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Information on EC 6.1.1.19 - arginine-tRNA ligase and Organism(s) Escherichia coli and UniProt Accession B1XHE4

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Escherichia coli
UNIPROT: B1XHE4 not found.
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The taxonomic range for the selected organisms is: Escherichia coli
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
Synthetase, arginyl-transfer ribonucleate
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + L-arginine + tRNAArg = AMP + diphosphate + L-arginyl-tRNAArg
show the reaction diagram
random addition of substrates with all steps in rapid equilibrium except for the interconversion of the central quarternary complexes
-
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(ACG)
AMP + diphosphate + L-arginyl-soybean tRNAArg(ACG)
show the reaction diagram
tRNA from Glycine max
-
-
?
2'-deoxyadenosine 5'-triphosphate + L-arginine + tRNAArg
2'-deoxyadenosine 5'-monophosphate + diphosphate + L-arginyl-tRNAArg
show the reaction diagram
-
-
-
-
?
2-chloroadenosine 5'-triphosphate + L-arginine + tRNAArg
2-chloroadenosine 5'-monophosphate + diphosphate + L-arginyl-tRNAArg
show the reaction diagram
-
-
-
-
?
3'-deoxyadenosine 5'-triphosphate + L-arginine + tRNAArg
3'-deoxyadenosine 5'-monophosphate + diphosphate + L-arginyl-tRNAArg
show the reaction diagram
-
-
-
-
?
3'-methoxyadenosine 5'-triphosphate + L-arginine + tRNAArg
3'-methoxyadenosine 5'-monophosphate + diphosphate + L-arginyl-tRNAArg
show the reaction diagram
-
-
-
-
?
8-azaadenosine 5'-triphosphate + L-arginine + tRNAArg
8-azaadenosine 5'-monophosphate + diphosphate + L-arginyl-tRNAArg
show the reaction diagram
-
-
-
-
?
ATP + L-arginine + tRNAArg
AMP + diphosphate + L-arginyl-tRNAArg
show the reaction diagram
tubercidin 5'-triphosphate + L-arginine + tRNAArg
tubercidin 5'-monophosphate + diphosphate + L-arginyl-tRNAArg
show the reaction diagram
-
-
-
-
?
additional information
?
-
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
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Co2+
-
CoCl2, complete activation at a concentration of 5 mM in excess of the total ATP concentration, 24% as effective as Mg2+
Fe2+
-
FeCl2, complete activation at a concentration of 5 mM in excess of the total ATP concentration, 29% as effective as Mg2+
K+
-
50 mM is required for full activity
Mn2+
-
MnCl2, complete activation at a concentration of 5 mM in excess of the total ATP concentration, 49% as effective as Mg2+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2'-methoxyadenosine 5'-triphosphate
-
-
2-Aminopurine riboside 5'-triphosphate
-
-
6-N-Benzyladenosine 5'-triphosphate
-
-
8-azido-ATP
-
-
8-azidoadenosine 5'-triphosphate
-
-
8-bromoadenosine 5'-triphosphate
-
-
argininosuccinate
-
-
citrulline
-
-
homoarginine
-
-
K2SO4
-
45 mM
ornithine
-
-
p-hydroxymercuribenzoate
-
tRNA or DTT protects against heat inactivation
Periodate-oxidized tRNA
-
mixed type non-competitive, irreversible
-
purine riboside
-
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,2-Diaminoethane
-
supports aminoacylation in presence of crude tRNA not in presence of resolved tRNA
1,2-diaminopropane
-
supports aminoacylation in presence of crude tRNA not in presence of resolved tRNA
1,3-Diamino-2-hydroxypropane
-
supports aminoacylation in presence of crude tRNA not in presence of resolved tRNA
1,3-diaminopropane
-
supports aminoacylation in presence of crude tRNA not in presence of resolved tRNA
spermidine
-
supports aminoacylation in presence of crude tRNA not in presence of resolved tRNA
spermine
-
supports aminoacylation in presence of crude tRNA not in presence of resolved tRNA
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00029 - 0.0041
tRNAArg(ACG)
-
1.5
2'-deoxyadenosine 5'-triphosphate
-
NTP-diphosphate exchange
1.3 - 2.5
2-Chloroadenosine 5'-triphosphate
0.5
3'-Deoxyadenosine 5'-triphosphate
-
aminoacylation
0.1
3'-Methoxyadenosine 5'-triphosphate
-
aminoacylation
3 - 3.3
8-azaadenosine 5'-triphosphate
0.009 - 0.7
Arg
0.84 - 4.3
ATP
0.0073 - 0.0137
L-arginine
0.00044 - 0.0042
tRNAArg
0.2 - 0.4
tubercidin 5'-triphosphate
additional information
additional information
-
effect on the Km of several variations of the tRNAArg sequence
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0017 - 0.02
tRNAArg(ACG)
-
5.6 - 26
ATP
2 - 26
tRNAArg
additional information
additional information
-
effect on the turnover number of several variations of the tRNAArg sequence
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4.8 - 5.5
tRNAArg(ACG)
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
160
KCl
Escherichia coli
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.984
-
-
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8.1 - 8.5
-
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
60000
-
1 * 60000, SDS-PAGE
63000
-
gel filtration
68000
-
SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
-
1 * 60000, SDS-PAGE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
different tRNA acceptor stem helices are crystalized
-
hanging drop vapour diffusion method in complex form with tRNAArg at pH 5.6 using ammonium sulfate as a precipitating agent
-
sitting drop vapor diffusion method, using 50 mM HEPES (pH 7.2), 100 mM sodium acetate, 22% (w/v) PEG 3350
the tRNAArg microhelices RR-1660 and RR-1662 are crystalized
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
argS MA5002
-
mutant argS MA5002 differs from the wild-type ArgRS structural gene by one mutation, a substitution of an Arg by a Ser at position 134. It exhibits a 4times to 6times as low activity and a 5times as high Km value for ATP as the wild-type enzyme in aminoacylation and ATP-diphosphate exchange, Km values for Arg and tRNAArg remain unaltered
C320A
-
slight effect on activity
C537A
-
slight effect on activity
D118A
the mutation results in a 2fold increase in binding affinity
D317A
inactive
M460V
-
mutant cannot suppress the effect of the expression of FTOR126, a variant of the wild type tRNAArg
R324A
inactive
W162A
-
expression in Escherichia coli, 23% of wild-type activity
W172A
-
expression in Escherichia coli
W228A
-
expression in Escherichia coli
W349A
-
expression in Escherichia coli
W446A
-
expression in Escherichia coli
Y313A
the mutation results in a merely 2fold reduction in binding affinity
Y524D
-
mutant cannot suppress the effect of the expression of FTOR126, a variant of the wild type tRNAArg
additional information
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
affected by repeated freeze-thaw cycles
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 50% v/v glycerol, stable for at least 6 months
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Ni-NTA column chromatography and Source15Q column chromatography
DEAE-Sepharose CL-6B column chromatography
-
DEAE-Sepharose CL-6B column chromatography, hydroxylapatite chromatography, Sepharose CL-2B column chromatography, and Sephacryl S-300 gel filtration
-
Ni2+-NTA affinity resin column chromatography and Superdex 200 gel filtration
partial purification of recombinant enzymes using DEAE-Sepharose and Blue-Sepharose column chromatography
-
using chromatography on Ni-nitrilotriacetic acid agarose
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21 Codon Plus RP cells
expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli strain MT 102
-
overexpression in Escherichia coli
-
overexpression of the wild type and the argS1 mutant enzymes in Escherichia coli
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Eriani, G.; Dirheimer, G.; Gangloff, J.
Structure-function relationship of arginyl-tRNA synthetase from Escherichia coli: isolation and characterization of the argS mutation MA5002
Nucleic Acids Res.
18
1475-1479
1990
Escherichia coli
Manually annotated by BRENDA team
Yem, D.W.; Williams, L.S.
Evidence for the existence of two arginyl-transfer ribonucleic acid synthetase activities in Escherichia coli
J. Bacteriol.
113
891-894
1973
Escherichia coli, Escherichia coli AB1132
Manually annotated by BRENDA team
Williams, A.L.; Williams, L.S.
Control of arginine biosynthesis in Escherichia coli: characteriation of arginyl-transfer ribonucleic acid synthetase mutants
J. Bacteriol.
113
1433-1441
1973
Escherichia coli
Manually annotated by BRENDA team
Williams, A.L.; Yem, D.W.; McGinnis, E.; Williams, L.S.
Control of arginine biosynthesis in Escherichia coli: inhibition of arginyl-transfer ribonucleic acid synthetase activity
J. Bacteriol.
115
228-234
1973
Escherichia coli
Manually annotated by BRENDA team
Craine, J.E; Peterkofsky, A.
Studies of arginyl-tRNA synthetase from Escherichia coli B. Dual role of metals in enzyme catalysis
J. Biol. Chem.
251
241-246
1976
Escherichia coli, Escherichia coli B / ATCC 11303
Manually annotated by BRENDA team
Gerlo, E.; Charlier, J.
Irreversible inactivation of arginyl-tRNA ligase by periodate-oxidized tRNA
FEBS Lett.
99
25-28
1979
Escherichia coli
Manually annotated by BRENDA team
Charlier, J.; Gerlo, E.
Arginyl-tRNA synthetase from Escherichia coli K12. Purification, properties, and sequence of substrate addition
Biochemistry
18
3171-3178
1979
Escherichia coli
Manually annotated by BRENDA team
Gerlo, E.; Freist, W.; Charlier, J.
Arginyl-tRNA synthetase from Escherichia coli K12: specificity with regard to ATP analogs and their magnesium complexes
Hoppe-Seyler's Z. Physiol. Chem.
363
365-373
1982
Escherichia coli
Manually annotated by BRENDA team
Airas, R.K.
Differences in the magnesium dependences of the class I and class II aminoacyl-tRNA synthetases from Escherichia coli
Eur. J. Biochem.
240
223-231
1996
Escherichia coli
Manually annotated by BRENDA team
Yao, Y.N.; Zhang, Q.S.; Yan, X.Z.; Zhu, G.; Wang, E.D.
Escherichia coli tRNA(4)(Arg)(UCU) induces a constrained conformation of the crucial Omega-loop of arginyl-tRNA synthetase
Biochem. Biophys. Res. Commun.
313
129-134
2004
Escherichia coli
Manually annotated by BRENDA team
Liu, M.; Huang, Y.; Wu, J.; Wang, E.; Wang, Y.
Effect of cysteine residues on the activity of arginyl-tRNA synthetase from Escherichia coli
Biochemistry
38
11006-11011
1999
Escherichia coli
Manually annotated by BRENDA team
Zhang, Q.S.; Wang, E.D.; Wang, Y.L.
The role of tryptophan residues in Escherichia coli arginyl-tRNA synthetase
Biochim. Biophys. Acta
1387
136-142
1998
Escherichia coli
Manually annotated by BRENDA team
Kiga, D.; Sakamoto, K.; Sato, S.; Hirao, I.; Yokoyama, S.
Shifted positioning of the anticodon nucleotide residues of amber suppressor tRNA species by Escherichia coli arginyl-tRNA synthetase
Eur. J. Biochem.
268
6207-6213
2001
Escherichia coli
Manually annotated by BRENDA team
Zhang, Q.S.; Shen, L.; Wang, E.D.; Wang, Y.L.
Biosynthesis and characterization of 4-fluorotryptophan-labeled Escherichia coli arginyl-tRNA synthetase
J. Protein Chem.
18
187-192
1999
Escherichia coli
Manually annotated by BRENDA team
Zhou, M.; Azzi, A.; Xia, X.; Wang, E.D.; Lin, S.X.
Crystallization and preliminary X-ray diffraction analysis of E. coli arginyl-tRNA synthetase in complex form with a tRNAArg
Amino Acids
32
479-482
2007
Escherichia coli
Manually annotated by BRENDA team
Airas, R.K.
Analysis of the kinetic mechanism of arginyl-tRNA synthetase
Biochim. Biophys. Acta
1764
307-319
2006
Escherichia coli, Escherichia coli MRE 600
Manually annotated by BRENDA team
Eichert, A.; Schreiber, A.; Fuerste, J.P.; Perbandt, M.; Betzel, C.; Erdmann, V.A.; Foerster, C.
Escherichia coli tRNA(Arg) acceptor-stem isoacceptors: comparative crystallization and preliminary X-ray diffraction analysis
Acta Crystallogr. Sect. F
65
98-101
2009
Escherichia coli
Manually annotated by BRENDA team
Eichert, A.; Perbandt, M.; Oberthuer, D.; Schreiber, A.; Fuerste, J.P.; Betzel, C.; Erdmann, V.A.; Foerster, C.
Crystal structure of the E. coli tRNA(Arg) aminoacyl stem isoacceptor RR-1660 at 2.0 A resolution
Biochem. Biophys. Res. Commun.
385
84-87
2009
Escherichia coli
Manually annotated by BRENDA team
Aldinger, C.A.; Leisinger, A.K.; Igloi, G.L.
The influence of identity elements on the aminoacylation of tRNAArg by plant and Escherichia coli arginyl-tRNA synthetases
FEBS J.
279
3622-3638
2012
Escherichia coli (B1XHE4), Canavalia ensiformis (B2G3G6), Glycine max (B6ETP1), Glycine max
Manually annotated by BRENDA team
Bi, K.; Zheng, Y.; Gao, F.; Dong, J.; Wang, J.; Wang, Y.; Gong, W.
Crystal structure of E. coli arginyl-tRNA synthetase and ligand binding studies revealed key residues in arginine recognition
Protein Cell
5
151-159
2014
Escherichia coli (P11875), Escherichia coli
Manually annotated by BRENDA team