gainey, P.C.; Mawhinney, T.P.; Hilderman, R.H.
Evidence that lysyl- and/or arginyl-tRNA synthetases from rat liver contain carbohydrate
Biochem. Biophys. Res. Commun.
88
1052-1061
1979
Rattus norvegicus
Manually annotated by BRENDA team
Van Dang, C.; Mawhinney, T.P.; Hilderman, R.H.
Characterization of a homogeneous arginyl- and lysyl-tRNA synthetase complex isolated from rat liver. Arginyl- and lysyl-tRNA synthetases contain carbohydrates
Biochemistry
21
4891-4895
1982
Rattus norvegicus
Manually annotated by BRENDA team
Fu, R.; Fan, Y.Z.; Fan, Y.C.; Zhao, H.Y.
Expression of arginyl-tRNA synthetase in rats with focal cerebral ischemia
J. Huazhong Univ. Sci. Technol. Med. Sci.
34
172-175
2014
Rattus norvegicus (P40329)
Manually annotated by BRENDA team
Shen, Y.; Zhao, H.Y.; Wang, H.J.; Wang, W.L.; Zhang, L.Z.; Fu, R.
Ischemic preconditioning inhibits over-expression of arginyl-tRNA synthetase gene Rars in ischemia-injured neurons
J. Huazhong Univ. Sci. Technol. Med. Sci.
36
554-557
2016
Rattus norvegicus (P40329)
Manually annotated by BRENDA team