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Information on EC 6.1.1.2 - tryptophan-tRNA ligase
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EC Tree
6.1.1.2 tryptophan-tRNA ligaseSpecify your search results
Word Map
- 6.1.1.2
- synthetases
- aminoacyl-trna
- aminoacylation
- pancreas
- beef
-
anticodon
- stearothermophilus
- tyrrs
- tyrosyl-trna
- indoleamine
-
angiostatic
-
kmsks
-
ido
- tryptamine
-
tryptophan-dependent
-
aarss
- ap4a
- glutaminyl-trna
- hisrs
-
anticodon-binding
- glnrs
- medicine
- synthesis
- biotechnology
The enzyme appears in viruses and cellular organisms
Synonyms
tryptophanyl-trna synthetase, trprs, wars2, mini-trprs, t2-trprs, tryptophanyl trna synthetase, htrprs, trprs1, trprs ii, trp-rs, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
(Mt)TrpRS
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BsTRpRS
hWRS
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-
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IFP53
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-
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Synthetase, tryptophanyl-transfer ribonucleate
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T2-TrpRS
TrpRS
TrpRS1
TrpRS2
Tryptophan translase
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Tryptophan--tRNA ligase
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Tryptophanyl ribonucleic synthetase
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tryptophanyl tRNA synthetase
Tryptophanyl-transfer ribonucleate synthetase
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Tryptophanyl-transfer ribonucleic acid synthetase
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Tryptophanyl-transfer ribonucleic synthetase
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Tryptophanyl-transfer RNA synthetase
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Tryptophanyl-tRNA synthase
Tryptophanyl-tRNA synthetase
trytophanyl-tRNA synthetase
tyrosyl tRNA synthetase
WARS
WRS
additional information
TrpRS
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TrpRS
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Tryptophanyl-tRNA synthase
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Tryptophanyl-tRNA synthetase
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Tryptophanyl-tRNA synthetase
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additional information
TrpRS is a class I aminoacyl-tRNA synthetase characterized by a Rossmann-fold catalytic domain whose active site is recognizable by the presence of two conserved sequence motifs with consensus sequences HIGH and KMSKS
additional information
TrpRS is a class I aminoacyl-tRNA synthetase characterized by a Rossmann-fold catalytic domain whose active site is recognizable by the presence of two conserved sequence motifs with consensus sequences HIGH and KMSKS
additional information
TrpRS is a class I aminoacyl-tRNA synthetase characterized by a Rossmann-fold catalytic domain whose active site is recognizable by the presence of two conserved sequence motifs with consensus sequences HIGH and KMSKS
additional information
TrpRS is a class I aminoacyl-tRNA synthetase characterized by a Rossmann-fold catalytic domain whose active site is recognizable by the presence of two conserved sequence motifs with consensus sequences HIGH and KMSKS
additional information
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the enzyme belongs to the class I aminoacyl-tRNA transferases
additional information
-
the enzyme belongs to the class I aminoacyl-tRNA synthetases
additional information
TrpRS is a class I aminoacyl-tRNA synthetase characterized by a Rossmann-fold catalytic domain whose active site is recognizable by the presence of two conserved sequence motifs with consensus sequences HIGH and KMSKS
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + L-tryptophan + tRNATrp = AMP + diphosphate + L-tryptophyl-tRNATrp
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ATP + L-tryptophan + tRNATrp = AMP + diphosphate + L-tryptophyl-tRNATrp
2-step reaction, tRNATrp substrate recognition, mechanism and modeling
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ATP + L-tryptophan + tRNATrp = AMP + diphosphate + L-tryptophyl-tRNATrp
active site, 2 critical positions for amino acid discrimination
ATP + L-tryptophan + tRNATrp = AMP + diphosphate + L-tryptophyl-tRNATrp
random, bi-bi kinetic scheme mechanism, KMSKS motif loop is involved in the catalytic mechanism
ATP + L-tryptophan + tRNATrp = AMP + diphosphate + L-tryptophyl-tRNATrp
wide opening active site that adopts a compact conformation, modeling of substrate recognition and binding
ATP + L-tryptophan + tRNATrp = AMP + diphosphate + L-tryptophyl-tRNATrp
a nested, nonlinear model for the sum of metal-free and metal-catalyzed activities and its use in determining metal-free enzyme activity jointly with transition-state metal binding affinity is described, by fitting observed values obtained from Mg2+-depleted assays with increasing EDTA concentrations at known Mg2+ concentrations. Trp activation by TrpRS falls asymptotically to a plateau value 5 orders of magnitude below that observed for the Mg2+-supplemented enzyme at EDTA concentrations that reduce the free metal concentration to below 1 pmolar. The fitted regression model parameters yield a relative rate acceleration of 93000 attributable to the catalytic effect of Mg2+ and an enhanced transition state binding of Mg2+. Factorial analysis indicates that 80% of the reduction in free energy of activation effected by TrpRS arises from protein-ligand interactions
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ATP + L-tryptophan + tRNATrp = AMP + diphosphate + L-tryptophyl-tRNATrp
recognition of Trp is by an induced-fit mechanism involving conformational change of the AIDQ motif that creates a perfect pocket for the binding and activation of Trp and causes coupled movements of the N-terminal and C-terminal domains. The KMSAS loop has an inherent flexibility and binding of ATP stabilizes it in a closed conformation that secures the position of ATP for catalysis. Structural data indicate that the catalytic mechanism of the Trp activation reaction by hTrpRS involves more moderate conformational changes of the structural elements at the active site compared to bacterial TrpRS
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Aminoacylation
esterification
Aminoacylation
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esterification
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PATHWAY SOURCE
PATHWAYS
BRENDA
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SYSTEMATIC NAME
IUBMB Comments
L-tryptophan:tRNATrp ligase (AMP-forming)
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CAS REGISTRY NUMBER
COMMENTARY
9023-44-3
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + 2-azatryptophan + tRNATrp
AMP + diphosphate + 2-azatryptophyl-tRNATrp
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-
-
-
?
ATP + 4,5,6,7-tetrafluorotryptophan + tRNATrp
AMP + diphosphate + 4,5,6,7-tetrafluorotryptophyl-tRNATrp
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-
-
-
?
ATP + 4-aminotryptophan + tRNATrp
AMP + diphosphate + 4-aminotryptophyl-tRNATrp
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-
-
-
?
ATP + 4-fluorotryptophan + tRNATrp
AMP + diphosphate + 4-fluorotryptophyl-tRNATrp
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-
-
-
?
ATP + 4-hydroxytryptophan + tRNATrp
AMP + diphosphate + 4-hydroxytryptophyl-tRNATrp
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-
-
-
?
ATP + 4-methyltryptophan + tRNATrp
AMP + diphosphate + 4-methyltryptophyl-tRNATrp
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-
-
-
?
ATP + 5-aminotryptophan + tRNATrp
AMP + diphosphate + 5-aminotryptophyl-tRNATrp
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-
-
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?
ATP + 5-bromotryptophan + tRNATrp
AMP + diphosphate + 5-bromotryptophyl-tRNATrp
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-
-
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?
ATP + 5-fluorotryptophan + tRNATrp
AMP + diphosphate + 5-fluorotryptophyl-tRNATrp
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-
-
-
?
ATP + 5-hydroxy-L-tryptophan + tRNATrp
AMP + diphosphate + 5-hydroxy-L-tryptophan-tRNATrp
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mutant enzyme V144P selectively aminoacylates the cognate mutant opal suppressor tRNATrp(UCA) with 5-hydroxy-L-tryptophan and not with any endogenous amino acid
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-
?
ATP + 5-hydroxytryptophan + tRNATrp
AMP + diphosphate + 5-hydroxytryptophyl-tRNATrp
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-
-
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?
ATP + 5-iodotryptophan + tRNATrp
AMP + diphosphate + 5-iodotryptophyl-tRNATrp
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-
-
-
?
ATP + 5-methoxytryptophan + tRNATrp
AMP + diphosphate + 5-methoxytryptophyl-tRNATrp
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-
-
-
?
ATP + 5-methyltryptophan + tRNATrp
AMP + diphosphate + 5-methyltryptophyl-tRNATrp
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-
-
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?
ATP + 6-aminotryptophan + tRNATrp
AMP + diphosphate + 6-aminotryptophyl-tRNATrp
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-
-
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?
ATP + 6-fluorotryptophan + tRNATrp
AMP + diphosphate + 6-fluorotryptophyl-tRNATrp
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-
-
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?
ATP + 6-methyltryptophan + tRNATrp
AMP + diphosphate + 6-methyltryptophyl-tRNATrp
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-
-
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?
ATP + 7-aminotryptophan + tRNATrp
AMP + diphosphate + 7-aminotryptophyl-tRNATrp
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-
-
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?
ATP + 7-azatryptophan + tRNATrp
AMP + diphosphate + 7-azatryptophyl-tRNATrp
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-
-
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?
ATP + 7-methyltryptophan + tRNATrp
AMP + diphosphate + 7-methyltryptophyl-tRNATrp
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-
-
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?
ATP + L-tryptophan + Archeoglobus fulgidus tRNATrp(A73, wild-type)
AMP + diphosphate + Archeoglobus fulgidus L-tryptophanyl-tRNATrp(A73, wild-type)
preference profile regarding the discriminator base 73 of different tRNA(Trp) substrates in the order of decreasing efficiency is A, C, U, G. Modest preferences for A73 tRNA(Trp)
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-
?
ATP + L-tryptophan + Archeoglobus fulgidus tRNATrp(A73C)
AMP + diphosphate + Archeoglobus fulgidus L-tryptophanyl-tRNATrp(A73C)
preference profile regarding the discriminator base 73 of different tRNA(Trp) substrates in the order of decreasing efficiency is A, C, U, G. Modest preferences for A73 tRNA(Trp)
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-
?
ATP + L-tryptophan + Archeoglobus fulgidus tRNATrp(A73G)
AMP + diphosphate + Archeoglobus fulgidus L-tryptophanyl-tRNATrp(A73G)
preference profile regarding the discriminator base 73 of different tRNA(Trp) substrates in the order of decreasing efficiency is A, C, U, G. Modest preferences for A73 tRNA(Trp)
-
-
?
ATP + L-tryptophan + Archeoglobus fulgidus tRNATrp(A73U)
AMP + diphosphate + Archeoglobus fulgidus L-tryptophanyl-tRNATrp(A73U)
preference profile regarding the discriminator base 73 of different tRNA(Trp) substrates in the order of decreasing efficiency is A, C, U, G. Modest preferences for A73 tRNA(Trp)
-
-
?
ATP + L-tryptophan + Bacillus subtilis tRNATrp(A73, wild-type)
AMP + diphosphate + Bacillus subtilis L-tryptophanyl-tRNATrp(A73, wild-type)
preference profile regarding the discriminator base 73 of different tRNA(Trp) substrates in the order of decreasing efficiency is A, C, U, G. Modest preferences for A73 tRNA(Trp)
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-
?
ATP + L-tryptophan + Bacillus subtilis tRNATrp(A73C)
AMP + diphosphate + Bacillus subtilis L-tryptophanyl-tRNATrp(A73C)
preference profile regarding the discriminator base 73 of different tRNA(Trp) substrates in the order of decreasing efficiency is A, C, U, G. Modest preferences for A73 tRNA(Trp)
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-
?
ATP + L-tryptophan + Bacillus subtilis tRNATrp(A73G)
AMP + diphosphate + Bacillus subtilis L-tryptophanyl-tRNATrp(A73G)
preference profile regarding the discriminator base 73 of different tRNA(Trp) substrates in the order of decreasing efficiency is A, C, U, G. Modest preferences for A73 tRNA(Trp)
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?
ATP + L-tryptophan + Bacillus subtilis tRNATrp(A73U)
AMP + diphosphate + Bacillus subtilis L-tryptophanyl-tRNATrp(A73U)
preference profile regarding the discriminator base 73 of different tRNA(Trp) substrates in the order of decreasing efficiency is A, C, U, G. Modest preferences for A73 tRNA(Trp)
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?
ATP + L-tryptophan + bovine tRNATrp(G73, wild-type)
AMP + diphosphate + bovine L-tryptophanyl-tRNATrp(G73, wild-type)
preference profile regarding the discriminator base 73 of different tRNA(Trp) substrates in the order of decreasing efficiency is A, C, U, G. Modest preferences for A73 tRNA(Trp)
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-
?
ATP + L-tryptophan + bovine tRNATrp(G73A)
AMP + diphosphate + bovine L-tryptophanyl-tRNATrp(G73A)
preference profile regarding the discriminator base 73 of different tRNA(Trp) substrates in the order of decreasing efficiency is A, C, U, G. Modest preferences for A73 tRNA(Trp)
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-
?
ATP + L-tryptophan + bovine tRNATrp(G73C)
AMP + diphosphate + bovine L-tryptophanyl-tRNATrp(G73C)
preference profile regarding the discriminator base 73 of different tRNA(Trp) substrates in the order of decreasing efficiency is A, C, U, G. Modest preferences for A73 tRNA(Trp)
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-
?
ATP + L-tryptophan + bovine tRNATrp(G73U)
AMP + diphosphate + bovine L-tryptophanyl-tRNATrp(G73U)
preference profile regarding the discriminator base 73 of different tRNA(Trp) substrates in the order of decreasing efficiency is A, C, U, G. Modest preferences for A73 tRNA(Trp)
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?
ATP + L-tryptophan + tRNAArg
AMP + diphosphate + L-tryptophyl-tRNAArg
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-
-
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?
ATP + L-tryptophan + tRNATrp(A36C)
AMP + diphosphate + L-tryptophyl-tRNATrp(A36C)
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substrate mutant
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?
ATP + L-tryptophan + tRNATrp(A36G)
AMP + diphosphate + L-tryptophyl-tRNATrp(A36G)
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substrate mutant
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?
ATP + L-tryptophan + tRNATrp(A36U)
AMP + diphosphate + L-tryptophyl-tRNATrp(A36U)
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substrate mutant
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?
ATP + L-tryptophan + tRNATrp(A36U, A73G)
AMP + diphosphate + L-tryptophyl-tRNATrp(A36U, A73G)
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substrate mutant
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?
ATP + L-tryptophan + tRNATrp(A73C)
AMP + diphosphate + L-tryptophyl-tRNATrp(A73C)
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substrate mutant
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?
ATP + L-tryptophan + tRNATrp(A73G)
AMP + diphosphate + L-tryptophyl-tRNATrp(A73G)
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substrate mutant
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?
ATP + L-tryptophan + tRNATrp(A73U)
AMP + diphosphate + L-tryptophyl-tRNATrp(A73U)
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substrate mutant
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?
ATP + L-tryptophan + tRNATrp(C34A)
AMP + diphosphate + L-tryptophyl-tRNATrp(C34A)
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substrate mutant
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?
ATP + L-tryptophan + tRNATrp(C34G)
AMP + diphosphate + L-tryptophyl-tRNATrp(C34G)
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substrate mutant
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-
?
ATP + L-tryptophan + tRNATrp(C34U)
AMP + diphosphate + L-tryptophyl-tRNATrp(C34U)
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substrate mutant
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-
?
ATP + L-tryptophan + tRNATrp(C35A)
AMP + diphosphate + L-tryptophyl-tRNATrp(C35A)
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substrate mutant
-
-
?
ATP + L-tryptophan + tRNATrp(C35G)
AMP + diphosphate + L-tryptophyl-tRNATrp(C35G)
-
substrate mutant
-
-
?
ATP + L-tryptophan + tRNATrp(C35U)
AMP + diphosphate + L-tryptophyl-tRNATrp(C35U)
-
substrate mutant
-
-
?
ATP + L-tryptophan + tRNATrp(G1A-C72U)
AMP + diphosphate + L-tryptophyl-tRNATrp(G1A-C72U)
-
substrate mutant
-
-
?
ATP + L-tryptophan + tRNATrp(G1C-G72G)
AMP + diphosphate + L-tryptophyl-tRNATrp(G1C-G72G)
-
substrate mutant
-
-
?
ATP + L-tryptophan + tRNATrp(G1U-C72A)
AMP + diphosphate + L-tryptophyl-tRNATrp(G1U-C72A)
-
substrate mutant
-
-
?
ATP + L-tryptophan + tRNATrp(G2A-C71U)
AMP + diphosphate + L-tryptophyl-tRNATrp(G2A-C71U)
-
substrate mutant
-
-
?
ATP + L-tryptophan + tRNATrp(G2C-G71G)
AMP + diphosphate + L-tryptophyl-tRNATrp(G2C-G71G)
-
substrate mutant
-
-
?
ATP + L-tryptophan + tRNATrp(G2U-C71A)
AMP + diphosphate + L-tryptophyl-tRNATrp(G2U-C71A)
-
substrate mutant
-
-
?
ATP + L-tryptophan + tRNATrp(HOG1)
AMP + diphosphate + L-tryptophyl-tRNATrp(HOG1)
-
substrate mutant
-
-
?
ATP + L-tryptophan + tRNATrp(pppG1)
AMP + diphosphate + L-tryptophyl-tRNATrp(pppG1)
-
substrate mutant
-
-
?
L-tryptophan + ATP
L-Trp-adenylate + diphosphate
the enzyme also catalyzes the exchange of diphosphate in the diphosphate-ATP exchange assay
-
r
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophan-tRNATrp
-
-
-
?
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophan-tRNATrp
-
-
-
?
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophan-tRNATrp
-
-
-
?
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophan-tRNATrp
-
-
-
?
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophan-tRNATrp
-
-
-
?
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophan-tRNATrp
-
-
-
?
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophan-tRNATrp
-
-
-
-
?
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophan-tRNATrp
-
2-step reaction, tRNATrp substrate recognition, mechanism and modeling
-
?
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophan-tRNATrp
-
the 3 base pairs G2.C71, G3.C70, and G4.C69 are important identity elements in the tRNA acceptor stem providing tRNA substrate recognition for the enzyme, also the G73 discriminator base is involved in the recognition but cannot itself confer efficient aminoacylation activity
-
?
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophan-tRNATrp
-
BsTRpRS charges only the cognate mutant opal suppressor tRNATrp(UCA) and not endogenous mammalian tRNAs
-
-
?
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophan-tRNATrp
-
does not activate any natural amino acid except L-tryptophan
-
?
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophan-tRNATrp
wild-type and recombinant enzyme are specific for tRNATrp
-
?
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophan-tRNATrp
enzyme is required for embryonic survival, and is essential for viability of the fly
-
?
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophan-tRNATrp
-
-
-
?
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophan-tRNATrp
-
-
-
?
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophan-tRNATrp
-
-
-
?
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophan-tRNATrp
-
-
-
?
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophan-tRNATrp
-
-
-
?
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophan-tRNATrp
-
-
-
?
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophan-tRNATrp
-
-
-
?
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophan-tRNATrp
-
-
-
?
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophan-tRNATrp
-
-
-
?
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophan-tRNATrp
-
-
-
?
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophan-tRNATrp
-
-
?
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophan-tRNATrp
-
-
-
?
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophan-tRNATrp
-
-
-
?
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophan-tRNATrp
-
-
-
?
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophan-tRNATrp
-
-
-
?
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophan-tRNATrp
-
-
?
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophan-tRNATrp
-
-
?
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophan-tRNATrp
-
-
?
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophan-tRNATrp
-
full-length and mini enzyme isoforms
-
?
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophan-tRNATrp
-
enzyme contributes to biological processes involving cell signaling such as angiogenesis regulation
-
?
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophan-tRNATrp
-
full-length and mini enzyme isoforms, enzyme expression is regulated by a dual system of interferon gamma and interferon regulatory factor 1 via 2 specific tandem promoters leading to alternative splicing
-
?
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophan-tRNATrp
-
human mini, but not full-length, tryptophanyl-tRNA synthetase may play an important role in the intracellular regulation of protein synthesis under conditions of oxidative stress
-
-
?
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophan-tRNATrp