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ATP + 2-azatryptophan + tRNATrp
AMP + diphosphate + 2-azatryptophyl-tRNATrp
-
-
-
?
ATP + 4,5,6,7-tetrafluorotryptophan + tRNATrp
AMP + diphosphate + 4,5,6,7-tetrafluorotryptophyl-tRNATrp
-
-
-
?
ATP + 4-aminotryptophan + tRNATrp
AMP + diphosphate + 4-aminotryptophyl-tRNATrp
-
-
-
?
ATP + 4-fluorotryptophan + tRNATrp
AMP + diphosphate + 4-fluorotryptophyl-tRNATrp
-
-
-
?
ATP + 4-hydroxytryptophan + tRNATrp
AMP + diphosphate + 4-hydroxytryptophyl-tRNATrp
-
-
-
?
ATP + 4-methyltryptophan + tRNATrp
AMP + diphosphate + 4-methyltryptophyl-tRNATrp
-
-
-
?
ATP + 5-aminotryptophan + tRNATrp
AMP + diphosphate + 5-aminotryptophyl-tRNATrp
-
-
-
?
ATP + 5-bromotryptophan + tRNATrp
AMP + diphosphate + 5-bromotryptophyl-tRNATrp
-
-
-
?
ATP + 5-fluorotryptophan + tRNATrp
AMP + diphosphate + 5-fluorotryptophyl-tRNATrp
-
-
-
?
ATP + 5-hydroxy-L-tryptophan + tRNATrp
AMP + diphosphate + 5-hydroxy-L-tryptophan-tRNATrp
-
mutant enzyme V144P selectively aminoacylates the cognate mutant opal suppressor tRNATrp(UCA) with 5-hydroxy-L-tryptophan and not with any endogenous amino acid
-
?
ATP + 5-hydroxytryptophan + tRNATrp
AMP + diphosphate + 5-hydroxytryptophyl-tRNATrp
-
-
-
?
ATP + 5-iodotryptophan + tRNATrp
AMP + diphosphate + 5-iodotryptophyl-tRNATrp
-
-
-
?
ATP + 5-methoxytryptophan + tRNATrp
AMP + diphosphate + 5-methoxytryptophyl-tRNATrp
-
-
-
?
ATP + 5-methyltryptophan + tRNATrp
AMP + diphosphate + 5-methyltryptophyl-tRNATrp
-
-
-
?
ATP + 6-aminotryptophan + tRNATrp
AMP + diphosphate + 6-aminotryptophyl-tRNATrp
-
-
-
?
ATP + 6-fluorotryptophan + tRNATrp
AMP + diphosphate + 6-fluorotryptophyl-tRNATrp
-
-
-
?
ATP + 6-methyltryptophan + tRNATrp
AMP + diphosphate + 6-methyltryptophyl-tRNATrp
-
-
-
?
ATP + 7-aminotryptophan + tRNATrp
AMP + diphosphate + 7-aminotryptophyl-tRNATrp
-
-
-
?
ATP + 7-azatryptophan + tRNATrp
AMP + diphosphate + 7-azatryptophyl-tRNATrp
-
-
-
?
ATP + 7-methyltryptophan + tRNATrp
AMP + diphosphate + 7-methyltryptophyl-tRNATrp
-
-
-
?
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)
-
?
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)
-
?
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)
-
?
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)
-
?
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)
-
?
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)
-
?
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)
-
?
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)
-
?
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)
-
?
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)
-
?
ATP + L-tryptophan + tRNAArg
AMP + diphosphate + L-tryptophyl-tRNAArg
-
-
-
?
ATP + L-tryptophan + tRNATrp
?
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophan-tRNATrp
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophanyl-tRNATrp
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophyl-tRNATrp
ATP + L-tryptophan + tRNATrp(A36C)
AMP + diphosphate + L-tryptophyl-tRNATrp(A36C)
-
substrate mutant
-
?
ATP + L-tryptophan + tRNATrp(A36G)
AMP + diphosphate + L-tryptophyl-tRNATrp(A36G)
-
substrate mutant
-
?
ATP + L-tryptophan + tRNATrp(A36U)
AMP + diphosphate + L-tryptophyl-tRNATrp(A36U)
-
substrate mutant
-
?
ATP + L-tryptophan + tRNATrp(A36U, A73G)
AMP + diphosphate + L-tryptophyl-tRNATrp(A36U, A73G)
-
substrate mutant
-
?
ATP + L-tryptophan + tRNATrp(A73C)
AMP + diphosphate + L-tryptophyl-tRNATrp(A73C)
-
substrate mutant
-
?
ATP + L-tryptophan + tRNATrp(A73G)
AMP + diphosphate + L-tryptophyl-tRNATrp(A73G)
-
substrate mutant
-
?
ATP + L-tryptophan + tRNATrp(A73U)
AMP + diphosphate + L-tryptophyl-tRNATrp(A73U)
-
substrate mutant
-
?
ATP + L-tryptophan + tRNATrp(C34A)
AMP + diphosphate + L-tryptophyl-tRNATrp(C34A)
-
substrate mutant
-
?
ATP + L-tryptophan + tRNATrp(C34G)
AMP + diphosphate + L-tryptophyl-tRNATrp(C34G)
-
substrate mutant
-
?
ATP + L-tryptophan + tRNATrp(C34U)
AMP + diphosphate + L-tryptophyl-tRNATrp(C34U)
-
substrate mutant
-
?
ATP + L-tryptophan + tRNATrp(C35A)
AMP + diphosphate + L-tryptophyl-tRNATrp(C35A)
-
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
L-tryptophan + ATP + ADP
P1,P3-bis(5'-adenosyl)triphosphate + ?
-
-
-
?
L-tryptophan + ATP + NH3
L-tryptophanamide + AMP + diphosphate
-
-
-
?
P1,P3-bis(5'-adenosyl)triphosphate + L-tryptophan + tRNATrp
?
additional information
?
-
ATP + L-tryptophan + tRNATrp

?
-
-
-
?
ATP + 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
-
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
-
-
-
?
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
-
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
-
-
?
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
-
-
-
?
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
-
activity and fidelity are essential for viability
-
?
ATP + L-tryptophan + tRNATrp

AMP + diphosphate + L-tryptophanyl-tRNATrp
-
-
-
?
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophanyl-tRNATrp
-
-
?
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophanyl-tRNATrp
a two-step reaction of amino acid activation followed by aminoacylation, catalysis of amino acid activation involves three allosteric states: 1.open, 2. closed pre-transition state involving Mg2+ and an active site lysine residue, and 3. closed producs, the interconversions of these states entail significant domain motions driven by ligand binding, molecular dynamic simulations, overview
-
?
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophanyl-tRNATrp
-
-
-
?
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophanyl-tRNATrp
-
-
?
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophanyl-tRNATrp
-
-
-
?
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophanyl-tRNATrp
-
-
?
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophanyl-tRNATrp
involvement of heme in regulation of TrpRS aminoacylation activity
-
?
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophanyl-tRNATrp
bovine tRNATrp substrate, a two step reaction, the tryptophanyl-tRNA synthetase is a class I amino acid tRNA-synthetase, that catalyzes tryptophan activation in the absence of its cognate tRNA, cognate tRNA is not obligatory to catalyze amino acid activation, the integrated 3ā end of the tRNA is necessary to activate the ATP-diphosphate exchange reaction, overview
-
?
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophanyl-tRNATrp
tRNA substrate from Bos taurus, a two step reaction: the amino acid is first activated by ATP to form an aminoacyl-AMP, which is then transferred to the 3' end of the cognate tRNA to form an aminoacyl-tRNA, the discriminator base A73 of the tRNA is specifically recognized by an alpha-helix of the unique N-terminal domain and the anticodon loop by an alpha-helix insertion of the C-terminal domain, the N-terminal domain is involved in Trp activation, but is not essential for tRNA binding and acylation, tryptophan, anticodon, and acceptor arm recognition mechanisms, overview
-
?
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophanyl-tRNATrp
tRNA substrate from Bos taurus, tryptophan binding pocket structure, overview, two distinct tRNA conformations: uncharged tRNA is bound across the dimer, with anticodon and acceptor stem interacting with separate subunits, in this cross-dimer tRNA complex, the class I enzyme has a class II-like tRNA binding mode, the aminoacylated tRNA is bound only by the anticodon, the acceptor stem being free and having space to interact precisely with EF-1a, suggesting that the product of aminoacylation can be directly handed off to EF-1alpha for the next step of protein synthesis, recognition mechanisms, overview
-
?
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophanyl-tRNATrp
tRNA substrate from Saccharomyces cerevisiae
-
?
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophanyl-tRNATrp
-
-
-
?
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophanyl-tRNATrp
-
-
-
?
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophanyl-tRNATrp
-
-
?
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophanyl-tRNATrp
the enzyme is essential for translation
-
?
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophanyl-tRNATrp
-
both TrpRS1 and TrpRS2 are essential for growth and required for cytosolic and mitochondrial tryptophanyl-tRNA formation, respectively, the edited anticodon and the mitochondria-specific thiolation of U33 in the imported tRNATrp act as antideterminants for the cytosolic TrpRS1, the mitochondrion of Trypanosoma brucei does not encode any tRNAs, this deficiency is compensated for by the import of a small fraction of nearly all of its cytosolic tRNAs from the host
-
?
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophanyl-tRNATrp
-
because of editing in the mitochondrion, cytosolic and mitochondrial tRNATrp differ in an anticodon nucleotide and substrate specificity, although neither enzyme is able to recognize in vitro transcripts corresponding to unedited or edited tRNATrp, both efficiently aminoacylate isolated Trypanosoma brucei cytosolic tRNA in in vitro charging assays, overview
-
?
ATP + L-tryptophan + tRNATrp

AMP + diphosphate + L-tryptophyl-tRNATrp
-
-
?
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophyl-tRNATrp
the anticodon nucleotides C34, C35 and A36, discriminator base A73, G1-C72 and G2-C71 base pairs of acceptor stem are base-specifically recognized by the tryptophanyl-tRNA synthetase
-
?
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophyl-tRNATrp
-
-
?
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophyl-tRNATrp
the anticodon nucleotides C34, C35 and A36, discriminator base A73, G1-C72 and G2-C71 base pairs of acceptor stem are base-specifically recognized by the tryptophanyl-tRNA synthetase
-
?
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophyl-tRNATrp
-
-
-
?
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophyl-tRNATrp
-
-
?
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophyl-tRNATrp
-
-
-
?
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophyl-tRNATrp
-
-
?
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophyl-tRNATrp
-
-
?
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophyl-tRNATrp
N-terminally truncated Cryptosporidium parvum TrpRS is able to charge Escherichia coli tRNATrp with 3H-labeled tryptophan. The N-terminal extension domain is not required for activity
-
?
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophyl-tRNATrp
-
-
?
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophyl-tRNATrp
-
-
-
?
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophyl-tRNATrp
-
-
-
?
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophyl-tRNATrp
-
-
?
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophyl-tRNATrp
-
-
-
?
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophyl-tRNATrp
-
-
-
?
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophyl-tRNATrp
-
the active site is located in a deep, long pocket within the catalytic domain, and is surrounded by several conserved features
-
?
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophyl-tRNATrp
-
-
-
?
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophyl-tRNATrp
-
-
?
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophyl-tRNATrp
-
-
-
?
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophyl-tRNATrp
-
-
?
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophyl-tRNATrp
-
-
-
?
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophyl-tRNATrp
-
-
?
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophyl-tRNATrp
-
-
-
?
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophyl-tRNATrp
-
-
?
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophyl-tRNATrp
-
-
-
?
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophyl-tRNATrp
-
-
-
?
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophyl-tRNATrp
-
-
?
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophyl-tRNATrp
-
-
-
?
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophyl-tRNATrp
-
-
?
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophyl-tRNATrp
-
-
-
?
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophyl-tRNATrp
-
-
?
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophyl-tRNATrp
-
-
?
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophyl-tRNATrp
-
-
-
?
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophyl-tRNATrp
-
Trp and AMP binding structures, overview
-
?
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophyl-tRNATrp
-
-
-
?
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophyl-tRNATrp
-
-
?
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophyl-tRNATrp
-
-
?
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophyl-tRNATrp
-
-
?
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophyl-tRNATrp
neither isoform is capable of charging recombinant Escherichia coli tRNATrp, they are specific for trypanosomal tRNATrp
-
?
P1,P3-bis(5'-adenosyl)triphosphate + L-tryptophan + tRNATrp

?
-
-
-
?
P1,P3-bis(5'-adenosyl)triphosphate + L-tryptophan + tRNATrp
?
-
-
-
?
additional information

?
-
-
tryptophan-dependent ATP-diphosphate exchange: tryptophan + ATP + enzyme /Trp-AMP-enzyme + diphosphate
-
?
additional information
?
-
-
enzyme also performs the ATP-diphosphate exchange reaction
-
?
additional information
?
-
-
-
-
?
additional information
?
-
-
binding stoichiometry of tRNATrp and tryptophanyl-tRNA synthetase
-
?
additional information
?
-
-
no P1,P4-bis(5'-adenosyl)tetraphosphate synthesis
-
?
additional information
?
-
-
tryptophan-dependent ATP-diphosphate exchange: tryptophan + ATP + enzyme /Trp-AMP-enzyme + diphosphate
-
?
additional information
?
-
-
tryptophan-dependent ATP-diphosphate exchange: tryptophan + ATP + enzyme /Trp-AMP-enzyme + diphosphate
-
?
additional information
?
-
-
possibly involved in function other than tRNA aminoacylation
-
?
additional information
?
-
-
enzyme might by implicated in regulation of P1,P3-bis(5'-adenosyl)triphosphate/P1,P4-bis(5'-adenosyl)tetraphosphate ratio in the cell
-
?
additional information
?
-
-
tryptophanyl tRNA synthetase II interacts with nitric oxide synthetase and increases activity of nitric oxide synthetase
-
?
additional information
?
-
the homologue with defective active site is not capable of charging tRNA
-
?
additional information
?
-
the homologue with defective active site is not capable of charging tRNA
-
?
additional information
?
-
the homologue with defective active site is not capable of charging tRNA
-
?
additional information
?
-
-
the homologue with defective active site is not capable of charging tRNA
-
?
additional information
?
-
enzyme also performs the ATP-diphosphate exchange reaction
-
?
additional information
?
-
ligand-linked conformational stability changes associated with this catalytic cycle, overview
-
?
additional information
?
-
-
ligand-linked conformational stability changes associated with this catalytic cycle, overview
-
?
additional information
?
-
-
TrpRS MCD catalytic activity verifies a key prediction of the Rodin-Ohno hypothesis, overview
-
?
additional information
?
-
the enzyme also accepts L-tyrosine as substrate, albeit with lower catalytic efficiency
-
?
additional information
?
-
-
the enzyme also accepts L-tyrosine as substrate, albeit with lower catalytic efficiency
-
?
additional information
?
-
-
an ancestral tryptophanyl-tRNA synthetase precursor achieves high catalytic rate enhancement without ordered ground-state tertiary structures
-
?
additional information
?
-
-
modeling of probable tRNA binding, overview
-
?
additional information
?
-
-
mini isozyme specifically shows anti-proliferative and anti-angiogenic activity
-
?
additional information
?
-
the catalytic fragment exhibits potent angiostatic activity
-
?
additional information
?
-
-
the catalytic fragment exhibits potent angiostatic activity
-
?
additional information
?
-
-
the enzymes C-terminal domain, an EMAP II-like protein, inhibits angiogenesis signaling pathways and the development of blood vessels
-
?
additional information
?
-
-
interferon-gamma-inducible enzyme. Exposure to soluble cytotoxic T lymphocyte antigen-4 induces increased expression of tryptophanyl-tRNA synthetase in unseparated peripheral blood mononuclear cells, as well as in monocyte-derived mature dentritic cells. CD4+ cells and CD8+ cells isolated from peripheral blood mononuclear cells treated with soluble cytotoxic T lymphocyte antigen-4 show increased tryptophanyl-tRNA synthetase compared with untreated cells. Possibility that tryptophanyl-tRNA synthetase may be involved in an important mechanism regulating immune response
-
?
additional information
?
-
-
the vascular endothelial-cadherin-dependent pathway is proposed to link T2-TrpRS to inhibition of new blood vessel formation
-
?
additional information
?
-
-
tryptamine induces tryptophanyl-tRNA synthetase-mediated neurodegeneration with neurofibrillary tangles in human cell models, the dietary supplementation with tryptophan as a tryptamine competitor may not counteract the deleterious influence of tryptamine, overview
-
?
additional information
?
-
the enzyme interacts directly with elongation factor 1alpha, which carries charged tRNA to the ribosome
-
?
additional information
?
-
-
the enzyme interacts directly with elongation factor 1alpha, which carries charged tRNA to the ribosome
-
?
additional information
?
-
vascular endothelial cadherins tryptophan side chains fit into the tryptophan-specific active site of the synthetase
-
?
additional information
?
-
-
vascular endothelial cadherins tryptophan side chains fit into the tryptophan-specific active site of the synthetase
-
?
additional information
?
-
binding of vascular endothelial (VE)-cadherin, the NH2-terminal Trp2 and Trp4 residues of VE-cadherin are docked into the Trp- and adenosine-binding pockets of human TrpRS
-
?
additional information
?
-
-
binding of vascular endothelial (VE)-cadherin, the NH2-terminal Trp2 and Trp4 residues of VE-cadherin are docked into the Trp- and adenosine-binding pockets of human TrpRS
-
?
additional information
?
-
potential complex formation between TLR4-MD2 and the WRS monomer, putative binding model of TLR4-MD2 with the enzyme WRS homodimer based on a protein-protein docking study, complex crystal structure analysis, overview
-
?
additional information
?
-
-
potential complex formation between TLR4-MD2 and the WRS monomer, putative binding model of TLR4-MD2 with the enzyme WRS homodimer based on a protein-protein docking study, complex crystal structure analysis, overview
-
?
additional information
?
-
-
not: dATP
-
?
additional information
?
-
-
tryptamine induces tryptophanyl-tRNA synthetase-mediated neurodegeneration with neurofibrillary tangles in mouse models, the dietary supplementation with tryptophan as a tryptamine competitor may not counteract the deleterious influence of tryptamine, overview
-
?
additional information
?
-
-
tryptamine induces tryptophanyl-tRNA synthetase-mediated neurodegeneration with neurofibrillary tangles in mouse models, the dietary supplementation with tryptophan as a tryptamine competitor may not counteract the deleterious influence of tryptamine, overview
-
?
additional information
?
-
-
probably the enzyme fulfills some unknown function(s) important for digestion
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ATP + L-tryptophan + tRNATrp
?
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophan-tRNATrp
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophanyl-tRNATrp
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophyl-tRNATrp
additional information
?
-
ATP + L-tryptophan + tRNATrp

?
-
-
-
-
?
ATP + 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
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
-
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
-
activity and fidelity are essential for viability
-
?
ATP + L-tryptophan + tRNATrp

AMP + diphosphate + L-tryptophanyl-tRNATrp
-
-
-
-
?
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophanyl-tRNATrp
-
-
-
?
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophanyl-tRNATrp
-
-
-
-
?
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophanyl-tRNATrp
-
-
-
?
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophanyl-tRNATrp
-
-
-
-
?
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophanyl-tRNATrp
-
-
-
?
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophanyl-tRNATrp
involvement of heme in regulation of TrpRS aminoacylation activity
-
-
?
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophanyl-tRNATrp
-
-
-
-
?
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophanyl-tRNATrp
-
-
-
-
?
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophanyl-tRNATrp
the enzyme is essential for translation
-
-
?
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophanyl-tRNATrp
-
both TrpRS1 and TrpRS2 are essential for growth and required for cytosolic and mitochondrial tryptophanyl-tRNA formation, respectively, the edited anticodon and the mitochondria-specific thiolation of U33 in the imported tRNATrp act as antideterminants for the cytosolic TrpRS1, the mitochondrion of Trypanosoma brucei does not encode any tRNAs, this deficiency is compensated for by the import of a small fraction of nearly all of its cytosolic tRNAs from the host
-
-
?
ATP + L-tryptophan + tRNATrp

AMP + diphosphate + L-tryptophyl-tRNATrp
-
-
-
?
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophyl-tRNATrp
-
-
-
?
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophyl-tRNATrp
-
-
-
-
?
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophyl-tRNATrp
-
-
-
?
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophyl-tRNATrp
-
-
-
-
?
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophyl-tRNATrp
-
-
-
?
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophyl-tRNATrp
-
-
-
?
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophyl-tRNATrp
-
-
-
?
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophyl-tRNATrp
-
-
-
-
?
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophyl-tRNATrp
-
-
-
?
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophyl-tRNATrp
-
-
-
-
?
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophyl-tRNATrp
-
-
-
-
?
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophyl-tRNATrp
-
-
-
-
?
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophyl-tRNATrp
-
-
-
?
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophyl-tRNATrp
-
-
-
-
?
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophyl-tRNATrp
-
-
-
?
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophyl-tRNATrp
-
-
-
-
?
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophyl-tRNATrp
-
-
-
?
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophyl-tRNATrp
-
-
-
-
?
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophyl-tRNATrp
-
-
-
?
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophyl-tRNATrp
-
-
-
-
?
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophyl-tRNATrp
-
-
-
-
?
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophyl-tRNATrp
-
-
-
?
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophyl-tRNATrp
-
-
-
-
?
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophyl-tRNATrp
-
-
-
?
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophyl-tRNATrp
-
-
-
-
?
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophyl-tRNATrp
-
-
-
?
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophyl-tRNATrp
-
-
-
?
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophyl-tRNATrp
-
-
-
-
?
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophyl-tRNATrp
-
-
-
-
?
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophyl-tRNATrp
-
-
-
?
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophyl-tRNATrp
-
-
-
?
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophyl-tRNATrp
-
-
-
?
additional information

?
-
-
-
-
-
?
additional information
?
-
-
possibly involved in function other than tRNA aminoacylation
-
-
?
additional information
?
-
-
enzyme might by implicated in regulation of P1,P3-bis(5'-adenosyl)triphosphate/P1,P4-bis(5'-adenosyl)tetraphosphate ratio in the cell
-
-
?
additional information
?
-
-
tryptophanyl tRNA synthetase II interacts with nitric oxide synthetase and increases activity of nitric oxide synthetase
-
-
?
additional information
?
-
-
an ancestral tryptophanyl-tRNA synthetase precursor achieves high catalytic rate enhancement without ordered ground-state tertiary structures
-
-
?
additional information
?
-
-
mini isozyme specifically shows anti-proliferative and anti-angiogenic activity
-
?
additional information
?
-
the catalytic fragment exhibits potent angiostatic activity
-
?
additional information
?
-
-
the catalytic fragment exhibits potent angiostatic activity
-
?
additional information
?
-
-
the enzymes C-terminal domain, an EMAP II-like protein, inhibits angiogenesis signaling pathways and the development of blood vessels
-
?
additional information
?
-
-
interferon-gamma-inducible enzyme. Exposure to soluble cytotoxic T lymphocyte antigen-4 induces increased expression of tryptophanyl-tRNA synthetase in unseparated peripheral blood mononuclear cells, as well as in monocyte-derived mature dentritic cells. CD4+ cells and CD8+ cells isolated from peripheral blood mononuclear cells treated with soluble cytotoxic T lymphocyte antigen-4 show increased tryptophanyl-tRNA synthetase compared with untreated cells. Possibility that tryptophanyl-tRNA synthetase may be involved in an important mechanism regulating immune response
-
-
?
additional information
?
-
-
the vascular endothelial-cadherin-dependent pathway is proposed to link T2-TrpRS to inhibition of new blood vessel formation
-
-
?
additional information
?
-
-
tryptamine induces tryptophanyl-tRNA synthetase-mediated neurodegeneration with neurofibrillary tangles in human cell models, the dietary supplementation with tryptophan as a tryptamine competitor may not counteract the deleterious influence of tryptamine, overview
-
-
?
additional information
?
-
binding of vascular endothelial (VE)-cadherin, the NH2-terminal Trp2 and Trp4 residues of VE-cadherin are docked into the Trp- and adenosine-binding pockets of human TrpRS
-
-
?
additional information
?
-
-
binding of vascular endothelial (VE)-cadherin, the NH2-terminal Trp2 and Trp4 residues of VE-cadherin are docked into the Trp- and adenosine-binding pockets of human TrpRS
-
-
?
additional information
?
-
-
tryptamine induces tryptophanyl-tRNA synthetase-mediated neurodegeneration with neurofibrillary tangles in mouse models, the dietary supplementation with tryptophan as a tryptamine competitor may not counteract the deleterious influence of tryptamine, overview
-
-
?
additional information
?
-
-
tryptamine induces tryptophanyl-tRNA synthetase-mediated neurodegeneration with neurofibrillary tangles in mouse models, the dietary supplementation with tryptophan as a tryptamine competitor may not counteract the deleterious influence of tryptamine, overview
-
-
?
additional information
?
-
-
probably the enzyme fulfills some unknown function(s) important for digestion
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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Acidosis, Lactic
Expanding the Phenotype: Neurodevelopmental Disorder, Mitochondrial, With Abnormal Movements and Lactic Acidosis, With or Without Seizures (NEMMLAS) due to WARS2 Biallelic Variants, Encoding Mitochondrial Tryptophanyl-tRNA Synthase.
Acidosis, Lactic
Expanding the Phenotype: Neurodevelopmental Disorder, Mitochondrial, With Abnormal Movements and Lactic Acidosis, With or Without Seizures (NEMMLAS) Due to WARS2 Biallelic Variants, Encoding Mitochondrial Tryptophanyl-tRNA Synthase.
Alzheimer Disease
Mapping and molecular characterization of novel monoclonal antibodies to conformational epitopes on NH2 and COOH termini of mammalian tryptophanyl-tRNA synthetase reveal link of the epitopes to aggregation and Alzheimer's disease.
Alzheimer Disease
Synthetic Peptide Corresponding to The Amino-Terminal Region of the Human Tryptophanyl-Trna Synthetase, a Component Of Alzheimer'S Disease Special Congophlic Plaques Aggregates In Vitro to Form Amyloid-Like Fibrils.
Ataxia
Expanding the Phenotype: Neurodevelopmental Disorder, Mitochondrial, With Abnormal Movements and Lactic Acidosis, With or Without Seizures (NEMMLAS) due to WARS2 Biallelic Variants, Encoding Mitochondrial Tryptophanyl-tRNA Synthase.
Athetosis
Deficiency of WARS2, encoding mitochondrial tryptophanyl tRNA synthetase, causes severe infantile onset leukoencephalopathy.
Brain Diseases
Biallelic variants in WARS2 encoding mitochondrial tryptophanyl-tRNA synthase in six individuals with mitochondrial encephalopathy.
Breast Neoplasms
Concurrent Gene Signatures for Han Chinese Breast Cancers.
Carcinogenesis
Tryptamine-mediated stabilization of tryptophanyl-tRNA synthetase in human cervical carcinoma cell line.
Carcinoma
Tryptamine-mediated stabilization of tryptophanyl-tRNA synthetase in human cervical carcinoma cell line.
Colonic Neoplasms
The prognostic significance of tryptophanyl-tRNA synthetase in colorectal cancer.
Colorectal Neoplasms
Hypoxia signature of splice forms of tryptophanyl-tRNA synthetase marks pancreatic cancer cells with distinct metastatic abilities.
Colorectal Neoplasms
Identification of differential proteins in colorectal cancer cells treated with caffeic acid phenethyl ester.
Colorectal Neoplasms
The prognostic significance of tryptophanyl-tRNA synthetase in colorectal cancer.
Dyskinesias
Expanding the Phenotype: Neurodevelopmental Disorder, Mitochondrial, With Abnormal Movements and Lactic Acidosis, With or Without Seizures (NEMMLAS) due to WARS2 Biallelic Variants, Encoding Mitochondrial Tryptophanyl-tRNA Synthase.
Dyskinesias
Expanding the Phenotype: Neurodevelopmental Disorder, Mitochondrial, With Abnormal Movements and Lactic Acidosis, With or Without Seizures (NEMMLAS) Due to WARS2 Biallelic Variants, Encoding Mitochondrial Tryptophanyl-tRNA Synthase.
Epilepsy
Deficiency of WARS2, encoding mitochondrial tryptophanyl tRNA synthetase, causes severe infantile onset leukoencephalopathy.
Eye Diseases
A fragment of human TrpRS as a potent antagonist of ocular angiogenesis.
Gastrointestinal Stromal Tumors
Role of Immune Microenvironment in Gastrointestinal Stromal Tumors.
Hyperkinesis
Mutation of the WARS2 Gene as the Cause of a Severe Hyperkinetic Movement Disorder.
Infections
Corrigendum: Secreted tryptophanyl-tRNA synthetase as a primary defence system against infection.
Infections
Secreted tryptophanyl-tRNA synthetase as a primary defence system against infection.
Intellectual Disability
Biallelic mutations in mitochondrial tryptophanyl-tRNA synthetase cause Levodopa-responsive infantile-onset Parkinsonism.
Intellectual Disability
Deficiency of WARS2, encoding mitochondrial tryptophanyl tRNA synthetase, causes severe infantile onset leukoencephalopathy.
Intellectual Disability
Mutations of the aminoacyl-tRNA-synthetases SARS and WARS2 are implicated in the etiology of autosomal recessive intellectual disability.
Leukemia
Chaperon-like Activation of Serum-Inducible Tryptophanyl-tRNA Synthetase Phosphorylation through Refolding as a Tool for Analysis of Clinical Samples.
Leukemia, Myeloid
Interferons induce accumulation of diadenosine triphosphate (Ap3A) in human cultured cells.
Leukoencephalopathies
Biallelic mutations in mitochondrial tryptophanyl-tRNA synthetase cause Levodopa-responsive infantile-onset Parkinsonism.
Leukoencephalopathies
Deficiency of WARS2, encoding mitochondrial tryptophanyl tRNA synthetase, causes severe infantile onset leukoencephalopathy.
Leukoencephalopathies
Mutations in the mitochondrial tryptophanyl-tRNA synthetase cause growth retardation and progressive leukoencephalopathy.
Lymphoma
Design and synthesis of novel spirooxindole-indenoquinoxaline derivatives as novel tryptophanyl-tRNA synthetase inhibitors.
Lymphoma, B-Cell
Design and synthesis of novel spirooxindole-indenoquinoxaline derivatives as novel tryptophanyl-tRNA synthetase inhibitors.
Malaria
An appended domain results in an unusual architecture for malaria parasite tryptophanyl-tRNA synthetase.
Melanoma
Tryptophanyl-tRNA synthetase (WARS) expression in uveal melanoma - possible contributor during uveal melanoma progression.
Microcephaly
Deficiency of WARS2, encoding mitochondrial tryptophanyl tRNA synthetase, causes severe infantile onset leukoencephalopathy.
Mitochondrial Diseases
Biallelic variants in WARS2 encoding mitochondrial tryptophanyl-tRNA synthase in six individuals with mitochondrial encephalopathy.
Mitochondrial Diseases
Mutations in the mitochondrial tryptophanyl-tRNA synthetase cause growth retardation and progressive leukoencephalopathy.
Mouth Neoplasms
Overexpressed tryptophanyl-tRNA synthetase, an angiostatic protein, enhances oral cancer cell invasiveness.
Movement Disorders
Co-occurring WARS2 and CHRNA6 mutations in a child with a severe form of infantile parkinsonism.
Movement Disorders
Mutation of the WARS2 Gene as the Cause of a Severe Hyperkinetic Movement Disorder.
Myocardial Infarction
Different angiogenesis effect of mini-TyrRS/mini-TrpRS by systemic administration of modified siRNAs in rats with acute myocardial infarction.
Myocardial Infarction
Effect of mini-tyrosyl-tRNA synthetase/mini-tryptophanyl-tRNA synthetase on ischemic angiogenesis in rats: proliferation and migration of endothelial cells.
Myocardial Infarction
Tryptophanyl-tRNA synthetase gene polymorphisms and risk of incident myocardial infarction.
Neoplasm Metastasis
The prognostic significance of tryptophanyl-tRNA synthetase in colorectal cancer.
Neoplasms
Chaperon-like Activation of Serum-Inducible Tryptophanyl-tRNA Synthetase Phosphorylation through Refolding as a Tool for Analysis of Clinical Samples.
Neoplasms
Differential protein synthesis and expression levels in normal and neoplastic human prostate cells and their regulation by type I and II interferons.
Neoplasms
Evidence for the involvement of SDF-1 and CXCR4 in the disruption of endothelial cell-branching morphogenesis and angiogenesis by TNF-alpha and IFN-gamma.
Neoplasms
Hypoxia signature of splice forms of tryptophanyl-tRNA synthetase marks pancreatic cancer cells with distinct metastatic abilities.
Neoplasms
Overexpressed tryptophanyl-tRNA synthetase, an angiostatic protein, enhances oral cancer cell invasiveness.
Neoplasms
Prediction of Recurrence and Survival for Triple-Negative Breast Cancer (TNBC) by a Protein Signature in Tissue Samples.
Neoplasms
Role of Immune Microenvironment in Gastrointestinal Stromal Tumors.
Neoplasms
The prognostic significance of tryptophanyl-tRNA synthetase in colorectal cancer.
Neoplasms
The role of indoleamine 2,3-dioxygenase in the anti-tumour activity of human interferon-gamma in vivo.
Neuroblastoma
Mapping and molecular characterization of novel monoclonal antibodies to conformational epitopes on NH2 and COOH termini of mammalian tryptophanyl-tRNA synthetase reveal link of the epitopes to aggregation and Alzheimer's disease.
Neurodegenerative Diseases
Tryptamine Induces Tryptophanyl-tRNA Synthetase-Mediated Neurodegeneration With Neurofibrillary Tangles in Human Cell and Mouse Models.
Obesity, Abdominal
Mutant Wars2 gene in spontaneously hypertensive rats impairs brown adipose tissue function and predisposes to visceral obesity.
Ovarian Neoplasms
Chaperon-like Activation of Serum-Inducible Tryptophanyl-tRNA Synthetase Phosphorylation through Refolding as a Tool for Analysis of Clinical Samples.
Pancreatic Neoplasms
Hypoxia signature of splice forms of tryptophanyl-tRNA synthetase marks pancreatic cancer cells with distinct metastatic abilities.
Pancreatic Neoplasms
Mapping and molecular characterization of novel monoclonal antibodies to conformational epitopes on NH2 and COOH termini of mammalian tryptophanyl-tRNA synthetase reveal link of the epitopes to aggregation and Alzheimer's disease.
Parkinsonian Disorders
Biallelic mutations in mitochondrial tryptophanyl-tRNA synthetase cause Levodopa-responsive infantile-onset Parkinsonism.
Parkinsonian Disorders
Co-occurring WARS2 and CHRNA6 mutations in a child with a severe form of infantile parkinsonism.
Protein Deficiency
Diet-Related Metabolic Perturbations of Gut Microbial Shikimate Pathway-Tryptamine-tRNA Aminoacylation-Protein Synthesis in Human Health and Disease.
Quadriplegia
Deficiency of WARS2, encoding mitochondrial tryptophanyl tRNA synthetase, causes severe infantile onset leukoencephalopathy.
Renal Insufficiency, Chronic
Serum levels and activity of indoleamine2,3-dioxygenase and tryptophanyl-tRNA synthetase and their association with disease severity in patients with chronic kidney disease.
Sarcoma, Avian
Chaperon-like Activation of Serum-Inducible Tryptophanyl-tRNA Synthetase Phosphorylation through Refolding as a Tool for Analysis of Clinical Samples.
Seizures
Expanding the Phenotype: Neurodevelopmental Disorder, Mitochondrial, With Abnormal Movements and Lactic Acidosis, With or Without Seizures (NEMMLAS) due to WARS2 Biallelic Variants, Encoding Mitochondrial Tryptophanyl-tRNA Synthase.
Seizures
Expanding the Phenotype: Neurodevelopmental Disorder, Mitochondrial, With Abnormal Movements and Lactic Acidosis, With or Without Seizures (NEMMLAS) Due to WARS2 Biallelic Variants, Encoding Mitochondrial Tryptophanyl-tRNA Synthase.
Sepsis
Clinical value of full-length tryptophanyl-tRNA synthetase for sepsis detection in critically ill patients - A retrospective clinical assessment.
Stomach Neoplasms
Expression of Indoleamine 2, 3-dioxygenase 1 (IDO1) and Tryptophanyl-tRNA Synthetase (WARS) in Gastric Cancer Molecular Subtypes.
tryptophan-trna ligase deficiency
Biallelic mutations in mitochondrial tryptophanyl-tRNA synthetase cause Levodopa-responsive infantile-onset Parkinsonism.
tryptophan-trna ligase deficiency
Severe hepatopathy and neurological deterioration after start of valproate treatment in a 6-year-old child with mitochondrial tryptophanyl-tRNA synthetase deficiency.
Virus Diseases
Released Tryptophanyl-tRNA Synthetase Stimulates Innate Immune Responses against Viral Infection.
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0.00006
Archeoglobus fulgidus tRNATrp(A73, wild-type)
pH 7.0, 65°C
-
0.00005
Archeoglobus fulgidus tRNATrp(A73C)
pH 7.0, 65°C
-
0.00006
Archeoglobus fulgidus tRNATrp(A73G)
pH 7.0, 65°C
-
0.00005
Archeoglobus fulgidus tRNATrp(A73U)
pH 7.0, 65°C
-
0.00009
Bacillus subtilis tRNATrp(A73, wild-type)
pH 7.0, 65°C
-
0.00012
Bacillus subtilis tRNATrp(A73C)
pH 7.0, 65°C
-
0.0001
Bacillus subtilis tRNATrp(A73G)
pH 7.0, 65°C
-
0.00012
Bacillus subtilis tRNATrp(A73U)
pH 7.0, 65°C
-
0.00018
bovine tRNATrp(G73, wild-type)
pH 7.0, 65°C
-
0.00021
bovine tRNATrp(G73A)
pH 7.0, 65°C
-
0.00022
bovine tRNATrp(G73C)
pH 7.0, 65°C
-
0.00017
bovine tRNATrp(G73U)
pH 7.0, 65°C
-
0.00073 - 0.027
L-tryptophan
1
P1,P3-bis(5'-adenosyl)triphosphate
0.0021
tRNAArg
-
pH 7.5, 60°C
0.0059
tRNATrp(A36C)
-
substrate mutant, pH 7.5, 60°C
-
0.0053
tRNATrp(A36G)
-
substrate mutant, pH 7.5, 60°C
-
0.0058
tRNATrp(A36U)
-
substrate mutant, pH 7.5, 60°C
-
0.0098
tRNATrp(A36U, A73G)
-
substrate mutant, pH 7.5, 60°C
-
0.0017
tRNATrp(A73C)
-
substrate mutant, pH 7.5, 60°C
-
0.0058
tRNATrp(A73G)
-
substrate mutant, pH 7.5, 60°C
-
0.0051
tRNATrp(A73U)
-
substrate mutant, pH 7.5, 60°C
-
0.06
tRNATrp(C34A)
-
substrate mutant, pH 7.5, 60°C
-
0.038
tRNATrp(C34G)
-
substrate mutant, pH 7.5, 60°C
-
0.048
tRNATrp(C34U)
-
substrate mutant, pH 7.5, 60°C
-
0.014
tRNATrp(C35A)
-
substrate mutant, pH 7.5, 60°C
-
0.038
tRNATrp(C35G)
-
substrate mutant, pH 7.5, 60°C
-
0.021
tRNATrp(C35U)
-
substrate mutant, pH 7.5, 60°C
-
0.025
tRNATrp(G1A-C72U)
-
substrate mutant, pH 7.5, 60°C
-
0.0055
tRNATrp(G1C-G72G)
-
substrate mutant, pH 7.5, 60°C
-
0.021
tRNATrp(G1U-C72A)
-
substrate mutant, pH 7.5, 60°C
-
0.015
tRNATrp(G2A-C71U)
-
substrate mutant, pH 7.5, 60°C
-
0.0019
tRNATrp(G2C-G71G)
-
substrate mutant, pH 7.5, 60°C
-
0.0058
tRNATrp(G2U-C71A)
-
substrate mutant, pH 7.5, 60°C
-
0.006
tRNATrp(HOG1)
-
substrate mutant, pH 7.5, 60°C
-
0.012
tRNATrp(pppG1)
-
substrate mutant, pH 7.5, 60°C
-
additional information
additional information
-
0.03
ATP

-
-
0.041
ATP
-
25°C, pH 9.0, mutant enzyme K149G, activation of Trp
0.046
ATP
-
25°C, pH 9.0, mutant enzyme K149E, activation of Trp
0.048
ATP
-
25°C, pH 9.0, mutant enzyme E153D, activation of Trp
0.065
ATP
-
25°C, pH 9.0, wild-type enzyme, activation of Trp
0.088
ATP
-
pH 7.5, 30°C, recombinant enzyme
0.121
ATP
-
25°C, pH 9.0, mutant enzyme K149R, activation of Trp
0.129
ATP
-
recombinant wild-type
0.15
ATP
-
enzyme form TRS108, tRNA esterification
0.22
ATP
-
aminoacylation
0.252
ATP
-
recombinant truncated mutant
0.278
ATP
-
25°C, pH 9.0, mutant enzyme K149D/E153R, activation of Trp
0.4
ATP
pH 9.0, 22°C, recombinant enzyme, exchange assay
0.5
ATP
-
enzyme form TRS82, tRNA esterification
0.5
ATP
-
diphosphate, tryptophan-dependent ATP-diphosphate exchange
1.552
ATP
-
25°C, pH 9.0, mutant enzyme E153K, activation of Trp
2
ATP
-
enzyme form TRS108 and TRS92
2
ATP
-
tryptophan-dependent ATP-diphosphate exchange
0.00073
L-tryptophan

-
pH 7.5, 22°C, wild-type enzyme
0.000943
L-tryptophan
wild type enzyme, in 0.1 M Tris-HCl (pH 7.5), 0.01 M potassium fluoride, 5 mM MgCl2, at 37°C
0.0015
L-tryptophan
-
recombinant wild-type
0.0019
L-tryptophan
-
recombinant truncated mutant
0.0021
L-tryptophan
-
pH 7.5, 22°C, deletion 108-122 mutant
0.0023
L-tryptophan
-
pH 7.5, 22°C, deletion 234-238 mutant
0.00527
L-tryptophan
wild type enzyme, in 0.1 M Tris-HCl (pH 7.5), 0.01 M potassium fluoride, 5 mM MnCl2, at 37°C
0.0074
L-tryptophan
-
pH 7.5, 30°C, recombinant enzyme
0.017
L-tryptophan
-
recombinant enyzme
0.027
L-tryptophan
pH 9.0, 22°C, recombinant enzyme, exchange assay
1
P1,P3-bis(5'-adenosyl)triphosphate

-
tryptophanamide formation
1
P1,P3-bis(5'-adenosyl)triphosphate
-
aminoacylation, ammonia
0.00012
tRNATrp

-
aminoacylation
0.00018
tRNATrp
-
pH 7.5, 22°C, wild-type enzyme
0.00022
tRNATrp
-
pH 7.5, 22°C, deletion 108-122 mutant
0.00029
tRNATrp
pH 7.5, 30°C, mutant V85K
0.00031
tRNATrp
-
recombinant wild-type
0.00038
tRNATrp
-
enzyme form TRS108, tRNA esterification
0.0005
tRNATrp
-
22°C, pH 7.5, tRNATrp from Bacillus subtilis, mutant enzyme K149R, aminoacylation
0.00052
tRNATrp
-
pH 7.5, 22°C, deletion 234-238 mutant
0.00061
tRNATrp
-
22°C, pH 7.5, tRNATrp from Bacillus subtilis, wild-type enzyme, aminoacylation
0.00062
tRNATrp
-
recombinant mutant
0.0008
tRNATrp
-
enzyme form TRS82, tRNA esterification
0.00087
tRNATrp
-
22°C, pH 7.5, tRNATrp from Bacillus subtilis, mutant enzyme K149E, aminoacylation
0.00088
tRNATrp
-
22°C, pH 7.5, tRNATrp from Bacillus subtilis, mutant enzyme E153D, aminoacylation
0.0011
tRNATrp
-
pH 7.5, 30°C, recombinant enzyme
0.00113
tRNATrp
-
22°C, pH 7.5, tRNATrp from Bacillus subtilis, mutant enzyme E153K, aminoacylation
0.00121
tRNATrp
pH 7.5, 30°C, recombinant wild-type enzyme
0.00121
tRNATrp
-
22°C, pH 7.5, tRNATrp from Bacillus subtilis, mutant enzyme K149G, aminoacylation
0.00123
tRNATrp
-
22°C, pH 7.5, tRNATrp from Bacillus subtilis, mutant enzyme E153G, aminoacylation
0.00126
tRNATrp
-
22°C, pH 7.5, tRNATrp from Bacillus subtilis, mutant enzyme K149D/E153R, aminoacylation
0.0013
tRNATrp
pH 7.5, 30°C, wild-type enzyme
0.00141
tRNATrp
pH 7.5, 30°C, mutant V85A
0.00184
tRNATrp
pH 7.5, 30°C, mutant V90A
0.002
tRNATrp
-
recombinant truncated mutant
0.00214
tRNATrp
pH 7.5, 30°C, mutant V85S
0.00223
tRNATrp
pH 7.5, 30°C, mutant V85A/V90A
0.0052
tRNATrp
pH 7.5, 30°C, mutant V90S
0.0085
tRNATrp
pH 7.5, 30°C, mutant V85E
0.0248
tRNATrp
pH 7.5, 30°C, mutant V85L
0.00045
Trp

-
enzyme form TRS82, tryptophan-dependent ATP-diphosphate exchange
0.0005
Trp
-
enzyme form TRS108, tryptophan-dependent ATP-diphosphate exchange
0.0025
Trp
-
enzyme form TRS108, tRNA esterification
0.0033
Trp
-
25°C, pH 9.0, mutant enzyme E153D, activation of Trp
0.0037
Trp
-
25°C, pH 9.0, mutant enzyme K149E, activation of Trp
0.0038
Trp
-
25°C, pH 9.0, mutant enzyme K149G, activation of Trp
0.0046
Trp
-
25°C, pH 9.0, wild-type enzyme, activation of Trp
0.005
Trp
-
enzyme form TRS82, tRNA esterification
0.0099
Trp
-
25°C, pH 9.0, mutant enzyme K149R, activation of Trp
0.06
Trp
-
25°C, pH 9.0, mutant enzyme K149D/E153R, activation of Trp
0.128
Trp
-
25°C, pH 9.0, mutant enzyme E153K, activation of Trp
additional information
additional information

-
kinetic behavior in adenylation
-
additional information
additional information
-
kinetic parameters of tryptophan-dependent ATP-diphosphate exchange reaction
-
additional information
additional information
diphosphate exchange kinetics show non-reciprocal cooperativity between ATP and Trp
-
additional information
additional information
-
kinetic investigation of enzyme activity with diverse tRNATrp mutants
-
additional information
additional information
kinetics of diverse recombinant mutant enzymes, overview
-
additional information
additional information
-
kinetics of diverse recombinant mutant enzymes, overview
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.53
Archeoglobus fulgidus tRNATrp(A73, wild-type)
pH 7.0, 65°C
-
0.11
Archeoglobus fulgidus tRNATrp(A73C)
pH 7.0, 65°C
-
0.07
Archeoglobus fulgidus tRNATrp(A73G)
pH 7.0, 65°C
-
0.09
Archeoglobus fulgidus tRNATrp(A73U)
pH 7.0, 65°C
-
0.14
Bacillus subtilis tRNATrp(A73, wild-type)
pH 7.0, 65°C
-
0.06
Bacillus subtilis tRNATrp(A73C)
pH 7.0, 65°C
-
0.04
Bacillus subtilis tRNATrp(A73G)
pH 7.0, 65°C
-
0.05
Bacillus subtilis tRNATrp(A73U)
pH 7.0, 65°C
-
0.03
bovine tRNATrp(G73, wild-type)
pH 7.0, 65°C
-
0.08
bovine tRNATrp(G73A)
pH 7.0, 65°C
-
0.06
bovine tRNATrp(G73C)
pH 7.0, 65°C
-
0.04
bovine tRNATrp(G73U)
pH 7.0, 65°C
-
0.16
tRNAArg
-
pH 7.5, 60°C
11
tRNATrp(A36C)
-
substrate mutant, pH 7.5, 60°C
-
4.4
tRNATrp(A36G)
-
substrate mutant, pH 7.5, 60°C
-
21
tRNATrp(A36U)
-
substrate mutant, pH 7.5, 60°C
-
0.27
tRNATrp(A36U, A73G)
-
substrate mutant, pH 7.5, 60°C
-
5.5
tRNATrp(A73C)
-
substrate mutant, pH 7.5, 60°C
-
0.62
tRNATrp(A73G)
-
substrate mutant, pH 7.5, 60°C
-
6.1
tRNATrp(A73U)
-
substrate mutant, pH 7.5, 60°C
-
0.17
tRNATrp(C34A)
-
substrate mutant, pH 7.5, 60°C
-
0.13
tRNATrp(C34G)
-
substrate mutant, pH 7.5, 60°C
-
0.11
tRNATrp(C34U)
-
substrate mutant, pH 7.5, 60°C
-
0.15
tRNATrp(C35A)
-
substrate mutant, pH 7.5, 60°C
-
0.079
tRNATrp(C35G)
-
substrate mutant, pH 7.5, 60°C
-
0.47
tRNATrp(C35U)
-
substrate mutant, pH 7.5, 60°C
-
2.3
tRNATrp(G1A-C72U)
-
substrate mutant, pH 7.5, 60°C
-
0.34
tRNATrp(G1C-G72G)
-
substrate mutant, pH 7.5, 60°C
-
0.46
tRNATrp(G1U-C72A)
-
substrate mutant, pH 7.5, 60°C
-
19
tRNATrp(G2A-C71U)
-
substrate mutant, pH 7.5, 60°C
-
1.7
tRNATrp(G2C-G71G)
-
substrate mutant, pH 7.5, 60°C
-
7.2
tRNATrp(G2U-C71A)
-
substrate mutant, pH 7.5, 60°C
-
3.2
tRNATrp(HOG1)
-
substrate mutant, pH 7.5, 60°C
-
4.5
tRNATrp(pppG1)
-
substrate mutant, pH 7.5, 60°C
-
1.1
ATP

-
pH 7.5, 30°C, recombinant enzyme
1.4
ATP
pH 9.0, 22°C, recombinant enzyme, exchange assay
15
ATP
-
25°C, pH 9.0, mutant enzyme K149G, activation of Trp
16
ATP
-
25°C, pH 9.0, mutant enzyme K149E, activation of Trp
17
ATP
-
25°C, pH 9.0, mutant enzyme E153D, activation of Trp
22
ATP
-
25°C, pH 9.0, wild-type enzyme, activation of Trp
27
ATP
-
25°C, pH 9.0, mutant enzyme K149D/E153R, activation of Trp
46
ATP
-
25°C, pH 9.0, mutant enzyme K149R, activation of Trp
419
ATP
-
25°C, pH 9.0, mutant enzyme E153K, activation of Trp
0.59
L-tryptophan

-
pH 7.5, 22°C, deletion 234-238 mutant
0.61
L-tryptophan
-
pH 7.5, 22°C, deletion 108-122 mutant
0.9
L-tryptophan
-
pH 7.5, 22°C, wild-type enzyme
1.1
L-tryptophan
-
pH 7.5, 30°C, recombinant enzyme
1.2
L-tryptophan
pH 9.0, 22°C, recombinant enzyme, exchange assay
4.88
L-tryptophan
wild type enzyme, in 0.1 M Tris-HCl (pH 7.5), 0.01 M potassium fluoride, 5 mM MnCl2, at 37°C
5.45
L-tryptophan
wild type enzyme, in 0.1 M Tris-HCl (pH 7.5), 0.01 M potassium fluoride, 5 mM MgCl2, at 37°C
6.08
L-tryptophan
-
pH 7.5, 22°C, deletion 108-122 mutant
6.08
L-tryptophan
-
pH 7.5, 22°C, deletion 234-238 mutant
13.6
L-tryptophan
-
recombinant truncated mutant
24.5
L-tryptophan
-
recombinant wild-type
0.0009
tRNATrp

pH 7.5, 30°C, mutant V85K
0.016
tRNATrp
-
22°C, pH 7.5, tRNATrp from Bacillus subtilis, mutant enzyme K149D/E153R, aminoacylation
0.02
tRNATrp
-
22°C, pH 7.5, tRNATrp from Bacillus subtilis, mutant enzyme E153K, aminoacylation
0.02
tRNATrp
pH 7.5, 30°C, mutant V85E
0.028
tRNATrp
pH 7.5, 30°C, mutant V85S
0.03
tRNATrp
-
22°C, pH 7.5, tRNATrp from Bacillus subtilis, mutant enzyme E153D, aminoacylation
0.047
tRNATrp
pH 7.5, 30°C, mutant V85A/V90A
0.063
tRNATrp
pH 7.5, 30°C, mutant V90S
0.32
tRNATrp
-
22°C, pH 7.5, tRNATrp from Bacillus subtilis, mutant enzyme K149R, 0.32 aminoacylation
0.32
tRNATrp
-
22°C, pH 7.5, tRNATrp from Bacillus subtilis, wild-type enzyme, aminoacylation
0.48
tRNATrp
pH 7.5, 30°C, mutant V85A
0.59
tRNATrp
-
pH 7.5, 22°C, deletion 234-238 mutant
0.61
tRNATrp
-
pH 7.5, 22°C, deletion 108-122 mutant
0.67
tRNATrp
-
22°C, pH 7.5, tRNATrp from Bacillus subtilis, mutant enzyme K149E, aminoacylation
0.78
tRNATrp
-
22°C, pH 7.5, tRNATrp from Bacillus subtilis, mutant enzyme K149G, aminoacylation
0.9
tRNATrp
-
pH 7.5, 22°C, wild-type enzyme
1
tRNATrp
-
pH 7.5, 30°C, recombinant enzyme
1.33
tRNATrp
pH 7.5, 30°C, recombinant wild-type enzyme
1.37
tRNATrp
pH 7.5, 30°C, wild-type enzyme
1.39
tRNATrp
pH 7.5, 30°C, mutant V90A
2.22
tRNATrp
-
recombinant truncated mutant
2.94
tRNATrp
-
recombinant truncated mutant
3 - 6
tRNATrp
-
recombinant wild-type
3.17
tRNATrp
-
recombinant wild-type
3.3
tRNATrp
pH 7.5, 30°C, mutant V85L
5.11
tRNATrp
pH 7.5, 30°C, mutant V85L
6.08
tRNATrp
-
pH 7.5, 22°C, deletion 108-122 mutant
6.08
tRNATrp
-
pH 7.5, 22°C, deletion 234-238 mutant
13.9
tRNATrp
-
recombinant mutant
16
tRNATrp
-
pH 7.5, 60°C
2 - 8
Trp

-
25°C, pH 9.0, mutant enzyme K149D/E153R, activation of Trp
15
Trp
-
25°C, pH 9.0, mutant enzyme K149G, activation of Trp
16
Trp
-
25°C, pH 9.0, mutant enzyme K149E, activation of Trp
18
Trp
-
25°C, pH 9.0, mutant enzyme E153D, activation of Trp
22
Trp
-
25°C, pH 9.0, wild-type enzyme, activation of Trp
46
Trp
-
25°C, pH 9.0, mutant enzyme K149R, activation of Trp
419
Trp
-
25°C, pH 9.0, mutant enzyme E153K, activation of Trp
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