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Information on EC 6.1.1.2 - tryptophan-tRNA ligase and Organism(s) Homo sapiens and UniProt Accession P23381

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Word Map
The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
Synonyms
tryptophanyl-trna synthetase, trprs, wars2, mini-trprs, t2-trprs, tryptophanyl trna synthetase, htrprs, trprs1, trprs ii, trp-rs, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
mini tryptophanyl-tRNA synthetase
truncated form
mini-TrpRS
alternative splice variant
T2-TrpRS
composed of residues 94-471 of TrpRS
tryptophanyl tRNA synthetase
-
Tryptophanyl-tRNA synthase
-
trytophanyl-tRNA synthetase
-
WARS2
mitochondrial form
(Mt)TrpRS
-
-
-
-
hWRS
-
-
-
-
IFP53
-
-
-
-
Synthetase, tryptophanyl-transfer ribonucleate
-
-
-
-
T2-TrpRS
-
-
TrpRS
Tryptophan translase
-
-
-
-
Tryptophan--tRNA ligase
-
-
-
-
Tryptophanyl ribonucleic synthetase
-
-
-
-
Tryptophanyl-transfer ribonucleate synthetase
-
-
-
-
Tryptophanyl-transfer ribonucleic acid synthetase
-
-
-
-
Tryptophanyl-transfer ribonucleic synthetase
-
-
-
-
Tryptophanyl-transfer RNA synthetase
-
-
-
-
Tryptophanyl-tRNA synthase
Tryptophanyl-tRNA synthetase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + L-tryptophan + tRNATrp = AMP + diphosphate + L-tryptophyl-tRNATrp
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
esterification
Aminoacylation
esterification
Aminoacylation
PATHWAY SOURCE
PATHWAYS
-
-
SYSTEMATIC NAME
IUBMB Comments
L-tryptophan:tRNATrp ligase (AMP-forming)
-
CAS REGISTRY NUMBER
COMMENTARY hide
9023-44-3
-
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-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophan-tRNATrp
show the reaction diagram
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophanyl-tRNATrp
show the reaction diagram
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophyl-tRNATrp
show the reaction diagram
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophan-tRNATrp
show the reaction diagram
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophanyl-tRNATrp
show the reaction diagram
-
-
-
-
?
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophyl-tRNATrp
show the reaction diagram
-
-
-
-
?
L-tryptophan + ATP
L-Trp-adenylate + diphosphate
show the reaction diagram
the enzyme also catalyzes the exchange of diphosphate in the diphosphate-ATP exchange assay
-
r
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-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophan-tRNATrp
show the reaction diagram
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophanyl-tRNATrp
show the reaction diagram
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophyl-tRNATrp
show the reaction diagram
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophan-tRNATrp
show the reaction diagram
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophanyl-tRNATrp
show the reaction diagram
-
-
-
-
?
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophyl-tRNATrp
show the reaction diagram
-
-
-
-
?
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
succinylacetone
a heme biosynthesis inhibitor, inhibit cellular TrpRS activity in IFN-gamma-activated cells without affecting TrpRS protein expression
L-tryptophan
-
product inhibition at physiologic concentrations
tryptamine
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
hemin
heme can interact strongly with Zn2+-depleted full-length TrpRS, but not the Zn2+-bound enzyme, with a stoichiometric heme:protein ratio of 1:1 to enhance the aminoacylation activity significantly, involvement of heme in regulation of TrpRS aminoacylation activity, overview
glyceraldehyde 3-phosphate dehydrogenase
-
the oxidized form of glyceraldehyde 3-phosphate dehydrogenase interacts with both full-length and mini tryptophanyl-tRNA synthetase and specifically stimulates the aminoacylation potential of mini, but not full-length tryptophanyl-tRNA synthetase. In contrast, reduced glyceraldehyde 3-phosphate dehydrogenase does not bind to tryptophanyl-tRNA synthetase and does not influence their aminoacylation activity
-
interferon gamma
-
interferon regulatory factor 1
-
stimulates and regulates the enzyme isoforms expression via 2 specific interferon-gamma-sensitive promoters that are additionally regulated by the interferon gamma
-
interferons
-
interferons alpha, beta, and gamma, induction of accumulation of the enzyme, organelle-specific, the highest content is observed in the cytoplasm, followd by the nucleolus and the nucleus, the latter with a low enzyme content
-
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00029 - 0.0248
tRNATrp
0.088 - 0.4
ATP
0.0074 - 0.027
L-tryptophan
0.0011
tRNATrp
-
pH 7.5, 30°C, recombinant enzyme
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0009 - 5.11
tRNATrp
1.1 - 1.4
ATP
1.1 - 1.2
L-tryptophan
1
tRNATrp
-
pH 7.5, 30°C, recombinant enzyme
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0018
-
purified enzyme
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
-
assay at
9
exchange assay at
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
aminoacylation assay
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
22
exchange assay at, room temperature
30
-
assay at
37
-
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
peripheral blood mononuclear cells
Manually annotated by BRENDA team
-
monocyte-derived mature
Manually annotated by BRENDA team
-
umbilical vein
Manually annotated by BRENDA team
-
monocyte
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
-
enzyme TrpRS is overexpressed in OSCC tissues (139/146, 95.2%) compared with adjacent normal tissues. TrpRS knockdown or treatment with conditioned media obtained from TrpRS-knockdown cells significantly reduce oral cancer cell viability and invasiveness. TrpRS overexpression promotes cell migration and invasion. In addition, the extracellular addition of TrpRS rescues the invasion ability of TrpRS-knockdown cells. No significant association between TrpRS level and gender, age or N stage
Manually annotated by BRENDA team
-
CD4+ cell, CD8+ cell
Manually annotated by BRENDA team
-
endothelial cell
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
especially the periphery
Manually annotated by BRENDA team
-
the enzyme is secreted
-
Manually annotated by BRENDA team
-
low content
Manually annotated by BRENDA team
additional information
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
physiological function
malfunction
-
the angiostatic agent tryptophanyl-tRNA synthetase (TrpRS) is a dysregulated protein in oral squamous cell carcinoma (OSCC) based on a proteomics approach. TrpRS expression positively correlates with tumor stage, overall TNM stage, perineural invasion and tumor depth. TrpRS knockdown reduces cell viability and oral cancer cell migration and invasion
physiological function
additional information
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
SYWC_HUMAN
471
0
53165
Swiss-Prot
other Location (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
49000
transcript variant of WARS, determined by SDS-PAGE and Western blot analysis
53000
transcript variant of WARS, determined by SDS-PAGE and Western blot analysis
35000
x * 35000, recombinant His-tagged enzyme, expressed in insect cells, SDS-PAGE
53000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
method: crystal structure. Dimeric hTrpRS is structurally and functionally asymmetric with half of-the-sites reactivity
homodimer
-
?
x * 35000, recombinant His-tagged enzyme, expressed in insect cells, SDS-PAGE
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
proteolytic modification
a full-length and 3 N-terminal truncated enzyme forms by alternative splicing and proteolytic cleavage, the shortest fragment comprises the catalytic activity
phosphoprotein
-
-
proteolytic modification
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regulated mechanism, the C-terminal domain of the enzyme, which has anti-angiogenic activity and inhibits immune cells, is isolated by proteolytic cleavage or alternative splicing, the mini enzyme is a potent inhibitor of blood vessel development, the full-length enzyme is inactive, enzyme N-terminally processed by elastase, resulting in 2 different forms T1 and T2, has also anti-angiogenic activity
additional information
-
both full-length TrpRS and mini-TrpRS can be mobilized for exocytosis from endothelial cells, and the secreted TrpRS is cleaved by extracellular proteases to produce two additional N-terminally truncated fragments: T1-TrpRS (residues 71-471) and T2-TrpRS (residues 94-471)
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
catalytic fragment, hanging drop method, 0.002 ml protein solution: 8 mg/ml protein, 20 mM Tris-potassium phosphate, pH 6.8, 10 mM MgCl2, 5 mM 2-mercaptoethanol, plus equal volume of reservoir solution: 16% w/v polyethylene glycol 1500, 4% polyehylene glycol 3350, 0.2 M trisodium citrate dihydrate, pH 8.2, plus 0.0005 ml 30% 2-methyl-2,4-pentanediol, 7-10 days, 4°C, proteolytic cleavage of the enzyme into 2 fragments occurs during the crystallization process, X-ray diffraction structure determination at 2.5 A resolution using the MAD method, and analysis
crystal structure determination at 2.1 A resolution of the enzyme with a tryptophanyladenylate bound at the active site, cocrystal structure determination at 1.6 A resolution of an active fragment of the enzyme with its cognate amino acid analogue
crystal structure of hTrpRS in complexes with Trp, tryptophanamide and ATP and tryptophanyl-AMP, respectively, are all determined at 2.4 A resolution
crystals of native mini TrpRS are obtained by hanging-drop vapor diffusion at 4°C, crystal structure of human mini TrpRS is determined at a resolution of 2.3 A
purified protein in complex with uncharged tRNA and aminoacylated tRNA in a 1:1 mixture, sitting drop vapour diffusion method, 0.002 ml of protein in 10 mM HEPES, pH 7.5, 20 mM KCl, 0.02% NaN3, and 2 mM 2-mercaptoethanol, addition of 230 mM of TrpRS, 250 mM of tRNATrp, 5 mM tryptophan and 10 mM AMP-PNP, mixed with 0.002 ml reservoir solution containing 2 M ammonium sulfate and 0.1 M HEPES pH 6.9, 4°C, X-ray diffraction structure determination and analysis at 2.9 A resolution, SAD method using a selenium-labeled crystal
purified recombinant enzyme in complex with bovine tRNATrp, hanging drop vapor diffusion method, 4°C, 0.002 ml of protein solution containing 8 mg/ml of TrpRS with an equal amount of tRNA, 10 mM ATP, 1 mM Trp, 20 mM K2HPO4, pH 6.8, 10 mM MgCl2, 5 mM 2-mercaptoethanol and 0.5 mM PMSF, mixed with 0.002 ml reservoir solution containing 2 M (NH4)2SO4 and 50 mM HEPES, pH 7.0, 1-2 months, X-ray diffraction structure determination and analysis at 3.0 A resolution, modeling
structure of full length TrpRS is solved at 2.1 A, structure of mini-TRpRS is solved at 2.0 A
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A310W
T2-TrpRS mutant, AMP pocket is blocked, angiostatic activity involves the tryptophan and adenosine pockets
A7D
site-directed mutagenesis, the mutant shows reduced induction of TNF-alpha and MIP-1alpha production compared to wild-type
D382-TIEEHR-Q389
deletion of the tRNA anticodon-binding domain insertion, consisting of eight residues in the human TrpRS, abolishes the apoptotic activity of the enzyme for endothelial cells, whereas its translational catalysis and cell-binding activities remain unchanged
D99A
site-directed mutagenesis, the mutant shows reduced kcat and activity compared to the wild-type enzyme
D99E
site-directed mutagenesis, the mutant shows slightly reduced activity and kcat compared to the wild-type enzyme
D99K
site-directed mutagenesis, the mutant shows reduced kcat and activity compared to the wild-type enzyme
D99V
site-directed mutagenesis, the mutant shows reduced kcat and activity compared to the wild-type enzyme
E11L
site-directed mutagenesis, the mutant shows reduced induction of TNF-alpha and MIP-1alpha production compared to wild-type
E35G
site-directed mutagenesis, the mutant shows similar induction of TNF-alpha and MIP-1alpha production compared to wild-type
E451Q
site-directed mutagenesis, binds to VE-cadherin like the wild-type, full-length enzyme
G161W
T2-TrpRS mutant, tryptophan pocket is blocked by the bulky indole side chain of the tryptophan introduced at position 161, angiostatic activity involves the tryptophan and adenosine pockets
G172M
T2-TrpRS mutant, AMP pocket is blocked, angiostatic activity involves the tryptophan and adenosine pockets
H129A
site-directed mutagenesis, hemin binding capacity of the mutant enzymes compared to the wild-type enzyme, overview
H130R
H140A
site-directed mutagenesis, hemin binding capacity of the mutant enzymes compared to the wild-type enzyme, overview
H170A
site-directed mutagenesis, hemin binding capacity of the mutant enzymes compared to the wild-type enzyme, overview
H173A
site-directed mutagenesis, hemin binding capacity of the mutant enzymes compared to the wild-type enzyme, overview
H257A
site-directed mutagenesis, hemin binding capacity of the mutant enzymes compared to the wild-type enzyme, overview
H336A
site-directed mutagenesis, hemin binding capacity of the mutant enzymes compared to the wild-type enzyme, overview
H375A
site-directed mutagenesis, hemin binding capacity of the mutant enzymes compared to the wild-type enzyme, overview
H387A
site-directed mutagenesis, hemin binding capacity of the mutant enzymes compared to the wild-type enzyme, overview
H445A
site-directed mutagenesis, hemin binding capacity of the mutant enzymes compared to the wild-type enzyme, overview
H73A
site-directed mutagenesis, hemin binding capacity of the mutant enzymes compared to the wild-type enzyme, overview
I311E
mutation located at the appended beta1-beta2 hairpin and the AIDQ sequence of TrpRS that switch this enzyme to a tRNA-dependent mode in the tryptophan activation step
I311V
mutation located at the appended beta1-beta2 hairpin and the AIDQ sequence of TrpRS that switch this enzyme to a tRNA-dependent mode in the tryptophan activation step
K102A
site-directed mutagenesis, the mutant shows reduced kcat and activity compared to the wild-type enzyme
K102D
site-directed mutagenesis, the mutant shows reduced kcat and activity compared to the wild-type enzyme
K102I
site-directed mutagenesis, the mutant shows reduced kcat and activity compared to the wild-type enzyme
K102R
site-directed mutagenesis, the mutant shows slightly reduced activity and reduced kcat compared to the wild-type enzyme
K114Q
site-directed mutagenesis, binds to VE-cadherin like the wild-type, full-length enzyme
K153Q
site-directed mutagenesis, the human mini K153Q TrpRS mutant cannot inhibit VEGF-stimulated HUVEC migration and cannot bind to the extracellular domain of VE-cadherin
K418Q
site-directed mutagenesis, binds to VE-cadherin like the wild-type, full-length enzyme
K431A
site-directed mutagenesis, the mutant shows reduced kcat and activity compared to the wild-type enzyme
K431D
site-directed mutagenesis, the mutant shows reduced kcat and activity compared to the wild-type enzyme
K431I
site-directed mutagenesis, the mutant shows reduced kcat and activity compared to the wild-type enzyme
K431R
site-directed mutagenesis, the mutant shows reduced kcat and activity compared to the wild-type enzyme
L10D
site-directed mutagenesis, the mutant shows reduced induction of TNF-alpha and MIP-1alpha production compared to wild-type
L22G
site-directed mutagenesis, the mutant shows reduced induction of TNF-alpha and MIP-1alpha production compared to wild-type
L9D
site-directed mutagenesis, the mutant shows reduced induction of TNF-alpha and MIP-1alpha production compared to wild-type
M42D
site-directed mutagenesis, the mutant shows reduced induction of TNF-alpha and MIP-1alpha production compared to wild-type
N152G
site-directed mutagenesis, the mutant shows reduced induction of TNF-alpha and MIP-1alpha production compared to wild-type
N30G
site-directed mutagenesis, the mutant shows reduced induction of TNF-alpha and MIP-1alpha production compared to wild-type
Q145G
site-directed mutagenesis, the mutant shows reduced induction of TNF-alpha and MIP-1alpha production compared to wild-type
Q194A
site-directed mutagenesis, the mutant shows reduced kcat and activity compared to the wild-type enzyme
Q194L
site-directed mutagenesis, the mutant is inactive
R106A
site-directed mutagenesis, the mutant shows reduced kcat and activity compared to the wild-type enzyme
R106D
site-directed mutagenesis, the mutant shows reduced kcat and activity compared to the wild-type enzyme
R106I
site-directed mutagenesis, the mutant shows reduced kcat and activity compared to the wild-type enzyme
R106K
site-directed mutagenesis, the mutant shows slightly reduced activity and reduced kcat compared to the wild-type enzyme
T18G
site-directed mutagenesis, the mutant shows reduced induction of TNF-alpha and MIP-1alpha production compared to wild-type
V85A
mutation located at the appended beta1-beta2 hairpin and the AIDQ sequence of TrpRS that switch this enzyme to a tRNA-dependent mode in the tryptophan activation step, the mutant shows decreased, but visible tryptophan activation activity in the ATP-diphosphate exchange reaction
V85A/V90A
mutation located at the appended beta1-beta2 hairpin and the AIDQ sequence of TrpRS that switch this enzyme to a tRNA-dependent mode in the tryptophan activation step
V85E
mutation located at the appended beta1-beta2 hairpin and the AIDQ sequence of TrpRS that switch this enzyme to a tRNA-dependent mode in the tryptophan activation step
V85K
mutation located at the appended beta1-beta2 hairpin and the AIDQ sequence of TrpRS that switch this enzyme to a tRNA-dependent mode in the tryptophan activation step, the V85K mutant has barely detectable aminoacylation activity
V85L
mutation located at the appended beta1-beta2 hairpin and the AIDQ sequence of TrpRS that switch this enzyme to a tRNA-dependent mode in the tryptophan activation step, the V85L mutant is able to acylate bovine tRNATrp with very high effciency
V85S
mutation located at the appended beta1-beta2 hairpin and the AIDQ sequence of TrpRS that switch this enzyme to a tRNA-dependent mode in the tryptophan activation step, the mutant shows no activity in the ATP-diphosphate exchange reaction, but retains aminoacylation activity
V90A
mutation located at the appended beta1-beta2 hairpin and the AIDQ sequence of TrpRS that switch this enzyme to a tRNA-dependent mode in the tryptophan activation step, the mutant shows decreased, but visible tryptophan activation activity in the ATP-diphosphate exchange reaction, the V90 mutation enhances the hydrophobic interaction between V85 and I311
V90S
mutation located at the appended beta1-beta2 hairpin and the AIDQ sequence of TrpRS that switch this enzyme to a tRNA-dependent mode in the tryptophan activation step, the mutant shows decreased, but visible tryptophan activation activity in the ATP-diphosphate exchange reaction, the V90 mutation enhances the hydrophobic interaction between V85 and I311
Y159A
site-directed mutagenesis, the mutant shows reduced kcat and activity compared to the wild-type enzyme
Y159A/Q194A
T2-TrpRS mutant, enzyme specific recognition of the indole nitrogen of tryptophan is disrupted, angiostatic activity involves the tryptophan and adenosine pockets
Y159F
site-directed mutagenesis, the mutant shows slightly reduced activity and reduce kcat compared to the wild-type enzyme
additional information
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
tryptamine stabilizes and inhibits the enzyme
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
affinity purified using metal chelating chromatography
on a nickel affinity column
recombinant
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and dialysis, detagged enzyme by anion exchange chromatography, gel filtration, and dialysis
recombinant wild-type and mutant enzymes from Escherichia coli
the recombinant six-His-tagged proteins are purified on a nickel affinity column
large sclae, recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) derivative, 2.5fold, to homogeneity
-
recombinant from insect cells
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cDNA fragments of human full-length TrpRS, aa 1-471, mini TrpRS, aa 48-471, and T1 TrpRS, aa 71-471, are separately cloned into the pET20b vector for expression in Escherichia coli BL21DE3 cells
expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
expression of wild-type and mutant TrpRSs in Escherichia coli
gene trpS, enzyme expression in Escherichia coli strain BL21
gene WARS, constitutive expression
into the vector pET20b for expression in Escherichia coli BL21DE3 cells
overexpression of miniTrpRS in Escherichia coli BL21
protein epitope signature tags, fragments of 144 and 136 amino acids of the 53 kDa slice variant of WARS, are cloned for sequencing and for expression in Escherichia coli cells
recombinant expression of wild-type and mutant enzymes in Escherichia coli
determination of regulation involved promoter sequences
-
gene trpS, overexpression in Escherichia coli strain BL21(DE3) derivative as a His-tagged protein
-
isozyme hmtTrpRS, DNA and amino acid sequence determination and analysis, expression as C-terminally His-tagged enzyme in Spodoptera frugiperda Sf9 and HighFive BTI-NT-5B1-4 insect cells via baculovirus infection, expression as GFP-fusion protein in human 293 cells
tryptophanyl-tRNA synthetase (TrpRS) is a 53-kDa protein that consists of 471 amino acids, and a mini-TrpRS (residues 48-471) isoform is produced by alternative splicing, recombinant full-length, mini- or T2-TrpRS are constructed and expressed in OEC-M1 cells lacking endogenous TrpRS activity
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
human mini, but not full-length, TrpRS has angiostatic activity
medicine
-
TrpRS is differentially expressed in colorectal cancer and thus a potential prognostic marker
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kisselev, L.L.
Mammalian tryptophanyl-tRNA synthetases
Biochimie
75
1027-1039
1993
Bos taurus, Oryctolagus cuniculus, Ovis aries, Homo sapiens, Mammalia, Mus musculus, Primates, Rattus norvegicus, Rodentia, Ruminantia
Manually annotated by BRENDA team
Ewalt, K.L.; Schimmel, P.
Activation of angiogenic signaling pathways by two human tRNA synthetases
Biochemistry
41
13344-13349
2002
Homo sapiens
Manually annotated by BRENDA team
Paley, E.L.
Tryptamine-mediated stabilization of tryptophanyl-tRNA synthetase in human cervical carcinoma cell line
Cancer Lett.
137
1-7
1999
Homo sapiens
Manually annotated by BRENDA team
Jorgensen, R.; Sogaard, T.M.; Rossing, A.B.; Martensen, P.M.; Justesen, J.
Identification and characterization of human mitochondrial tryptophanyl-tRNA synthetase
J. Biol. Chem.
275
16820-16826
2000
Homo sapiens (Q9UGM6), Homo sapiens
Manually annotated by BRENDA team
Yu, Y.; Liu, Y.; Shen, N.; Xu, X.; Xu, F.; Jia, J.; Jin, Y.; Arnold, E.; Ding, J.
Crystal structure of human tryptophanyl-tRNA synthetase catalytic fragment: insights into substrate recognition, tRNA binding, and angiogenesis activity
J. Biol. Chem.
279
8378-8388
2004
Homo sapiens (P23381), Homo sapiens
Manually annotated by BRENDA team
Ivanova, Y.L.; Cherni, N.E.; Narovlyanskii, A.N.; Amchenkova, A.M.; Turpaev, K.T.; Popenko, V.I.
Distribution of tryptophanyl-tRNA synthetase in interferon-treated human monocytes
Mol. Biol.
32
736-742
1998
Homo sapiens
-
Manually annotated by BRENDA team
Liu, J.; Shue, E.; Ewalt, K.L.; Schimmel, P.
A new gamma-interferon-inducible promoter and splice variants of an anti-angiogenic human tRNA synthetase
Nucleic Acids Res.
32
719-727
2004
Homo sapiens
Manually annotated by BRENDA team
Yang, X.L.; Otero, F.J.; Skene, R.J.; McRee, D.E.; Schimmel, P.; de Pouplana, L.R.
Crystal structures that suggest late development of genetic code components for differentiating aromatic side chains
Proc. Natl. Acad. Sci. USA
100
15376-15380
2003
Homo sapiens (P23381), Homo sapiens
Manually annotated by BRENDA team
Xu, F.; Jia, J.; Jin, Y.; Wang, D.T.
High-level expression and single-step purification of human tryptophanyl-tRNA synthetase
Protein Expr. Purif.
23
296-300
2001
Homo sapiens
Manually annotated by BRENDA team
Wakasugi, K.; Nakano, T.; Morishima, I.
Oxidative stress-responsive intracellular regulation specific for the angiostatic form of human tryptophanyl-tRNA synthetase
Biochemistry
44
225-232
2005
Homo sapiens
Manually annotated by BRENDA team
Boasso, A.; Herbeuval, J.P.; Hardy, A.W.; Winkler, C.; Shearer, G.M.
Regulation of indoleamine 2,3-dioxygenase and tryptophanyl-tRNA-synthetase by CTLA-4-Fc in human CD4+ T cells
Blood
105
1574-1581
2005
Homo sapiens
Manually annotated by BRENDA team
Tzima, E.; Reader, J.S.; Irani-Tehrani, M.; Ewalt, K.L.; Schwartz, M.A.; Schimmel, P.
VE-cadherin links tRNA synthetase cytokine to anti-angiogenic function
J. Biol. Chem.
280
2405-2408
2005
Homo sapiens
Manually annotated by BRENDA team
Kise, Y.; Lee, S.W.; Park, S.G.; Fukai, S.; Sengoku, T.; Ishii, R.; Yokoyama, S.; Kim, S.; Nureki, O.
A short peptide insertion crucial for angiostatic activity of human tryptophanyl-tRNA synthetase
Nat. Struct. Mol. Biol.
11
149-156
2004
Homo sapiens (P23381), Homo sapiens
Manually annotated by BRENDA team
Yang, X.L.; Schimmel, P.; Ewalt, K.L.
Relationship of two human tRNA synthetases used in cell signaling
Trends Biochem. Sci.
29
250-256
2004
Homo sapiens (P23381), Homo sapiens
Manually annotated by BRENDA team
Wakasugi, K.
Human tryptophanyl-tRNA synthetase binds with heme to enhance its aminoacylation activity
Biochemistry
46
11291-11298
2007
Homo sapiens (P23381), Homo sapiens
Manually annotated by BRENDA team
Yang, X.L.; Otero, F.J.; Ewalt, K.L.; Liu, J.; Swairjo, M.A.; Koehrer, C.; RajBhandary, U.L.; Skene, R.J.; McRee, D.E.; Schimmel, P.
Two conformations of a crystalline human tRNA synthetase-tRNA complex: implications for protein synthesis
EMBO J.
25
2919-2929
2006
Homo sapiens (P23381), Homo sapiens
Manually annotated by BRENDA team
Paley, E.L.; Denisova, G.; Sokolova, O.; Posternak, N.; Wang, X.; Brownell, A.L.
Tryptamine induces tryptophanyl-tRNA synthetase-mediated neurodegeneration with neurofibrillary tangles in human cell and mouse models
Neuromolecular Med.
9
55-82
2007
Homo sapiens, Mus musculus, Mus musculus BALB/c
Manually annotated by BRENDA team
Shen, N.; Guo, L.; Yang, B.; Jin, Y.; Ding, J.
Structure of human tryptophanyl-tRNA synthetase in complex with tRNATrp reveals the molecular basis of tRNA recognition and specificity
Nucleic Acids Res.
34
3246-3258
2006
Homo sapiens (P23381), Homo sapiens
Manually annotated by BRENDA team
Guo, L.T.; Chen, X.L.; Zhao, B.T.; Shi, Y.; Li, W.; Xue, H.; Jin, Y.X.
Human tryptophanyl-tRNA synthetase is switched to a tRNA-dependent mode for tryptophan activation by mutations at V85 and I311
Nucleic Acids Res.
35
5934-5943
2007
Homo sapiens (P23381), Homo sapiens
Manually annotated by BRENDA team
Shen, N.; Zhou, M.; Yang, B.; Yu, Y.; Dong, X.; Ding, J.
Catalytic mechanism of the tryptophan activation reaction revealed by crystal structures of human tryptophanyl-tRNA synthetase in different enzymatic states
Nucleic Acids Res.
36
1288-1299
2008
Homo sapiens (P23381), Homo sapiens
Manually annotated by BRENDA team
Wakasugi, K.
An exposed cysteine residue of human angiostatic mini tryptophanyl-tRNA synthetase
Biochemistry
49
3156-3160
2010
Homo sapiens (P23381), Homo sapiens
Manually annotated by BRENDA team
Ghanipour, A.; Jirstroem, K.; Ponten, F.; Glimelius, B.; Pahlman, L.; Birgisson, H.
The prognostic significance of tryptophanyl-tRNA synthetase in colorectal cancer
Cancer Epidemiol. Biomarkers Prev.
18
2949-2956
2009
Homo sapiens
Manually annotated by BRENDA team
Wakasugi, K.
Species-specific differences in the regulation of the aminoacylation activity of mammalian tryptophanyl-tRNA synthetases
FEBS Lett.
584
229-232
2010
Bos taurus, Mus musculus, Homo sapiens (P23381), Homo sapiens
Manually annotated by BRENDA team
Hansia, P.; Ghosh, A.; Vishveshwara, S.
Ligand dependent intra and inter subunit communication in human tryptophanyl tRNA synthetase as deduced from the dynamics of structure networks
Mol. Biosyst.
5
1860-1872
2009
Homo sapiens (P23381), Homo sapiens
Manually annotated by BRENDA team
Hjelm, B.; Fernandez, C.D.; Loefblom, J.; Stahl, S.; Johannesson, H.; Rockberg, J.; Uhlen, M.
Exploring epitopes of antibodies toward the human tryptophanyl-tRNA synthetase
N. Biotechnol.
27
129-137
2010
Homo sapiens (P23381), Homo sapiens
Manually annotated by BRENDA team
Zhou, Q.; Kapoor, M.; Guo, M.; Belani, R.; Xu, X.; Kiosses, W.B.; Hanan, M.; Park, C.; Armour, E.; Do, M.H.; Nangle, L.A.; Schimmel, P.; Yang, X.L.
Orthogonal use of a human tRNA synthetase active site to achieve multifunctionality
Nat. Struct. Mol. Biol.
17
57-61
2010
Homo sapiens (P23381), Homo sapiens
Manually annotated by BRENDA team
Bhattacharyya, M.; Ghosh, A.; Hansia, P.; Vishveshwara, S.
Allostery and conformational free energy changes in human tryptophanyl-tRNA synthetase from essential dynamics and structure networks
Proteins
78
506-517
2010
Homo sapiens (P23381), Homo sapiens
Manually annotated by BRENDA team
Ahn, Y.H.; Park, S.; Choi, J.J.; Park, B.K.; Rhee, K.H.; Kang, E.; Ahn, S.; Lee, C.H.; Lee, J.S.; Inn, K.S.; Cho, M.L.; Park, S.H.; Park, K.; Park, H.J.; Lee, J.H.; Park, J.W.; Kwon, N.H.; Shim, H.; Han, B.W.; Kim, P.; Lee, J.Y.; Jeon, Y.; Huh, J.W.; Jin, M.; Kim, S.
Secreted tryptophanyl-tRNA synthetase as a primary defence system against infection
Nat. Microbiol.
2
16191
2016
Homo sapiens (P23381), Homo sapiens, Mus musculus (P32921), Mus musculus, Mus musculus C57BL/6 (P32921)
Manually annotated by BRENDA team
Lee, C.W.; Chang, K.P.; Chen, Y.Y.; Liang, Y.; Hsueh, C.; Yu, J.S.; Chang, Y.S.; Yu, C.J.
Overexpressed tryptophanyl-tRNA synthetase, an angiostatic protein, enhances oral cancer cell invasiveness
Oncotarget
6
21979-21992
2015
Homo sapiens
Manually annotated by BRENDA team
Nakamoto, T.; Miyanokoshi, M.; Tanaka, T.; Wakasugi, K.
Identification of a residue crucial for the angiostatic activity of human mini tryptophanyl-tRNA synthetase by focusing on its molecular evolution
Sci. Rep.
6
24750
2016
Bos taurus (P17248), Bos taurus, Homo sapiens (P23381), Homo sapiens, Danio rerio (Q6PBS3), Danio rerio, Arabidopsis thaliana (Q9SR15)
Manually annotated by BRENDA team