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Information on EC 6.1.1.2 - tryptophan-tRNA ligase
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6.1.1.2 tryptophan-tRNA ligaseSpecify your search results
Word Map
- 6.1.1.2
- synthetases
- aminoacyl-trna
- aminoacylation
- pancreas
- beef
- stearothermophilus
-
anticodon
- tyrrs
-
kmsks
- indoleamine
- tyrosyl-trna
-
angiostatic
- tryptamine
-
ido
-
tryptophan-dependent
- glutaminyl-trna
- glnrs
- medicine
- ap4a
-
aarss
-
anticodon-binding
- synthesis
- biotechnology
The enzyme appears in viruses and cellular organisms
Synonyms
tryptophanyl-trna synthetase, trprs, wars2, t2-trprs, mini-trprs, tryptophanyl trna synthetase, htrprs, trprs1, trprs ii, trp-rs, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
BsTRpRS
T2-TrpRS
TrpRS
TrpRS1
TrpRS2
tryptophanyl tRNA synthetase
Tryptophanyl-tRNA synthase
Tryptophanyl-tRNA synthetase
trytophanyl-tRNA synthetase
tyrosyl tRNA synthetase
WARS
WRS
additional information
TrpRS
-
Tryptophanyl-tRNA synthetase
-
additional information
TrpRS is a class I aminoacyl-tRNA synthetase characterized by a Rossmann-fold catalytic domain whose active site is recognizable by the presence of two conserved sequence motifs with consensus sequences HIGH and KMSKS
additional information
TrpRS is a class I aminoacyl-tRNA synthetase characterized by a Rossmann-fold catalytic domain whose active site is recognizable by the presence of two conserved sequence motifs with consensus sequences HIGH and KMSKS
additional information
TrpRS is a class I aminoacyl-tRNA synthetase characterized by a Rossmann-fold catalytic domain whose active site is recognizable by the presence of two conserved sequence motifs with consensus sequences HIGH and KMSKS
additional information
TrpRS is a class I aminoacyl-tRNA synthetase characterized by a Rossmann-fold catalytic domain whose active site is recognizable by the presence of two conserved sequence motifs with consensus sequences HIGH and KMSKS
additional information
-
the enzyme belongs to the class I aminoacyl-tRNA transferases
additional information
-
the enzyme belongs to the class I aminoacyl-tRNA synthetases
additional information
TrpRS is a class I aminoacyl-tRNA synthetase characterized by a Rossmann-fold catalytic domain whose active site is recognizable by the presence of two conserved sequence motifs with consensus sequences HIGH and KMSKS
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + L-tryptophan + tRNATrp = AMP + diphosphate + L-tryptophyl-tRNATrp
-
-
-
-
ATP + L-tryptophan + tRNATrp = AMP + diphosphate + L-tryptophyl-tRNATrp
2-step reaction, tRNATrp substrate recognition, mechanism and modeling
-
ATP + L-tryptophan + tRNATrp = AMP + diphosphate + L-tryptophyl-tRNATrp
active site, 2 critical positions for amino acid discrimination
ATP + L-tryptophan + tRNATrp = AMP + diphosphate + L-tryptophyl-tRNATrp
random, bi-bi kinetic scheme mechanism, KMSKS motif loop is involved in the catalytic mechanism
ATP + L-tryptophan + tRNATrp = AMP + diphosphate + L-tryptophyl-tRNATrp
wide opening active site that adopts a compact conformation, modeling of substrate recognition and binding
ATP + L-tryptophan + tRNATrp = AMP + diphosphate + L-tryptophyl-tRNATrp
a nested, nonlinear model for the sum of metal-free and metal-catalyzed activities and its use in determining metal-free enzyme activity jointly with transition-state metal binding affinity is described, by fitting observed values obtained from Mg2+-depleted assays with increasing EDTA concentrations at known Mg2+ concentrations. Trp activation by TrpRS falls asymptotically to a plateau value 5 orders of magnitude below that observed for the Mg2+-supplemented enzyme at EDTA concentrations that reduce the free metal concentration to below 1 pmolar. The fitted regression model parameters yield a relative rate acceleration of 93000 attributable to the catalytic effect of Mg2+ and an enhanced transition state binding of Mg2+. Factorial analysis indicates that 80% of the reduction in free energy of activation effected by TrpRS arises from protein-ligand interactions
-
ATP + L-tryptophan + tRNATrp = AMP + diphosphate + L-tryptophyl-tRNATrp
recognition of Trp is by an induced-fit mechanism involving conformational change of the AIDQ motif that creates a perfect pocket for the binding and activation of Trp and causes coupled movements of the N-terminal and C-terminal domains. The KMSAS loop has an inherent flexibility and binding of ATP stabilizes it in a closed conformation that secures the position of ATP for catalysis. Structural data indicate that the catalytic mechanism of the Trp activation reaction by hTrpRS involves more moderate conformational changes of the structural elements at the active site compared to bacterial TrpRS
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Aminoacylation
esterification
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PATHWAY SOURCE
PATHWAYS
BRENDA
MetaCyc
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SYSTEMATIC NAME
IUBMB Comments
L-tryptophan:tRNATrp ligase (AMP-forming)
-
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CAS REGISTRY NUMBER
COMMENTARY
9023-44-3
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + 2-azatryptophan + tRNATrp
AMP + diphosphate + 2-azatryptophyl-tRNATrp
-
-
-
?
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(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
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophan-tRNATrp
-
-
-
?
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophan-tRNATrp
-
-
-
?
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophan-tRNATrp
-
-
-
?
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophan-tRNATrp
-
-
-
?
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophan-tRNATrp
-
-
-
?
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophan-tRNATrp
-
-
-
?
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophan-tRNATrp
-
-
-
?
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophan-tRNATrp
-
2-step reaction, tRNATrp substrate recognition, mechanism and modeling
-
?
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophan-tRNATrp
-
the 3 base pairs G2.C71, G3.C70, and G4.C69 are important identity elements in the tRNA acceptor stem providing tRNA substrate recognition for the enzyme, also the G73 discriminator base is involved in the recognition but cannot itself confer efficient aminoacylation activity
-
?
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophan-tRNATrp
-
BsTRpRS charges only the cognate mutant opal suppressor tRNATrp(UCA) and not endogenous mammalian tRNAs
-
?
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophan-tRNATrp
-
does not activate any natural amino acid except L-tryptophan
-
?
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophan-tRNATrp
wild-type and recombinant enzyme are specific for tRNATrp
-
?
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophan-tRNATrp
enzyme is required for embryonic survival, and is essential for viability of the fly
-
?
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophan-tRNATrp
-
-
-
?
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophan-tRNATrp
-
-
-
?
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophan-tRNATrp
-
-
-
?
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophan-tRNATrp
-
-
-
?
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophan-tRNATrp
-
-
-
?
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophan-tRNATrp
-
-
-
?
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophan-tRNATrp
-
-
-
?
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophan-tRNATrp
-
-
-
?
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophan-tRNATrp
-
-
-
?
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophan-tRNATrp
-
-
-
?
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophan-tRNATrp
-
-
?
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophan-tRNATrp
-
-
-
?
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophan-tRNATrp
-
-
-
?
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophan-tRNATrp
-
-
-
?
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophan-tRNATrp
-
-
-
?
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophan-tRNATrp
-
-
?
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophan-tRNATrp
-
-
?
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophan-tRNATrp
-
-
?
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophan-tRNATrp
-
full-length and mini enzyme isoforms
-
?
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophan-tRNATrp
-
enzyme contributes to biological processes involving cell signaling such as angiogenesis regulation
-
?
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophan-tRNATrp
-
full-length and mini enzyme isoforms, enzyme expression is regulated by a dual system of interferon gamma and interferon regulatory factor 1 via 2 specific tandem promoters leading to alternative splicing
-
?
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophan-tRNATrp
-
human mini, but not full-length, tryptophanyl-tRNA synthetase may play an important role in the intracellular regulation of protein synthesis under conditions of oxidative stress
-
?
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophan-tRNATrp
-
-
-
?
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
-
?
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
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
-
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
-
?
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
?
-
-
binding stoichiometry of tRNATrp and tryptophanyl-tRNA synthetase
-
?
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
?
-
-
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.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + 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
-
-
-
?
additional information
?
-
-
possibly involved in function other than tRNA aminoacylation
-
-
?
additional information
?
-
-
enzyme might by implicated in regulation of P1,P3-bis(5'-adenosyl)triphosphate/P1,P4-bis(5'-adenosyl)tetraphosphate ratio in the cell
-
-
?
additional information
?
-
-
tryptophanyl tRNA synthetase II interacts with nitric oxide synthetase and increases activity of nitric oxide synthetase
-
-
?
additional information
?
-
-
an ancestral tryptophanyl-tRNA synthetase precursor achieves high catalytic rate enhancement without ordered ground-state tertiary structures
-
-
?
additional information
?
-
-
mini isozyme specifically shows anti-proliferative and anti-angiogenic activity
-
?
additional information
?
-
the catalytic fragment exhibits potent angiostatic activity
-
?
additional information
?
-
-
the catalytic fragment exhibits potent angiostatic activity
-
?
additional information
?
-
-
the enzymes C-terminal domain, an EMAP II-like protein, inhibits angiogenesis signaling pathways and the development of blood vessels
-
?
additional information
?
-
-
interferon-gamma-inducible enzyme. Exposure to soluble cytotoxic T lymphocyte antigen-4 induces increased expression of tryptophanyl-tRNA synthetase in unseparated peripheral blood mononuclear cells, as well as in monocyte-derived mature dentritic cells. CD4+ cells and CD8+ cells isolated from peripheral blood mononuclear cells treated with soluble cytotoxic T lymphocyte antigen-4 show increased tryptophanyl-tRNA synthetase compared with untreated cells. Possibility that tryptophanyl-tRNA synthetase may be involved in an important mechanism regulating immune response
-
-
?
additional information
?
-
-
the vascular endothelial-cadherin-dependent pathway is proposed to link T2-TrpRS to inhibition of new blood vessel formation
-
-
?
additional information
?
-
-
tryptamine induces tryptophanyl-tRNA synthetase-mediated neurodegeneration with neurofibrillary tangles in human cell models, the dietary supplementation with tryptophan as a tryptamine competitor may not counteract the deleterious influence of tryptamine, overview
-
-
?
additional information
?
-
binding of vascular endothelial (VE)-cadherin, the NH2-terminal Trp2 and Trp4 residues of VE-cadherin are docked into the Trp- and adenosine-binding pockets of human TrpRS
-
-
?
additional information
?
-
-
binding of vascular endothelial (VE)-cadherin, the NH2-terminal Trp2 and Trp4 residues of VE-cadherin are docked into the Trp- and adenosine-binding pockets of human TrpRS
-
-
?
additional information
?
-
-
tryptamine induces tryptophanyl-tRNA synthetase-mediated neurodegeneration with neurofibrillary tangles in mouse models, the dietary supplementation with tryptophan as a tryptamine competitor may not counteract the deleterious influence of tryptamine, overview
-
-
?
additional information
?
-
-
tryptamine induces tryptophanyl-tRNA synthetase-mediated neurodegeneration with neurofibrillary tangles in mouse models, the dietary supplementation with tryptophan as a tryptamine competitor may not counteract the deleterious influence of tryptamine, overview
-
-
?
additional information
?
-
-
probably the enzyme fulfills some unknown function(s) important for digestion
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ATP
assemble of the ATP binding site by domain movement, acts as a key allosteric effector on the enzyme, conformational trigger, not requiring tryptophan pocket ligands, enzyme forms high-affinity complexes at low ATP concentration and low-affinity complexes at high ATP concentration
ATP
Mg2+-ATP interactions are coupled to interactions between ATP and active-site lysine side-chains
ATP
-
the ATP-binding site, a loop formed by the residues 311-315 of the KMSAS motif, is sandwiched by the characteristic class I HIGH motif, residues 84-87, and by residues 272-275 of a GIEQ motif that is weakly conserved among TrpRS sequences
additional information
indolmycin and ATP form a ternary complex with BsTrpRS
-
additional information
-
indolmycin and ATP form a ternary complex with BsTrpRS
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
Mn2+
replacing Mg2+ with Mn2+ reduces the specificity for L-tryptophan, increasing the relative activation of L-tyrosine by about 3.5fold
Zn2+
additional information
Mg2+
Mg2+-ATP interactions are coupled to interactions between ATP and active-site lysine side-chains
Zn2+
TrpRS is a Zn2+-binding protein, highly activates the enzyme, the activation effect is reduced by protoporphyrin IX, overview
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2-[5-[(6-(ethoxycarbonyl)-5-(4-fluorophenyl)-3-oxo-7-phenyl-5H-[1,3]thiazolo[3,2-a]pyrimidin-2(3H)-ylidene)methyl]-2-furyl]benzoic acid
-
3-[(4-[[4-oxo-2-(phenylimino)-1,3-thiazolidin-5-ylidene]methyl]phenoxy) methyl]benzoic acid
-
3-[[([[2-(4-chlorophenyl)-4-quinolinyl]carbonyl]amino)carbothioyl]amino]benzoic acid
-
Adenosine-5'-chloromethylphosphonate
-
ATP-diphosphate exchange, reversible, incompetitive
succinylacetone
a heme biosynthesis inhibitor, inhibit cellular TrpRS activity in IFN-gamma-activated cells without affecting TrpRS protein expression
chuangxinmycin
-
CAS: 63339-68-4, natural product, first isolated from Actinoplanes tsinanensis, potent and selective inhibition of the aminoacylation
indolmycin
competitive inhibitor, produced by Streptomyces griseus, causes selective, mechanism-based inhibition of the bacterial enzyme, which preferentially binds indolmycin about 1500fold more tightly than its tryptophan substrate, binding structure analysis overview. Long range coupling to residues within an allosteric region called the D1 switch of BsTrpRS positions the Mg2+ ion in a manner that allows it to assist in transition state stabilization. The Mg2+ ion in the inhibited complex forms significantly closer contacts with non-bridging oxygen atoms from each phosphate group of ATP and three water molecules than occur in the (presumably catalytically competent) pre-transition state (preTS) crystal structures. This altered coordination stabilizes a ground state Mg2+-ATP-configuration, accounting for the high affinity inhibition of BsTrpRS by indolmycin
tryptamine
-
competitive, inhibition of the enzyme leads to inhibition of protein biosynthesis, tryptamine stabilizes the enzyme
tryptamine
-
a metabolic tryptophan analog that acts as a potent competitive inhibitor of TrpRS, overview
tryptamine
-
a metabolic tryptophan analog that acts as a potent competitive inhibitor of TrpRS, overview
additional information
indolmycin and ATP form a ternary complex with BsTrpRS
-
additional information
-
indolmycin and ATP form a ternary complex with BsTrpRS
-
additional information
the full-length-WRS-induced TNF-alpha and MIP-1alpha production is significantly inhibited when TLR4, MD2, and TLR2 (to lesser degree) are suppressed
-
additional information
-
the full-length-WRS-induced TNF-alpha and MIP-1alpha production is significantly inhibited when TLR4, MD2, and TLR2 (to lesser degree) are suppressed
-
additional information
the full-length-WRS-induced TNF-alpha and MIP-1alpha production is significantly inhibited when TLR4, MD2, and TLR2 (to lesser degree) are suppressed
-
additional information
-
the full-length-WRS-induced TNF-alpha and MIP-1alpha production is significantly inhibited when TLR4, MD2, and TLR2 (to lesser degree) are suppressed
-
additional information
-
no inhibition by chuangximycin methyl ester, hydroxamic acid, amide, hydroxymethyl or tetrazole analogue
-
additional information
screening for SeWRS inhibitors, binding site mapping and virtual screening, modeling, overview, MIC values, and cytotoxic activities of inhibitors, overview
-
additional information
-
screening for SeWRS inhibitors, binding site mapping and virtual screening, modeling, overview, MIC values, and cytotoxic activities of inhibitors, overview
-
additional information
-
indolmycin, a potential antibacterial drug, completely inhibits bacterial tryptophanyl-tRNA synthetases, identifying indolmycin resistance genes leads to the discovery of a gene encoding an indolmycin-resistant isoform of tryptophanyl-tRNA synthetase
-
additional information
indolmycin, a potential antibacterial drug, completely inhibits bacterial tryptophanyl-tRNA synthetases, identifying indolmycin resistance genes leads to the discovery of a gene encoding an indolmycin-resistant isoform of tryptophanyl-tRNA synthetase
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
glyceraldehyde 3-phosphate dehydrogenase
-
the oxidized form of glyceraldehyde 3-phosphate dehydrogenase interacts with both full-length and mini tryptophanyl-tRNA synthetase and specifically stimulates the aminoacylation potential of mini, but not full-length tryptophanyl-tRNA synthetase. In contrast, reduced glyceraldehyde 3-phosphate dehydrogenase does not bind to tryptophanyl-tRNA synthetase and does not influence their aminoacylation activity
-
hemin
heme can interact strongly with Zn2+-depleted full-length TrpRS, but not the Zn2+-bound enzyme, with a stoichiometric heme:protein ratio of 1:1 to enhance the aminoacylation activity significantly, involvement of heme in regulation of TrpRS aminoacylation activity, overview
interferon regulatory factor 1
-
stimulates and regulates the enzyme isoforms expression via 2 specific interferon-gamma-sensitive promoters that are additionally regulated by the interferon gamma
-
interferons
-
interferons alpha, beta, and gamma, induction of accumulation of the enzyme, organelle-specific, the highest content is observed in the cytoplasm, followd by the nucleolus and the nucleus, the latter with a low enzyme content
-
interferon gamma
-
strong upregulation of the alternatively spliced truncated mini enzyme form
-
interferon gamma
-
strongly stimulates and regulates the expression of the enzyme isoforms via 2 specific interferon-gamma-sensitive promoters that are additionally regulated by the interferon regulatory factor 1
-
additional information
TrpRS is highly upregulated by interferon-gamma, IFN-gamma
-
additional information
-
TrpRS is highly upregulated by interferon-gamma, IFN-gamma
-
additional information
-
tryptamine induces tryptophanyl-tRNA synthetase-mediated neurodegeneration with neurofibrillary tangles in human cell models, overview
-
additional information
-
tryptamine induces tryptophanyl-tRNA synthetase-mediated neurodegeneration with neurofibrillary tangles in mouse models, overview
-
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
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.
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.
Gastrointestinal Stromal Tumors
Role of Immune Microenvironment in Gastrointestinal Stromal Tumors.
Hyperkinesis
Mutation of the WARS2 Gene as the Cause of a Severe Hyperkinetic Movement Disorder.
Infections
Corrigendum: Secreted tryptophanyl-tRNA synthetase as a primary defence system against infection.
Infections
Secreted tryptophanyl-tRNA synthetase as a primary defence system against infection.
Intellectual Disability
Biallelic mutations in mitochondrial tryptophanyl-tRNA synthetase cause Levodopa-responsive infantile-onset Parkinsonism.
Intellectual Disability
Deficiency of WARS2, encoding mitochondrial tryptophanyl tRNA synthetase, causes severe infantile onset leukoencephalopathy.
Intellectual Disability
Mutations of the aminoacyl-tRNA-synthetases SARS and WARS2 are implicated in the etiology of autosomal recessive intellectual disability.
Leukemia
Chaperon-like Activation of Serum-Inducible Tryptophanyl-tRNA Synthetase Phosphorylation through Refolding as a Tool for Analysis of Clinical Samples.
Leukemia, Myeloid
Interferons induce accumulation of diadenosine triphosphate (Ap3A) in human cultured cells.
Leukoencephalopathies
Biallelic mutations in mitochondrial tryptophanyl-tRNA synthetase cause Levodopa-responsive infantile-onset Parkinsonism.
Leukoencephalopathies
Deficiency of WARS2, encoding mitochondrial tryptophanyl tRNA synthetase, causes severe infantile onset leukoencephalopathy.
Leukoencephalopathies
Mutations in the mitochondrial tryptophanyl-tRNA synthetase cause growth retardation and progressive leukoencephalopathy.
Lymphoma
Design and synthesis of novel spirooxindole-indenoquinoxaline derivatives as novel tryptophanyl-tRNA synthetase inhibitors.
Lymphoma, B-Cell
Design and synthesis of novel spirooxindole-indenoquinoxaline derivatives as novel tryptophanyl-tRNA synthetase inhibitors.
Malaria
An appended domain results in an unusual architecture for malaria parasite tryptophanyl-tRNA synthetase.
Melanoma
Tryptophanyl-tRNA synthetase (WARS) expression in uveal melanoma - possible contributor during uveal melanoma progression.
Microcephaly
Deficiency of WARS2, encoding mitochondrial tryptophanyl tRNA synthetase, causes severe infantile onset leukoencephalopathy.
Mitochondrial Diseases
Biallelic variants in WARS2 encoding mitochondrial tryptophanyl-tRNA synthase in six individuals with mitochondrial encephalopathy.
Mitochondrial Diseases
Mutations in the mitochondrial tryptophanyl-tRNA synthetase cause growth retardation and progressive leukoencephalopathy.
Mouth Neoplasms
Overexpressed tryptophanyl-tRNA synthetase, an angiostatic protein, enhances oral cancer cell invasiveness.
Movement Disorders
Co-occurring WARS2 and CHRNA6 mutations in a child with a severe form of infantile parkinsonism.
Movement Disorders
Mutation of the WARS2 Gene as the Cause of a Severe Hyperkinetic Movement Disorder.
Myocardial Infarction
Different angiogenesis effect of mini-TyrRS/mini-TrpRS by systemic administration of modified siRNAs in rats with acute myocardial infarction.
Myocardial Infarction
Effect of mini-tyrosyl-tRNA synthetase/mini-tryptophanyl-tRNA synthetase on ischemic angiogenesis in rats: proliferation and migration of endothelial cells.
Myocardial Infarction
Tryptophanyl-tRNA synthetase gene polymorphisms and risk of incident myocardial infarction.
Neoplasm Metastasis
The prognostic significance of tryptophanyl-tRNA synthetase in colorectal cancer.
Neoplasms
Chaperon-like Activation of Serum-Inducible Tryptophanyl-tRNA Synthetase Phosphorylation through Refolding as a Tool for Analysis of Clinical Samples.
Neoplasms
Differential protein synthesis and expression levels in normal and neoplastic human prostate cells and their regulation by type I and II interferons.
Neoplasms
Evidence for the involvement of SDF-1 and CXCR4 in the disruption of endothelial cell-branching morphogenesis and angiogenesis by TNF-alpha and IFN-gamma.
Neoplasms
Hypoxia signature of splice forms of tryptophanyl-tRNA synthetase marks pancreatic cancer cells with distinct metastatic abilities.
Neoplasms
Overexpressed tryptophanyl-tRNA synthetase, an angiostatic protein, enhances oral cancer cell invasiveness.
Neoplasms
Prediction of Recurrence and Survival for Triple-Negative Breast Cancer (TNBC) by a Protein Signature in Tissue Samples.
Neoplasms
The prognostic significance of tryptophanyl-tRNA synthetase in colorectal cancer.
Neoplasms
The role of indoleamine 2,3-dioxygenase in the anti-tumour activity of human interferon-gamma in vivo.
Neuroblastoma
Mapping and molecular characterization of novel monoclonal antibodies to conformational epitopes on NH2 and COOH termini of mammalian tryptophanyl-tRNA synthetase reveal link of the epitopes to aggregation and Alzheimer's disease.
Neurodegenerative Diseases
Tryptamine Induces Tryptophanyl-tRNA Synthetase-Mediated Neurodegeneration With Neurofibrillary Tangles in Human Cell and Mouse Models.
Obesity, Abdominal
Mutant Wars2 gene in spontaneously hypertensive rats impairs brown adipose tissue function and predisposes to visceral obesity.
Ovarian Neoplasms
Chaperon-like Activation of Serum-Inducible Tryptophanyl-tRNA Synthetase Phosphorylation through Refolding as a Tool for Analysis of Clinical Samples.
Pancreatic Neoplasms
Hypoxia signature of splice forms of tryptophanyl-tRNA synthetase marks pancreatic cancer cells with distinct metastatic abilities.
Pancreatic Neoplasms
Mapping and molecular characterization of novel monoclonal antibodies to conformational epitopes on NH2 and COOH termini of mammalian tryptophanyl-tRNA synthetase reveal link of the epitopes to aggregation and Alzheimer's disease.
Parkinsonian Disorders
Biallelic mutations in mitochondrial tryptophanyl-tRNA synthetase cause Levodopa-responsive infantile-onset Parkinsonism.
Parkinsonian Disorders
Co-occurring WARS2 and CHRNA6 mutations in a child with a severe form of infantile parkinsonism.
Protein Deficiency
Diet-Related Metabolic Perturbations of Gut Microbial Shikimate Pathway-Tryptamine-tRNA Aminoacylation-Protein Synthesis in Human Health and Disease.
Quadriplegia
Deficiency of WARS2, encoding mitochondrial tryptophanyl tRNA synthetase, causes severe infantile onset leukoencephalopathy.
Renal Insufficiency, Chronic
Serum levels and activity of indoleamine2,3-dioxygenase and tryptophanyl-tRNA synthetase and their association with disease severity in patients with chronic kidney disease.
Sarcoma, Avian
Chaperon-like Activation of Serum-Inducible Tryptophanyl-tRNA Synthetase Phosphorylation through Refolding as a Tool for Analysis of Clinical Samples.
Seizures
Expanding the Phenotype: Neurodevelopmental Disorder, Mitochondrial, With Abnormal Movements and Lactic Acidosis, With or Without Seizures (NEMMLAS) due to WARS2 Biallelic Variants, Encoding Mitochondrial Tryptophanyl-tRNA Synthase.
Seizures
Expanding the Phenotype: Neurodevelopmental Disorder, Mitochondrial, With Abnormal Movements and Lactic Acidosis, With or Without Seizures (NEMMLAS) Due to WARS2 Biallelic Variants, Encoding Mitochondrial Tryptophanyl-tRNA Synthase.
Sepsis
Clinical value of full-length tryptophanyl-tRNA synthetase for sepsis detection in critically ill patients - A retrospective clinical assessment.
Stomach Neoplasms
Expression of Indoleamine 2, 3-dioxygenase 1 (IDO1) and Tryptophanyl-tRNA Synthetase (WARS) in Gastric Cancer Molecular Subtypes.
tryptophan-trna ligase deficiency
Biallelic mutations in mitochondrial tryptophanyl-tRNA synthetase cause Levodopa-responsive infantile-onset Parkinsonism.
tryptophan-trna ligase deficiency
Severe hepatopathy and neurological deterioration after start of valproate treatment in a 6-year-old child with mitochondrial tryptophanyl-tRNA synthetase deficiency.
Virus Diseases
Released Tryptophanyl-tRNA Synthetase Stimulates Innate Immune Responses against Viral Infection.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00006
Archeoglobus fulgidus tRNATrp(A73, wild-type)
pH 7.0, 65°C
-
0.00009
Bacillus subtilis tRNATrp(A73, wild-type)
pH 7.0, 65°C
-
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
0.00527
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
0.0005
tRNATrp
-
22°C, pH 7.5, tRNATrp from Bacillus subtilis, mutant enzyme K149R, aminoacylation
0.00061
tRNATrp
-
22°C, pH 7.5, tRNATrp from Bacillus subtilis, wild-type enzyme, aminoacylation
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
0.00113
tRNATrp
-
22°C, pH 7.5, tRNATrp from Bacillus subtilis, mutant enzyme E153K, aminoacylation
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
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
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.53
Archeoglobus fulgidus tRNATrp(A73, wild-type)
pH 7.0, 65°C
-
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
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
0.03
tRNATrp
-
22°C, pH 7.5, tRNATrp from Bacillus subtilis, mutant enzyme E153D, aminoacylation
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
0.67
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
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
164
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
1090
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
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
indolmycin Michaelis-Menten inhibition kinetics
-
additional information
additional information
-
indolmycin Michaelis-Menten inhibition kinetics
-
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0187 - 0.0228
2-[5-[(6-(ethoxycarbonyl)-5-(4-fluorophenyl)-3-oxo-7-phenyl-5H-[1,3]thiazolo[3,2-a]pyrimidin-2(3H)-ylidene)methyl]-2-furyl]benzoic acid
0.0151 - 0.0183
3-[(4-[[4-oxo-2-(phenylimino)-1,3-thiazolidin-5-ylidene]methyl]phenoxy) methyl]benzoic acid
0.0352 - 0.0422
3-[[([[2-(4-chlorophenyl)-4-quinolinyl]carbonyl]amino)carbothioyl]amino]benzoic acid
0.0187
2-[5-[(6-(ethoxycarbonyl)-5-(4-fluorophenyl)-3-oxo-7-phenyl-5H-[1,3]thiazolo[3,2-a]pyrimidin-2(3H)-ylidene)methyl]-2-furyl]benzoic acid
Staphylococcus epidermidis
pH 8.0, 25°C, assay method b
0.0228
2-[5-[(6-(ethoxycarbonyl)-5-(4-fluorophenyl)-3-oxo-7-phenyl-5H-[1,3]thiazolo[3,2-a]pyrimidin-2(3H)-ylidene)methyl]-2-furyl]benzoic acid
Staphylococcus epidermidis
pH 8.0, 25°C, assay method a
0.0151
3-[(4-[[4-oxo-2-(phenylimino)-1,3-thiazolidin-5-ylidene]methyl]phenoxy) methyl]benzoic acid
Staphylococcus epidermidis
pH 8.0, 25°C, assay method b
0.0183
3-[(4-[[4-oxo-2-(phenylimino)-1,3-thiazolidin-5-ylidene]methyl]phenoxy) methyl]benzoic acid
Staphylococcus epidermidis
pH 8.0, 25°C, assay method a
0.0352
3-[[([[2-(4-chlorophenyl)-4-quinolinyl]carbonyl]amino)carbothioyl]amino]benzoic acid
Staphylococcus epidermidis
pH 8.0, 25°C, assay method b
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20
22
25
30
37
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain ATCC 12228; strains ATCC 12228 and ATCC 35984
SwissProt
brenda
gene trpRS1, an auxiliary, antibiotic-resistant tryptophanyl-tRNA synthetase gene
-
-
brenda
TrpRS homologue 1; the Entamoeba histolytica genome contains three sequences that appear to be TrpRS homologues
UniProt
brenda
TrpRS homologue 2; the Entamoeba histolytica genome contains three sequences that appear to be TrpRS homologues
UniProt
brenda
TrpRS homologue 3; the Entamoeba histolytica genome contains three sequences that appear to be TrpRS homologues
UniProt
brenda
purified native and selenomethionyl enzyme
Uniprot
brenda
2 enzyme isoforms by alternative splicing in vivo, i.e. full-length and mini enzyme
-
-
brenda
mitochondrial specific isozyme containing a mitochondrial localization signal sequence
SwissProt
brenda
gene trpRS1, an auxiliary, antibiotic-resistant tryptophanyl-tRNA synthetase gene
-
-
brenda
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
UniProt
brenda