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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 3 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
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-
?
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
-
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?
P1,P3-bis(5'-adenosyl)triphosphate + L-tryptophan + tRNATrp
?
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-
-
-
?
P1,P3-bis(5'-adenosyl)triphosphate + L-tryptophan + tRNATrp
?
-
-
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?
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
-
-
?
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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.
Breast Neoplasms
Tryptophanyl-tRNA Synthetase Sensitizes Hormone Receptor-Positive Breast Cancer to Docetaxel-Based Chemotherapy.
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.
Lymphatic Metastasis
The prognostic significance of tryptophanyl-tRNA synthetase in colorectal cancer.
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.
Lymphoma, Large B-Cell, Diffuse
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.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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 enzyme
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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evolution
-
the activation reaction mechanism of TrpRS from the basal eukaryote Gardia lamblia differs from that of higher eukaryotes, overview. The N-terminus of the class I aminoacyl-tRNA synthetase from Gardia lamblia forms a 16-residue alpha-helix. This helix replaces a beta-hairpin that is required by human TrpRS for normal activity and infers to play a similar role in all eukaryotic TrpRS
evolution
the Trypanosoma brucei genome contains separate cytosolic and mitochondrial isoforms of TrpRS that are both required and have diverged in their respective tRNA recognition domains
evolution
-
an ancestral tryptophanyl-tRNA synthetase precursor achieves high catalytic rate enhancement without ordered ground-state tertiary structures. The TrpRS Urzyme catalytic activity arises neither from tiny amounts of wild-type enzyme, nor from a separate population of folded and highly active Urzyme molecules not in equilibrium with the general population. AaRS Urzymes lack much of the mass of modern aaRS, retaining only a small portion of the hydrophobic cores of the full-length enzymes. AaRS Urzymes contain 120-130 amino acids, and consist of little more than is required to form intact active sites. They retain over 60% of the transition-state stabilization free energy for amino acid activation and the ability to aminoacylate tRNA. Further, they preserve about 20% of the Gibbs energies necessary to discriminate between competing amino acid substrates and preferentially activate amino acids from within, rather than outside, their own class. A major fraction of TrpRS Urzyme molecules contribute to the rate acceleration by transiently forming tight transition-state complexes
malfunction
a human mini K153Q TrpRS mutant cannot inhibit VEGF-stimulated HUVEC migration and cannot bind to the extracellular domain of VE-cadherin
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
malfunction
the full-length-WRS-induced TNF-alpha and MIP-1alpha production is significantly inhibited when TLR4, MD2, and TLR2 (to lesser degree) are suppressed, full-length-WRS-induced neutrophil infiltration is almost ablated in the TLR4-/- and MD2-/- mice, and partially reduced in TLR2-/- mice. Although truncated WRS mutant lacking N47 can bring the two TLR4-MD2 complexes into proximity through homodimerization of the WRS catalytic domain, it may not be able to induce the functional dimerization of TLR4-MD2 to activate downstream signalling
malfunction
the full-length-WRS-induced TNF-alpha and MIP-1alpha production is significantly inhibited when TLR4, MD2, and TLR2 (to lesser degree) are suppressed, human full-length-WRS-induced neutrophil infiltration is almost ablated in the TLR4-/- and MD2-/- mice, and partially reduced in TLR2-/- mice. Although truncated WRS mutant lacking N47 can bring the two TLR4-MD2 complexes into proximity through homodimerization of the WRS catalytic domain, it may not be able to induce the functional dimerization of TLR4-MD2 to activate downstream signalling
malfunction
-
the full-length-WRS-induced TNF-alpha and MIP-1alpha production is significantly inhibited when TLR4, MD2, and TLR2 (to lesser degree) are suppressed, full-length-WRS-induced neutrophil infiltration is almost ablated in the TLR4-/- and MD2-/- mice, and partially reduced in TLR2-/- mice. Although truncated WRS mutant lacking N47 can bring the two TLR4-MD2 complexes into proximity through homodimerization of the WRS catalytic domain, it may not be able to induce the functional dimerization of TLR4-MD2 to activate downstream signalling
-
physiological function
-
TrpRS is an aminoacyl-tRNA synthetase involved in protein synthesis and regulation of RNA transcription and translation and is an inhibitor of angiogenesis
physiological function
-
specific activation of amino acids by aminoacyl-tRNA synthetases is essential for maintaining translational fidelity
physiological function
-
the auxiliary, antibiotic-resistant tryptophanyl-tRNA synthetase gene trpRS1 in Streptomyces coelicolor is regulated by a ribosome-mediated attenuator in the 5' leader of its mRNA region, overview. This regulatory element controls gene transcription in response to the physiological effects of indolmycin and chuangxinmycin, two antibiotic enzyme inhibitors. Tryptophanyl-tRNA synthetase activity is inversely correlated with antitermination of trpRS1 transcription
physiological function
-
the Escherichia coli lysyl tRNA synthetase is responsible for misacylating the initial amber suppressor version of Saccharomyces cerevisiae tryptophanyl tRNA. Role of tRNA flexibility in molecular recognition and the engineering and evolution of tRNA specificity
physiological function
the organism requires a separate mitochondrial TrpRS isoform because the majority of tRNATrp in the trypanosomatid mitochondrion is posttranscriptionally modified by thiolation of U33 and by RNA-editing of the anticodon, residues 34-36, from CCA to UCA
physiological function
aminoacyl-tRNA synthetases catalyze the first step of protein synthesis, which comprises the aminoacylation of their cognate tRNAs. Noncanonical functions distinct from aminoacylation are reported
physiological function
aminoacyl-tRNA synthetases catalyze the first step of protein synthesis, which comprises the aminoacylation of their cognate tRNAs. Noncanonical functions distinct from aminoacylation are reported
physiological function
aminoacyl-tRNA synthetases catalyze the first step of protein synthesis, which comprises the aminoacylation of their cognate tRNAs. Noncanonical functions distinct from aminoacylation are reported, such as the cell-signaling functions of human tryptophanyl-tRNA synthetase (TrpRS) and tyrosyl-tRNA synthetase (TyrRS) in pathways connected to the immune system or angiogenesis. Human mini, but not full-length, TrpRS is an angiostatic factor. The interaction between mini TrpRS and the extracellular domain of vascular endothelial (VE) cadherin is crucial for its angiostatic activity. The Lys153 residue of human mini TrpRS is a VE-cadherin binding site and is therefore crucial for its angiostatic activity, molecular mechanism of the angiostatic activity of human mini TrpRS, overview. VE-cadherin belongs to the cadherin superfamily of cell-cell adhesion molecules and plays a key role in vascular endothelial growth factor (VEGF)-mediated endothelial survival, endothelial barrier function, and angiogenesis
physiological function
aminoacyl-tRNA synthetases catalyze the first step of protein synthesis, which comprises the aminoacylation of their cognate tRNAs. Noncanonical functions distinct from aminoacylation are reported. Arabidopsis thaliana TrpRS does inhibit VEGF-induced endothelial migration
physiological function
aminoacyl-tRNA synthetases maintain the fidelity of the genetic code by ensuring the charging of tRNA with its cognate amino acid
physiological function
regulation of endometrial tryptophanyl tRNA synthetase protein expression by the implanting and post-implanting conceptus,t the conceptus-derived signals favourably influences uterine environment for implantation through regulation of WARS expression in ovine caruncular endometrium
physiological function
-
secreted TrpRS promotes OSCC progression via an extrinsic pathway
physiological function
the secreted tryptophanyl-tRNA synthetase is a primary defence system against infection, it functions as an intrinsic defensive factor against infection. Administration of full-length murine WRS into Salmonella typhimurium-infected mice reduces the levels of bacteria and improves mouse survival, whereas its titration with the specific antibody aggravates the infection. Full-length WRS protects mice from typhimurium infection-induced lethality. The enzyme is secreted in N-terminal truncated form or in full-length form, the full-length wild-type enzyme, but not the short form, is rapidly secreted upon pathogen infection to prime innate immunity. Proposed working mechanism of full-length-WRS for TLR4-MD2 activation, overview
physiological function
the secreted tryptophanyl-tRNA synthetase is a primary defence system against infection, it functions as an intrinsic defensive factor against infection. Full-length WRS responds promptly to pathogens before the onset of innate immune responses. Prompt secretion of enzyme WRS from cultured human peripheral blood mononuclear cells (PBMCs) following infection with Salmonella typhimurium, Escherichia coli, Listeria monocytogenes, Staphylococcus aureus, and Candida albicans. Human full-length-WRS as an endogenous ligand of TLR4, which promptly triggers innate immunity against infection. Proposed working mechanism of full-length-WRS for TLR4-MD2 activation, overview
physiological function
-
the secreted tryptophanyl-tRNA synthetase is a primary defence system against infection, it functions as an intrinsic defensive factor against infection. Administration of full-length murine WRS into Salmonella typhimurium-infected mice reduces the levels of bacteria and improves mouse survival, whereas its titration with the specific antibody aggravates the infection. Full-length WRS protects mice from typhimurium infection-induced lethality. The enzyme is secreted in N-terminal truncated form or in full-length form, the full-length wild-type enzyme, but not the short form, is rapidly secreted upon pathogen infection to prime innate immunity. Proposed working mechanism of full-length-WRS for TLR4-MD2 activation, overview
-
physiological function
-
the Escherichia coli lysyl tRNA synthetase is responsible for misacylating the initial amber suppressor version of Saccharomyces cerevisiae tryptophanyl tRNA. Role of tRNA flexibility in molecular recognition and the engineering and evolution of tRNA specificity
-
additional information
one of the TrpRS gene homologues has lost the active site motifs characteristic of the class I aminoacyl-tRNA synthetase catalytic domain while retaining the conserved features of a fully formed tRNATrp recognition domain
additional information
one of the TrpRS gene homologues has lost the active site motifs characteristic of the class I aminoacyl-tRNA synthetase catalytic domain while retaining the conserved features of a fully formed tRNATrp recognition domain
additional information
one of the TrpRS gene homologues has lost the active site motifs characteristic of the class I aminoacyl-tRNA synthetase catalytic domain while retaining the conserved features of a fully formed tRNATrp recognition domain
additional information
-
one of the TrpRS gene homologues has lost the active site motifs characteristic of the class I aminoacyl-tRNA synthetase catalytic domain while retaining the conserved features of a fully formed tRNATrp recognition domain
additional information
-
15N tryptophanyl-tRNA synthetase Urzyme structure analysis by heteronuclear single quantum coherence (HSQC) NMR spectroscopy supplemented by circular dichroism, thermal melting, and induced fluorescence of bound dye. TrpRS Urzyme is not a typical protein domain. Transition state stabilization and catalytic activity from molten globules, overview
additional information
-
both full-length TrpRS and mini-TrpRS splicing variants 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). Extracellular treatment of TrpRS promotes cell invasion in oral cancer cells
additional information
both the ATP configuration and Mg2+ coordination in the human cytosolic (Hc)TrpRS preTS structure differ greatly from the BsTrpRS preTS structure. The effect of these differences is that catalysis occurs via a different transition state stabilization mechanism in HcTrpRS with a yet-to-be determined role for Mg2+
additional information
-
both the ATP configuration and Mg2+ coordination in the human cytosolic (Hc)TrpRS preTS structure differ greatly from the BsTrpRS preTS structure. The effect of these differences is that catalysis occurs via a different transition state stabilization mechanism in HcTrpRS with a yet-to-be determined role for Mg2+
additional information
tryptophanyl-tRNA synthetase (TrpRS) exists in two forms: a full-length TrpRS and a mini TrpRS. Both human and bovine mini TrpRSs inhibit VEGF-induced endothelial migration, whereas zebrafish mini TrpRS and Arabidopsis thaliana wild-type TrpRS do not. The bovine full-length TrpRS and zebrafish full-length TrpRS have no effect on VEGF-stimulated HUVEC chemotaxis
additional information
-
tryptophanyl-tRNA synthetase (TrpRS) exists in two forms: a full-length TrpRS and a mini TrpRS. Both human and bovine mini TrpRSs inhibit VEGF-induced endothelial migration, whereas zebrafish mini TrpRS and Arabidopsis thaliana wild-type TrpRS do not. The bovine full-length TrpRS and zebrafish full-length TrpRS have no effect on VEGF-stimulated HUVEC chemotaxis
additional information
tryptophanyl-tRNA synthetase (TrpRS) exists in two forms: a full-length TrpRS and a mini TrpRS. Both human and bovine mini TrpRSs inhibit VEGF-induced endothelial migration, whereas zebrafish mini TrpRS and Arabidopsis thaliana wild-type TrpRS do not. The bovine full-length TrpRS has no effect on VEGF-stimulated HUVEC chemotaxis
additional information
-
tryptophanyl-tRNA synthetase (TrpRS) exists in two forms: a full-length TrpRS and a mini TrpRS. Both human and bovine mini TrpRSs inhibit VEGF-induced endothelial migration, whereas zebrafish mini TrpRS and Arabidopsis thaliana wild-type TrpRS do not. The bovine full-length TrpRS has no effect on VEGF-stimulated HUVEC chemotaxis
additional information
tryptophanyl-tRNA synthetase (TrpRS) exists in two forms: a full-length TrpRS and a mini TrpRS. Both human and bovine mini TrpRSs inhibit VEGF-induced endothelial migration, whereas zebrafish mini TrpRS and Arabidopsis thaliana wild-type TrpRS do not. The zebrafish full-length TrpRS has no effect on VEGF-stimulated HUVEC chemotaxis
additional information
-
tryptophanyl-tRNA synthetase (TrpRS) exists in two forms: a full-length TrpRS and a mini TrpRS. Both human and bovine mini TrpRSs inhibit VEGF-induced endothelial migration, whereas zebrafish mini TrpRS and Arabidopsis thaliana wild-type TrpRS do not. The zebrafish full-length TrpRS has no effect on VEGF-stimulated HUVEC chemotaxis
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E153D
-
ratio of turnover number to Km-value for ATP is 109% of wild-type value, ratio of turnover number to Km-value for Trp is 114% of wild-type value, ratio of turnover number to Km-value for Bacillus subtilis tRNATrp is 89% of wild-type value
E153G
-
no detectable activity in activation of Trp unless tRNATRp is added to the reaction
E153K
-
ratio of turnover number to Km-value for ATP is 79% of wild-type value, ratio of turnover number to Km-value for Trp is 68% of wild-type value, ratio of turnover number to Km-value for Bacillus subtilis tRNATrp is 3% of wild-type value
K149D/E153R
-
ratio of turnover number to Km-value for ATP is 30% of wild-type value, ratio of turnover number to Km-value for Trp is 10% of wild-type value, ratio of turnover number to Km-value for Bacillus subtilis tRNATrp is 1% of wild-type value
K149E
-
ratio of turnover number to Km-value for ATP is 99.7% of wild-type value, ratio of turnover number to Km-value for Trp is 89% of wild-type value, ratio of turnover number to Km-value for Bacillus subtilis tRNATrp is 37% of wild-type value
K149G
-
ratio of turnover number to Km-value for ATP is 111% of wild-type value, ratio of turnover number to Km-value for Trp is 88% of wild-type value, ratio of turnover number to Km-value for Bacillus subtilis tRNATrp is 55% of wild-type value
K149R
-
ratio of turnover number to Km-value for ATP is 112% of wild-type value, ratio of turnover number to Km-value for Trp is 98% of wild-type value, ratio of turnover number to Km-value for Bacillus subtilis tRNATrp is 64% of wild-type value
V144P
-
mutant selectively aminoacylates the cognate mutant opal suppressor tRNATrp(UCA) with 5-hydroxy-L-tryptophan and not with any endogenous amino acid
W92A
-
mutant enzymes Trp92 to Phe, Trp92 to Gln and Trp92 to Ala. Mutant enzymes are inactive in partial reaction of Trp-activation and in overall reaction of tRNA tryptophanylation
W92F
-
mutant enzymes Trp92 to Phe, Trp92 to Gln and Trp92 to Ala. Mutant enzymes are inactive in partial reaction of Trp-activation and in overall reaction of tRNA tryptophanylation
W92Q
-
mutant enzymes Trp92 to Phe, Trp92 to Gln and Trp92 to Ala. Mutant enzymes are inactive in partial reaction of Trp-activation and in overall reaction of tRNA tryptophanylation
E438A
-
TrpRS single mutant
R135H
-
TrpRS single mutant
R135H/E438A
-
TrpRS double mutant, binds with Zn2+ or heme to enhance its aminoacylation activity
H445E
site-directed mutagenesis, the zebrafish mini mutant TrpRS interacts with VE-cadherin significantly as does human mini wild-type TrpRS, while the zebrafish wild-type enzyme does not
Q107K
site-directed mutagenesis, the zebrafish mini mutant TrpRS interacts with VE-cadherin significantly as does human mini wild-type TrpRS, while the zebrafish wild-type enzyme does not
Q146K
site-directed mutagenesis, the zebrafish mini mutant TrpRS interacts with VE-cadherin significantly as does human mini wild-type TrpRS, while the zebrafish wild-type enzyme does not
Q411K
site-directed mutagenesis, the zebrafish mini mutant TrpRS interacts with VE-cadherin significantly as does human mini wild-type TrpRS, while the zebrafish wild-type enzyme does not
D146A
-
site-directed mutagensis, the mutant shows highly reduced activity compared to the wild-type enzyme
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
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
H48N
-
naturally occuring mutation of TrpRS2
H48Q
-
naturally occuring mutation of TrpRS2
TrpRS2(H48N)
-
ORF mutant, constructed for analysing the indolmycin resistance
TrpRS2(H48Q)
-
ORF mutant, constructed for analysing the indolmycin resistance
TrpRS2(L9F)
-
ORF mutant, constructed for analysing the indolmycin resistance
TrpRS2(L9F/H48Q)
-
ORF mutant, constructed for analysing the indolmycin resistance
TrpRS2(L9F/Q13K)
-
ORF mutant, constructed for analysing the indolmycin resistance
TrpRS2(Q13K)
-
ORF mutant, constructed for analysing the indolmycin resistance
TrpRS2[C(-17)A/H48Q]
-
locus mutant, constructed for analysing the indolmycin resistance
TrpRS2[C(-17)A/L9F]
-
locus mutant, constructed for analysing the indolmycin resistance
TrpRS2[C(-17)A]
-
locus mutant, constructed for analysing the indolmycin resistance
TrpRS2[G(-13)T/H48Q]
-
locus mutant, constructed for analysing the indolmycin resistance
TrpRS2[G(-13)T/L9F]
-
locus mutant, constructed for analysing the indolmycin resistance
TrpRS2[G(-13)T]
-
locus mutant, constructed for analysing the indolmycin resistance
H48N
-
naturally occuring mutation of TrpRS2
-
H48Q
-
naturally occuring mutation of TrpRS2
-
H130R
site-directed mutagenesis, the Zn2+-unbound mutant cannot bind heme in contrast to the Zn2+-free wild-type enzyme
H130R
full-length H130R TrpRS is constitutively active, the mini H130R TrpRS mutant forms disulfide bonds and there are additional functional differences between the full-length and mini forms
H130R
mutant, constitutively active
additional information
full-legnth Arabidopsis thaliana TrpRS lacks the N-terminal domain compared to enzymes from mammls and Danio rerio
additional information
-
construction of deletion mutants with decreased activity by deletion of residues 108-122, causing loss of 44% activity, or 234-238, causing loss of 80% activity, or both parts, resulting in an inactive mutant enzyme, deletion of residues 234-238 affected the normally induced expression at 37°C
additional information
-
construction of tRNATrp mutants altered in the acceptor stem region, overview
additional information
bovine mini TrpRS lacks the first 52 amino acids
additional information
-
bovine mini TrpRS lacks the first 52 amino acids
additional information
Cryptosporidium parvum TrpRS remains fully active in charging tRNATrp after truncation of the N-terminal extra domain
additional information
-
Cryptosporidium parvum TrpRS remains fully active in charging tRNATrp after truncation of the N-terminal extra domain
additional information
zebrafish mini TrpRS lacks the first 42 amino acids
additional information
-
zebrafish mini TrpRS lacks the first 42 amino acids
additional information
-
developed an orthogonal tryptophanyl tRNA synthetase and tRNA pair, derived from Saccharomyces cerevisiae, modification of the G:C content of the anticodon stem and therefore reducing the structural flexibility of this stem eliminates misacylation by the Escherichia coli lysyl tRNA synthetase, and led to the development of a functional, orthogonal suppressor pair
additional information
-
developed an orthogonal tryptophanyl tRNA synthetase and tRNA pair, derived from Saccharomyces cerevisiae, modification of the G:C content of the anticodon stem and therefore reducing the structural flexibility of this stem eliminates misacylation by the Escherichia coli lysyl tRNA synthetase, and led to the development of a functional, orthogonal suppressor pair
-
additional information
-
construction of a catalytically active wild-type and mutant TrpRS minimal catalytic domains, structures, overview
additional information
multiple ligand binding conformation simulations with a virtual polyA mobile loop mutant and a virtual K111A mutant, interaction analysis, overview
additional information
-
multiple ligand binding conformation simulations with a virtual polyA mobile loop mutant and a virtual K111A mutant, interaction analysis, overview
additional information
construction of truncated enzyme variants, hemin binding capacities, overview
additional information
-
construction of truncated enzyme variants, hemin binding capacities, overview
additional information
preparation of alpha17 deletion mini-TrpRS, DELTAD382Q389, by site-directed mutagensis, overview
additional information
-
preparation of alpha17 deletion mini-TrpRS, DELTAD382Q389, by site-directed mutagensis, overview
additional information
generation of N-terminal 51 amino acid-deleted enzyme WRS mutant (mDELTAN51-WRS). The full-length wild-type enzyme, but not mini-WRS, activates macrophages to prime innate immune responses. The N-terminal 47 aa that are lacking in mini-WRS may be necessary for the correct orientation of the TLR4-MD2 dimers that is required for the activation of downstream signal pathways. Reduced levels of TNF-alpha and MIP-1alpha in culture supernatants of bone marrow derived macrophages treated with WRS enzyme mutants, except for mutant E35G causing slightly increased levels
additional information
-
generation of N-terminal 51 amino acid-deleted enzyme WRS mutant (mDELTAN51-WRS). The full-length wild-type enzyme, but not mini-WRS, activates macrophages to prime innate immune responses. The N-terminal 47 aa that are lacking in mini-WRS may be necessary for the correct orientation of the TLR4-MD2 dimers that is required for the activation of downstream signal pathways. Reduced levels of TNF-alpha and MIP-1alpha in culture supernatants of bone marrow derived macrophages treated with WRS enzyme mutants, except for mutant E35G causing slightly increased levels
additional information
-
generation of TrpRS-knockdown OEC-M1 cells by siRNA expression
additional information
human mini TrpRS lacks the first 47 amino acids
additional information
-
human mini TrpRS lacks the first 47 amino acids
additional information
targeted deletions and missense point mutations within the trpRS1 leader deregulate transcription
additional information
-
targeted deletions and missense point mutations within the trpRS1 leader deregulate transcription
additional information
-
targeted deletions and missense point mutations within the trpRS1 leader deregulate transcription
-
additional information
a Streptomyces coelicolor TrpRS1 null mutant is constructed
additional information
a Streptomyces coelicolor TrpRS1 null mutant is constructed
additional information
a Streptomyces coelicolor TrpRS2 null mutant is constructed
additional information
a Streptomyces coelicolor TrpRS2 null mutant is constructed
additional information
-
targeted deletions and missense point mutations within the trpRS1 leader deregulate transcription
additional information
-
targeted deletions and missense point mutations within the trpRS1 leader deregulate transcription
-
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Homo sapiens (P23381), Homo sapiens
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Homo sapiens (P23381), Homo sapiens
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Homo sapiens (P23381), Homo sapiens
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Streptomyces coelicolor, Streptomyces griseus (B1VQY7)
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Wakasugi, K.
An exposed cysteine residue of human angiostatic mini tryptophanyl-tRNA synthetase
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Homo sapiens (P23381), Homo sapiens
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Ghanipour, A.; Jirstroem, K.; Ponten, F.; Glimelius, B.; Pahlman, L.; Birgisson, H.
The prognostic significance of tryptophanyl-tRNA synthetase in colorectal cancer
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Homo sapiens
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Homo sapiens (P23381), Homo sapiens
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Homo sapiens (P23381), Homo sapiens
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Dong, X.; Zhou, M.; Zhong, C.; Yang, B.; Shen, N.; Ding, J.
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Pyrococcus horikoshii (O59584), Pyrococcus horikoshii
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Allostery and conformational free energy changes in human tryptophanyl-tRNA synthetase from essential dynamics and structure networks
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Homo sapiens (P23381), Homo sapiens
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Regulation of an auxiliary, antibiotic-resistant tryptophanyl-tRNA synthetase gene via ribosome-mediated transcriptional attenuation
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Streptomyces coelicolor, Streptomyces avermitilis (Q82HU1), Streptomyces avermitilis, Streptomyces coelicolor M600, Streptomyces avermitilis ATCC 31267 (Q82HU1)
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Arakaki, T.L.; Carter, M.; Napuli, A.J.; Verlinde, C.L.; Fan, E.; Zucker, F.; Buckner, F.S.; Van Voorhis, W.C.; Hol, W.G.; Merritt, E.A.
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Giardia intestinalis
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Cryptosporidium parvum (Q5CYP8), Cryptosporidium parvum, Entamoeba histolytica (C4LU94), Entamoeba histolytica (C4LUB5), Entamoeba histolytica (C4M7U9), Entamoeba histolytica, Trypanosoma brucei (Q580R7), Trypanosoma brucei
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Zhou, M.; Dong, X.; Shen, N.; Zhong, C.; Ding, J.
Crystal structures of Saccharomyces cerevisiae tryptophanyl-tRNA synthetase: new insights into the mechanism of tryptophan activation and implications for anti-fungal drug design
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Escherichia coli, Escherichia coli CSH108
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Guo, Q.; Gong, Q.; Tong, K.L.; Vestergaard, B.; Costa, A.; Desgres, J.; Wong, M.; Grosjean, H.; Zhu, G.; Wong, J.T.; Xue, H.
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Plasmodium falciparum
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Tsuchiya W, Umehara T, Kuno A, Hasegawa T.
Determination of tryptophan tRNA recognition sites for tryptophanyl-tRNA synthetase from hyperthermophilic archaeon, Aeropyrum pernix K1
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Aeropyrum pernix (Q9Y924), Aeropyrum pernix, Aeropyrum pernix DSM 11879 (Q9Y924)
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An appended domain results in an unusual architecture for malaria parasite tryptophanyl-tRNA synthetase
PLoS ONE
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Plasmodium falciparum (Q8IDW3), Plasmodium falciparum
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Mus musculus (P32921), Mus musculus
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An ancestral tryptophanyl-tRNA synthetase precursor achieves high catalytic rate enhancement without ordered ground-state tertiary structures
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Geobacillus stearothermophilus
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Al-Gubory, K.H.; Arianmanesh, M.; Garrel, C.; Fowler, P.A.
The conceptus regulates tryptophanyl-tRNA synthetase and superoxide dismutase 2 in the sheep caruncular endometrium during early pregnancy
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Ovis aries (W5NVE5), Ovis aries
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Selective inhibition of bacterial tryptophanyl-tRNA synthetases by indolmycin is mechanism-based
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Geobacillus stearothermophilus (P00953), Geobacillus stearothermophilus
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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
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Homo sapiens (P23381), Homo sapiens, Mus musculus (P32921), Mus musculus, Mus musculus C57BL/6 (P32921)
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Dong, X.; Zhou, M.; Zhong, C.; Yang, B.; Shen, N.; Ding, J.
Crystal structure of Pyrococcus horikoshii tryptophanyl-tRNA synthetase and structure-based phylogenetic analysis suggest an archaeal origin of tryptophanyl-tRNA synthetase
Nucleic Acids Res.
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Pyrococcus horikoshii (O59584), Pyrococcus horikoshii
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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
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Homo sapiens
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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
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24750
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Bos taurus (P17248), Bos taurus, Homo sapiens (P23381), Homo sapiens, Danio rerio (Q6PBS3), Danio rerio, Arabidopsis thaliana (Q9SR15)
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