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ATP + 3-(2-naphthyl)alanine + tRNATyr
AMP + diphosphate + 3-(2-naphthyl)alanyl-tRNATyr
ATP + 3-(5-hydroxypyridin-2-yl)-L-alanine + tRNATyr
?
-
-
-
-
?
ATP + 3-amino-L-tyrosine + tRNATyr
AMP + 3-amino-L-Tyr-tRNATyr + diphosphate
-
mutant Y43G, aminoacylation assay
-
?
ATP + 3-azido-L-tyrosine + tRNATyr
AMP + 3-azido-L-Tyr-tRNATyr + diphosphate
-
mutant Y43G, aminoacylation assay
-
?
ATP + 3-azido-L-tyrosine + tRNATyr
AMP + diphosphate + 3-azido-L-tyrosyl-tRNATyr
ATP + 3-chloro-L-tyrosine + tRNATyr
AMP + 3-chloro-L-Tyr-tRNATyr + diphosphate
-
mutant Y43G, aminoacylation assay
-
?
ATP + 3-iodo-L-tyrosine + tRNATyr
AMP + 3-iodo-L-Tyr-tRNATyr + diphosphate
-
mutant Y43G, aminoacylation assay
-
?
ATP + 3-iodo-L-tyrosine + tRNATyr
AMP + diphosphate + 3-iodo-L-tyrosyl-tRNATyr
ATP + 3-iodo-L-tyrosine + tRNATyr
AMP + L-Tyr-tRNATyr + diphosphate
-
mutant Y73V/Q195C and other mutants, no activity with the wild-type enzyme
-
?
ATP + 3-methoxy-L-tyrosine + tRNATyr
AMP + 3-methoxy-L-Tyr-tRNATyr + diphosphate
-
mutant Y43G, aminoacylation assay
-
?
ATP + 3-nitro-L-tyrosine + tRNATyr
AMP + 3-nitro-L-Tyr-tRNATyr + diphosphate
-
mutant Y43G, aminoacylation assay
-
?
ATP + 4-acetylphenylalanine + tRNATyr
AMP + diphosphate + 4-acetylphenylalanyl-tRNATyr
ATP + 4-bromophenylalanine + tRNATyr
AMP + diphosphate + 4-bromophenylalanyl-tRNATyr
ATP + D-3,4-dihydroxyphenylalanine + tRNATyr
AMP + D-3,4-dihydroxyphenylalanine-tRNATyr + diphosphate
-
mutant Y43G, aminoacylation assay
-
?
ATP + D-tyrosine + tRNATyr
AMP + D-Tyr-tRNATyr + diphosphate
-
mutant Y43G, aminoacylation assay
-
?
ATP + D-tyrosine + tRNATyr
AMP + diphosphate + D-tyrosyl-tRNATyr
-
enzyme TyrRS has a detectable, natural activity for the D-tyrosine stereoisomer, only tenfold less than for L-Tyr
-
-
?
ATP + L-3,4-dihydroxyphenylalanine + tRNATyr
AMP + L-3,4-dihydroxyphenylalanine-tRNATyr + diphosphate
-
mutant Y43G, aminoacylation assay
-
?
ATP + L-beta-(5-hydroxy-2-pyridyl)-alanine + tRNATyr
AMP + L-beta-(5-hydroxy-2-pyridyl)-alanine-tRNATyr + diphosphate
ATP + L-tyrosine + tRNATyr
AMP + diphosphate + L-tyrosyl-tRNATyr
ATP + L-tyrosine + tRNATyr
AMP + L-Tyr-tRNATyr + diphosphate
ATP + L-tyrosine + tRNATyr(G34C)
AMP + diphosphate + L-tyrosyl-tRNATyr(G34C)
ATP + L-tyrosine + tRNATyr(wild-type)
AMP + diphosphate + L-tyrosyl-tRNATyr(wild-type)
ATP + L-tyrosine + tRNATyrGTA
AMP + diphosphate + L-tyrosyl-tRNATyrGTA
two sequences, tRNATyr1 and tRNATyr2, substrate CHO tRNATyrGTA is recombinantly expressed. CHOTyrRS is able to attach Phe to both tRNATyr2 and CHO total tRNA containing native tRNATyr, excluding the possibility that mischarging results from the lack of post-transcriptional modifications to the in vitro-transcribed substrate
-
-
?
ATP + m-fluoro-D,L-tyrosine + tRNATyr
AMP + m-fluoro-D,L-Tyr-tRNATyr + diphosphate
-
mutant Y43G, aminoacylation assay
-
?
ATP + N-acetyl-L-tyrosine + tRNATyr
AMP + N-acetyl-L-Tyr-tRNATyr + diphosphate
-
wild-type and mutant Y43G, aminoacylation assay
-
?
ATP + N-formyl-L-tyrosine + tRNATyr
AMP + N-formyl-L-Tyr-tRNATyr + diphosphate
-
wild-type and mutant Y43G, aminoacylation assay
-
?
ATP + N-o-nitrophenylsulfenyl-L-tyrosine + tRNATyr
AMP + N-o-nitrophenylsulfenyl-L-Tyr-tRNATyr + diphosphate
-
wild-type and mutant Y43G, aminoacylation assay
-
?
ATP + O-dansyl-L-tyrosine + tRNATyr
AMP + O-dansyl-L-Tyr-tRNATyr + diphosphate
-
wild-type and mutant Y43G, aminoacylation assay
-
?
ATP + O-methyl-L-tyrosine + tRNATyr
AMP + O-methyl-L-Tyr-tRNATyr + diphosphate
ATP + O-phospho-L-tyrosine + tRNATyr
AMP + O-phospho-L-Tyr-tRNATyr + diphosphate
-
wild-type and mutant Y43G, aminoacylation assay
-
?
ATP + p-acetyl-L-phenylalanine + tRNATyr
AMP + diphosphate + p-acetyl-L-phenylalanyl-tRNATyr
-
aminoacyl-tRNA synthetases are designed through a combination of homology modeling, molecular docking and binding affinity computation with the purpose of incorporating pACPhe into proteins in Escherichia coli
-
-
?
ATP + p-iodophenylalanine + tRNATyr
AMP + diphosphate + p-iodophenylalanyl-tRNATyr
-
a variant of the Methanococcus jannaschii tyrosyl synthetase that selectively incorporates para-iodophenylalanine in response to an amber stop codon is identified
-
-
?
ATP + tyrosine + tRNATyr
?
-
-
-
-
-
ATP + tyrosine + tRNATyr
AMP + Tyr-tRNATyr + diphosphate
additional information
?
-
AMP + diphosphate

ATP
-
-
-
-
AMP + diphosphate
ATP
-
-
-
-
AMP + diphosphate
ATP
-
-
-
-
AMP + diphosphate
ATP
-
-
-
-
-
AMP + diphosphate
ATP
-
-
-
-
ATP + 3-(2-naphthyl)alanine + tRNATyr

AMP + diphosphate + 3-(2-naphthyl)alanyl-tRNATyr
-
activity of a natural mutant enzyme, NpAla TyrRS activity
-
-
?
ATP + 3-(2-naphthyl)alanine + tRNATyr
AMP + diphosphate + 3-(2-naphthyl)alanyl-tRNATyr
-
activity of a natural mutant enzyme, NpAla TyrRS activity, altered specificity is due to both side-chain and backbone rearrangements within the active site that modify hydrogen bonds and packing interactions with substrate, as well as disrupt the alpha8-helix, which spans the WT active site
-
-
?
ATP + 3-azido-L-tyrosine + tRNATyr

AMP + diphosphate + 3-azido-L-tyrosyl-tRNATyr
-
-
-
-
?
ATP + 3-azido-L-tyrosine + tRNATyr
AMP + diphosphate + 3-azido-L-tyrosyl-tRNATyr
-
-
-
-
?
ATP + 3-azido-L-tyrosine + tRNATyr
AMP + diphosphate + 3-azido-L-tyrosyl-tRNATyr
-
-
-
-
?
ATP + 3-iodo-L-tyrosine + tRNATyr

AMP + diphosphate + 3-iodo-L-tyrosyl-tRNATyr
-
-
-
-
?
ATP + 3-iodo-L-tyrosine + tRNATyr
AMP + diphosphate + 3-iodo-L-tyrosyl-tRNATyr
-
-
-
-
?
ATP + 3-iodo-L-tyrosine + tRNATyr
AMP + diphosphate + 3-iodo-L-tyrosyl-tRNATyr
-
-
-
-
?
ATP + 4-acetylphenylalanine + tRNATyr

AMP + diphosphate + 4-acetylphenylalanyl-tRNATyr
-
activity of a natural mutant enzyme
-
-
?
ATP + 4-acetylphenylalanine + tRNATyr
AMP + diphosphate + 4-acetylphenylalanyl-tRNATyr
-
activity of a natural mutant enzyme, altered specificity is due to both side-chain and backbone rearrangements within the active site that modify hydrogen bonds and packing interactions with substrate, as well as disrupt the alpha8-helix, which spans the WT active site
-
-
?
ATP + 4-bromophenylalanine + tRNATyr

AMP + diphosphate + 4-bromophenylalanyl-tRNATyr
-
activity of a natural mutant enzyme, p-BrPhe TyrRS activity
-
-
?
ATP + 4-bromophenylalanine + tRNATyr
AMP + diphosphate + 4-bromophenylalanyl-tRNATyr
-
activity of a natural mutant enzyme, p-BrPhe TyrRS activity, altered specificity is due to both side-chain and backbone rearrangements within the active site that modify hydrogen bonds and packing interactions with substrate, as well as disrupt the alpha8-helix, which spans the WT active site
-
-
?
ATP + L-beta-(5-hydroxy-2-pyridyl)-alanine + tRNATyr

AMP + L-beta-(5-hydroxy-2-pyridyl)-alanine-tRNATyr + diphosphate
-
L-beta-(5-hydroxy-2-pyridyl)-alanine i.e. azatyrosine, mutant F130S, and wild-type enzyme the latter showing low activity
-
?
ATP + L-beta-(5-hydroxy-2-pyridyl)-alanine + tRNATyr
AMP + L-beta-(5-hydroxy-2-pyridyl)-alanine-tRNATyr + diphosphate
-
L-beta-(5-hydroxy-2-pyridyl)-alanine i.e. azatyrosine, mutant F130S shows 17fold higher activity in vivo than the wild-type enzyme
-
?
ATP + L-tyrosine + tRNATyr

AMP + diphosphate + L-tyrosyl-tRNATyr
-
-
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + diphosphate + L-tyrosyl-tRNATyr
the TyrRS specificity for tyrosine and conformity with the identity rules for tRNATyr for archea/eukarya, anticodon binding site, overview
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + diphosphate + L-tyrosyl-tRNATyr
functional idiosyncrasies of the viral TyrRS, activity with Escherichia coli tRNATyr, Plasmodium falciparum tRNATyr, and diverse wild-type and mutant Saccharomyces cerevisiae tRNATyrs, overview, the TyrRS specificity for tyrosine and recognition of the tRNATyr acceptor stem show conformity with the identity rules for tRNATyr for archea/eukarya, anticodon binding site, overview
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + diphosphate + L-tyrosyl-tRNATyr
-
-
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + diphosphate + L-tyrosyl-tRNATyr
-
-
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + diphosphate + L-tyrosyl-tRNATyr
-
-
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + diphosphate + L-tyrosyl-tRNATyr
-
-
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + diphosphate + L-tyrosyl-tRNATyr
-
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + diphosphate + L-tyrosyl-tRNATyr
-
-
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + diphosphate + L-tyrosyl-tRNATyr
-
-
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + diphosphate + L-tyrosyl-tRNATyr
-
-
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + diphosphate + L-tyrosyl-tRNATyr
-
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + diphosphate + L-tyrosyl-tRNATyr
-
-
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + diphosphate + L-tyrosyl-tRNATyr
-
-
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + diphosphate + L-tyrosyl-tRNATyr
-
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + diphosphate + L-tyrosyl-tRNATyr
-
-
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + diphosphate + L-tyrosyl-tRNATyr
-
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + diphosphate + L-tyrosyl-tRNATyr
-
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + diphosphate + L-tyrosyl-tRNATyr
-
-
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + diphosphate + L-tyrosyl-tRNATyr
-
-
-
-
-
ATP + L-tyrosine + tRNATyr
AMP + diphosphate + L-tyrosyl-tRNATyr
-
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + diphosphate + L-tyrosyl-tRNATyr
-
wild-type activity
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + diphosphate + L-tyrosyl-tRNATyr
-
-
-
-
ATP + L-tyrosine + tRNATyr
AMP + diphosphate + L-tyrosyl-tRNATyr
-
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + diphosphate + L-tyrosyl-tRNATyr
-
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + diphosphate + L-tyrosyl-tRNATyr
-
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + diphosphate + L-tyrosyl-tRNATyr
-
-
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + diphosphate + L-tyrosyl-tRNATyr
-
-
-
-
-
ATP + L-tyrosine + tRNATyr
AMP + diphosphate + L-tyrosyl-tRNATyr
-
-
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + diphosphate + L-tyrosyl-tRNATyr
-
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + diphosphate + L-tyrosyl-tRNATyr
-
-
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + diphosphate + L-tyrosyl-tRNATyr
identitification of determinants in the cognate tRNATyr, the tRNATyr molecule forms an L-shaped structure, the acceptor stem and anticodon loop of the tRNATyr interact with different subunits of the dimeric TyrRS molecule, overview
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + diphosphate + L-tyrosyl-tRNATyr
-
-
-
-
?
ATP + L-tyrosine + tRNATyr

AMP + L-Tyr-tRNATyr + diphosphate
-
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + L-Tyr-tRNATyr + diphosphate
-
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + L-Tyr-tRNATyr + diphosphate
-
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + L-Tyr-tRNATyr + diphosphate
-
-
-
r
ATP + L-tyrosine + tRNATyr
AMP + L-Tyr-tRNATyr + diphosphate
-
2-step reaction mechanism, 1. activation of the amino acid by MgATP2- to form an enzyme-bound aminoacyl-adenylate intermediate, 2. transfer of the amino acid to the 3'-end of its cognate tRNATyr
-
r
ATP + L-tyrosine + tRNATyr
AMP + L-Tyr-tRNATyr + diphosphate
-
2-step reaction, 1. activation of L-tyrosine with ATP to form L-Tyr-AMP, 2. transfer of the tyrosyl-group to tRNATyr
-
?
ATP + L-tyrosine + tRNATyr
AMP + L-Tyr-tRNATyr + diphosphate
the enzyme aminoacylates Escherichia coli tRNA as well as in vitro transcribed human mitochondrial tRNAs
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + L-Tyr-tRNATyr + diphosphate
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + L-Tyr-tRNATyr + diphosphate
-
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + L-Tyr-tRNATyr + diphosphate
-
wild-type and mutant Y43G, aminoacylation assay
-
?
ATP + L-tyrosine + tRNATyr(G34C)

AMP + diphosphate + L-tyrosyl-tRNATyr(G34C)
-
the enzyme strictly recognizes the C1-G72 base pair, whereas the enzyme from Thermus thermophilus recognizes the G1-C72 in a different manner using different residues
-
-
?
ATP + L-tyrosine + tRNATyr(G34C)
AMP + diphosphate + L-tyrosyl-tRNATyr(G34C)
the enzyme strictly recognizes the C1-G72 base pair, whereas the enzyme from Thermus thermophilus recognizes the G1-C72 in a different manner using different residues
-
-
?
ATP + L-tyrosine + tRNATyr(wild-type)

AMP + diphosphate + L-tyrosyl-tRNATyr(wild-type)
-
the enzyme strictly recognizes the C1-G72 base pair, whereas the enzyme from Thermus thermophilus recognizes the G1-C72 in a different manner using different residues
-
-
?
ATP + L-tyrosine + tRNATyr(wild-type)
AMP + diphosphate + L-tyrosyl-tRNATyr(wild-type)
the enzyme strictly recognizes the C1-G72 base pair, whereas the enzyme from Thermus thermophilus recognizes the G1-C72 in a different manner using different residues
-
-
?
ATP + O-methyl-L-tyrosine + tRNATyr

AMP + O-methyl-L-Tyr-tRNATyr + diphosphate
-
-
?
ATP + O-methyl-L-tyrosine + tRNATyr
AMP + O-methyl-L-Tyr-tRNATyr + diphosphate
-
wild-type and mutant Y43G, aminoacylation assay
-
?
ATP + tyrosine + tRNATyr

AMP + Tyr-tRNATyr + diphosphate
-
-
-
?
ATP + tyrosine + tRNATyr
AMP + Tyr-tRNATyr + diphosphate
-
K2ATP2- or Na2ATP2-
-
-
-
ATP + tyrosine + tRNATyr
AMP + Tyr-tRNATyr + diphosphate
-
-
-
-
-
ATP + tyrosine + tRNATyr
AMP + Tyr-tRNATyr + diphosphate
-
-
-
?
ATP + tyrosine + tRNATyr
AMP + Tyr-tRNATyr + diphosphate
-
r
-
-
ATP + tyrosine + tRNATyr
AMP + Tyr-tRNATyr + diphosphate
-
same affinity for tRNA or tRNA acylated with tyrosine
-
-
-
ATP + tyrosine + tRNATyr
AMP + Tyr-tRNATyr + diphosphate
-
-
-
?
ATP + tyrosine + tRNATyr
AMP + Tyr-tRNATyr + diphosphate
-
-
-
?
ATP + tyrosine + tRNATyr
AMP + Tyr-tRNATyr + diphosphate
-
-
-
r
ATP + tyrosine + tRNATyr
AMP + Tyr-tRNATyr + diphosphate
-
-
-
r
ATP + tyrosine + tRNATyr
AMP + Tyr-tRNATyr + diphosphate
-
Na2ATP2-, specific for tyrosine as amino acid
-
-
-
ATP + tyrosine + tRNATyr
AMP + Tyr-tRNATyr + diphosphate
-
phosphorothioate analogs of ATP
-
-
-
ATP + tyrosine + tRNATyr
AMP + Tyr-tRNATyr + diphosphate
-
2-step reaction mechanism, 1. activation of the amino acid by MgATP2- to form an enzyme-bound aminoacyl-adenylate intermediate, 2. transfer of the amino acid to the 3'-end of its cognate tRNATyr
-
r
ATP + tyrosine + tRNATyr
AMP + Tyr-tRNATyr + diphosphate
-
2-step reaction: 1. tyrosine activation to form the tyrosinyl-adenylate intermediate, 2. transfer of tyrosine from the tyrosinyl-adenylate intermediate to the tRNATyr
-
r
ATP + tyrosine + tRNATyr
AMP + Tyr-tRNATyr + diphosphate
-
extreme high fidelity in charging the tRNA with an amino acid
-
?
ATP + tyrosine + tRNATyr
AMP + Tyr-tRNATyr + diphosphate
-
tRNATyr substrate from Escherichia coli
-
?
ATP + tyrosine + tRNATyr
AMP + Tyr-tRNATyr + diphosphate
-
enzyme plays a key role in protein biosynthesis
-
?
ATP + tyrosine + tRNATyr
AMP + Tyr-tRNATyr + diphosphate
-
-
-
-
-
ATP + tyrosine + tRNATyr
AMP + Tyr-tRNATyr + diphosphate
-
-
-
?
ATP + tyrosine + tRNATyr
AMP + Tyr-tRNATyr + diphosphate
-
-
-
r
ATP + tyrosine + tRNATyr
AMP + Tyr-tRNATyr + diphosphate
-
-
-
-
ATP + tyrosine + tRNATyr
AMP + Tyr-tRNATyr + diphosphate
-
-
-
-
-
ATP + tyrosine + tRNATyr
AMP + Tyr-tRNATyr + diphosphate
-
-
-
?
ATP + tyrosine + tRNATyr
AMP + Tyr-tRNATyr + diphosphate
-
specificity for amino acids, with regard to the specificity for ATP the hydroxy group of ribose and the amino group in position 6 of the base are essential
-
-
-
ATP + tyrosine + tRNATyr
AMP + Tyr-tRNATyr + diphosphate
-
heterologous tRNATyr from Escherichia coli and Methanococcus jannashii, tyrosylation efficiency of tRNA variants: determinants are base pair C1-G72, discriminator residue A73, and the 3 anticodon bases G34, U35, and A36
-
?
ATP + tyrosine + tRNATyr
AMP + Tyr-tRNATyr + diphosphate
-
-
-
?
ATP + tyrosine + tRNATyr
AMP + Tyr-tRNATyr + diphosphate
-
-
-
?
ATP + tyrosine + tRNATyr
AMP + Tyr-tRNATyr + diphosphate
-
extreme high fidelity in charging the tRNA with an amino acid
-
?
ATP + tyrosine + tRNATyr
AMP + Tyr-tRNATyr + diphosphate
-
enzyme plays a key role in protein biosynthesis
-
?
ATP + tyrosine + tRNATyr
AMP + Tyr-tRNATyr + diphosphate
-
-
-
?
ATP + tyrosine + tRNATyr
AMP + Tyr-tRNATyr + diphosphate
-
tRNATyr structure requirements, the C-terminal domain has a crucial role in the recognition of tRNATyr, first by recognizing the tRNA's unique shape and secondly by participating in specific interactions with one of the anticodon bases
-
?
ATP + tyrosine + tRNATyr
AMP + Tyr-tRNATyr + diphosphate
-
-
-
?
ATP + tyrosine + tRNATyr
AMP + Tyr-tRNATyr + diphosphate
-
tRNATyr structure requirements, the C-terminal domain has a crucial role in the recognition of tRNATyr, first by recognizing the tRNA's unique shape and secondly by participating in specific interactions with one of the anticodon bases
-
?
additional information

?
-
mimivirus aminoacyl-tRNA synthetases function as regular translation enzymes in infected amoebas
-
-
-
additional information
?
-
-
no activity with 4-azido-L-phenylalanine, 4-amino-L-phenylalanine, 4-nitro-L-phenylalanine, 4-methyl-L-phenylalanine, 4-fluoro-L-phenylalanine, 4-chloro-L-phenylalanine, 4-bromo-L-phenylalanine
-
-
-
additional information
?
-
-
conformational flexibility of cytokine-like C-module of the enzyme
-
-
-
additional information
?
-
-
the presence of the C-terminal EMAP II-domain has no effect on the recognition of cognate Tyr and discrimination against noncognate Phe
-
-
-
additional information
?
-
the presence of the C-terminal EMAP II-domain has no effect on the recognition of cognate Tyr and discrimination against noncognate Phe
-
-
-
additional information
?
-
-
residues Asp81, Tyr175, Gln179, and Gln201 coordinate the ammonium group of the L-Tyr ligand
-
-
-
additional information
?
-
-
the enzyme's C-terminal domain, an EMAP II-like protein, is active in angiogenesis pathways and stimulates immune cells, when cleaved off the enzyme, it stimulates blood vessel development
-
?
additional information
?
-
-
TyrRS deficiency is involved in the autosomal dominant intermediate Charcot-Marie-Tooth neuropathy type C disorder, overview
-
-
-
additional information
?
-
-
recombinant hTyrRS also synthesizes kyotorphin from tyrosine, arginine, and ATP, cf. EC 6.3.2.24
-
-
-
additional information
?
-
-
two distinct conformational states of the active site in the three Leishmania major TyrRS structures
-
-
-
additional information
?
-
-
high degree of structural plasticity that is observed in these aminoacyl-tRNA synthetases, overview
-
-
-
additional information
?
-
enzyme TyrRS has a detectable, natural, tRNA-acylation activity for the D-tyrosine stereoisomer, being capable of charging D-Tyr onto tRNATyr to form D-Tyr-tRNA instead of the usual L-Tyr-tRNA
-
-
-
additional information
?
-
enzyme TyrRS has a detectable, natural, tRNA-acylation activity for the D-tyrosine stereoisomer, being capable of charging D-Tyr onto tRNATyr to form D-Tyr-tRNA instead of the usual L-Tyr-tRNA
-
-
-
additional information
?
-
-
enzyme MtTyrRS is incapable of cross-recognition and aminoacylation of human cytoplasmic tRNATyr
-
-
-
additional information
?
-
enzyme MtTyrRS is incapable of cross-recognition and aminoacylation of human cytoplasmic tRNATyr
-
-
-
additional information
?
-
enzyme MtTyrRS is incapable of cross-recognition and aminoacylation of human cytoplasmic tRNATyr
-
-
-
additional information
?
-
-
CYT-18 protein is a tyrosyl-tRNA synthetase adapted to function in group I intron splicing by acquiring a new RNA binding surface
-
-
-
additional information
?
-
-
no activity with tRNAAsp and tRNAPhe
-
?
additional information
?
-
the lack of cross-reactivity between archaeal/eukaryotic and bacterial TyrRS-tRNATyr pairs most probably lies in the different sequence of the last base pair of the acceptor stem, C1-G72 vs G1-C72, of tRNATyr, the recognition mode of Tyr-AMP is conserved among the TyrRSs from the three kingdoms, overview
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-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ATP + 3-(2-naphthyl)alanine + tRNATyr
AMP + diphosphate + 3-(2-naphthyl)alanyl-tRNATyr
-
activity of a natural mutant enzyme, NpAla TyrRS activity
-
-
?
ATP + 4-acetylphenylalanine + tRNATyr
AMP + diphosphate + 4-acetylphenylalanyl-tRNATyr
-
activity of a natural mutant enzyme
-
-
?
ATP + 4-bromophenylalanine + tRNATyr
AMP + diphosphate + 4-bromophenylalanyl-tRNATyr
-
activity of a natural mutant enzyme, p-BrPhe TyrRS activity
-
-
?
ATP + L-beta-(5-hydroxy-2-pyridyl)-alanine + tRNATyr
AMP + L-beta-(5-hydroxy-2-pyridyl)-alanine-tRNATyr + diphosphate
-
L-beta-(5-hydroxy-2-pyridyl)-alanine i.e. azatyrosine, mutant F130S shows 17fold higher activity in vivo than the wild-type enzyme
-
?
ATP + L-tyrosine + tRNATyr
AMP + diphosphate + L-tyrosyl-tRNATyr
ATP + L-tyrosine + tRNATyr
AMP + L-Tyr-tRNATyr + diphosphate
ATP + tyrosine + tRNATyr
?
-
-
-
-
-
ATP + tyrosine + tRNATyr
AMP + Tyr-tRNATyr + diphosphate
additional information
?
-
ATP + L-tyrosine + tRNATyr

AMP + diphosphate + L-tyrosyl-tRNATyr
-
-
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + diphosphate + L-tyrosyl-tRNATyr
the TyrRS specificity for tyrosine and conformity with the identity rules for tRNATyr for archea/eukarya, anticodon binding site, overview
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + diphosphate + L-tyrosyl-tRNATyr
-
-
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + diphosphate + L-tyrosyl-tRNATyr
-
-
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + diphosphate + L-tyrosyl-tRNATyr
-
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + diphosphate + L-tyrosyl-tRNATyr
-
-
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + diphosphate + L-tyrosyl-tRNATyr
-
-
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + diphosphate + L-tyrosyl-tRNATyr
-
-
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + diphosphate + L-tyrosyl-tRNATyr
-
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + diphosphate + L-tyrosyl-tRNATyr
-
-
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + diphosphate + L-tyrosyl-tRNATyr
-
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + diphosphate + L-tyrosyl-tRNATyr
-
-
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + diphosphate + L-tyrosyl-tRNATyr
-
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + diphosphate + L-tyrosyl-tRNATyr
-
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + diphosphate + L-tyrosyl-tRNATyr
-
-
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + diphosphate + L-tyrosyl-tRNATyr
-
-
-
-
-
ATP + L-tyrosine + tRNATyr
AMP + diphosphate + L-tyrosyl-tRNATyr
-
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + diphosphate + L-tyrosyl-tRNATyr
-
wild-type activity
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + diphosphate + L-tyrosyl-tRNATyr
-
-
-
-
ATP + L-tyrosine + tRNATyr
AMP + diphosphate + L-tyrosyl-tRNATyr
-
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + diphosphate + L-tyrosyl-tRNATyr
-
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + diphosphate + L-tyrosyl-tRNATyr
-
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + diphosphate + L-tyrosyl-tRNATyr
-
-
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + diphosphate + L-tyrosyl-tRNATyr
-
-
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + diphosphate + L-tyrosyl-tRNATyr
-
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + diphosphate + L-tyrosyl-tRNATyr
-
-
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + diphosphate + L-tyrosyl-tRNATyr
-
-
-
-
?
ATP + L-tyrosine + tRNATyr

AMP + L-Tyr-tRNATyr + diphosphate
-
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + L-Tyr-tRNATyr + diphosphate
-
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + L-Tyr-tRNATyr + diphosphate
-
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + L-Tyr-tRNATyr + diphosphate
-
-
-
r
ATP + L-tyrosine + tRNATyr
AMP + L-Tyr-tRNATyr + diphosphate
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + L-Tyr-tRNATyr + diphosphate
-
-
-
?
ATP + tyrosine + tRNATyr

AMP + Tyr-tRNATyr + diphosphate
-
-
-
?
ATP + tyrosine + tRNATyr
AMP + Tyr-tRNATyr + diphosphate
-
-
-
?
ATP + tyrosine + tRNATyr
AMP + Tyr-tRNATyr + diphosphate
-
-
-
?
ATP + tyrosine + tRNATyr
AMP + Tyr-tRNATyr + diphosphate
-
-
-
?
ATP + tyrosine + tRNATyr
AMP + Tyr-tRNATyr + diphosphate
-
-
-
r
ATP + tyrosine + tRNATyr
AMP + Tyr-tRNATyr + diphosphate
-
-
-
r
ATP + tyrosine + tRNATyr
AMP + Tyr-tRNATyr + diphosphate
-
enzyme plays a key role in protein biosynthesis
-
?
ATP + tyrosine + tRNATyr
AMP + Tyr-tRNATyr + diphosphate
-
-
-
?
ATP + tyrosine + tRNATyr
AMP + Tyr-tRNATyr + diphosphate
-
-
-
r
ATP + tyrosine + tRNATyr
AMP + Tyr-tRNATyr + diphosphate
-
-
-
?
ATP + tyrosine + tRNATyr
AMP + Tyr-tRNATyr + diphosphate
-
-
-
?
ATP + tyrosine + tRNATyr
AMP + Tyr-tRNATyr + diphosphate
-
-
-
?
ATP + tyrosine + tRNATyr
AMP + Tyr-tRNATyr + diphosphate
-
enzyme plays a key role in protein biosynthesis
-
?
ATP + tyrosine + tRNATyr
AMP + Tyr-tRNATyr + diphosphate
-
-
-
?
ATP + tyrosine + tRNATyr
AMP + Tyr-tRNATyr + diphosphate
-
-
-
?
additional information

?
-
mimivirus aminoacyl-tRNA synthetases function as regular translation enzymes in infected amoebas
-
-
-
additional information
?
-
-
the enzyme's C-terminal domain, an EMAP II-like protein, is active in angiogenesis pathways and stimulates immune cells, when cleaved off the enzyme, it stimulates blood vessel development
-
?
additional information
?
-
-
TyrRS deficiency is involved in the autosomal dominant intermediate Charcot-Marie-Tooth neuropathy type C disorder, overview
-
-
-
additional information
?
-
-
enzyme MtTyrRS is incapable of cross-recognition and aminoacylation of human cytoplasmic tRNATyr
-
-
-
additional information
?
-
enzyme MtTyrRS is incapable of cross-recognition and aminoacylation of human cytoplasmic tRNATyr
-
-
-
additional information
?
-
enzyme MtTyrRS is incapable of cross-recognition and aminoacylation of human cytoplasmic tRNATyr
-
-
-
additional information
?
-
-
CYT-18 protein is a tyrosyl-tRNA synthetase adapted to function in group I intron splicing by acquiring a new RNA binding surface
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
1-[4-[([4-[(naphthalen-1-yl)methyl]-5-oxo-2,5-dihydrothiophen-3-yl]oxy)carbonyl]phenyl]dibroman-1-ium
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3-(3,4-dichlorophenyl)-4-(2-(4-methylpiperazin-1-yl)ethoxy)furan-2(5H)-one
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3-(3,4-difluorophenyl)-4-(2-(piperidin-1-yl)ethoxy)furan-2(5H)-one
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-
3-(3,4-dimethoxyphenyl)-4-(2-(4-methylpiperazin-1-yl)ethoxy)furan-2(5H)-one
-
-
3-(3,4-dimethoxyphenyl)-4-(2-(piperidin-1-yl)ethoxy)furan-2(5H)-one
-
-
3-(3-bromophenyl)-4-(2-morpholinoethoxy)furan-2(5H)-one
-
-
3-(3-chlorophenyl)-4-(2-morpholinoethoxy)furan-2(5H)-one
-
-
3-(3-hydroxyphenyl)-4-(2-morpholinoethoxy)furan-2(5H)-one
-
-
3-(3-methoxyphenyl)-4-(2-morpholinoethoxy)furan-2(5H)-one
-
-
3-(4-bromophenyl)-4-(2-morpholinoethoxy)furan-2(5H)-one
-
-
3-(4-chlorophenyl)-4-(2-morpholinoethoxy)furan-2(5H)-one
-
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3-(4-hydroxyphenyl)-4-(2-morpholinoethoxy)furan-2(5H)-one
-
replacement of the morpholine-ring in the side chain of the compound with a substituent containing more hydrophilic groups is probably more suitable for further modification. Most potent agent against Staphylococcus aureus ATCC 25923 with MIC50 value of 0.00023 mg/ml
3-(4-methoxyphenyl)-4-(2-morpholinoethoxy)furan-2(5H)-one
-
-
3-phenyl-4-(2-(piperidin-1-yl)ethoxy)furan-2(5H)-one
-
-
3-phenyl-4-(2-(propylamino)ethoxy)furan-2(5H)-one
-
-
3-phenyl-4-(2-(pyrrolidin-1-yl)ethoxy)furan-2(5H)-one
-
-
3-phenyl-4-(phenylamino)furan-2(5H)-one
-
-
4-(2-(2,4-dichlorophenylformyloxy)ethoxy)-3-phenylfuran-2(5H)-one
-
-
4-(2-(2,4-dihydroxyphenylformyloxy)ethoxy)-3-phenylfuran-2(5H)-one
-
-
4-(2-(2,5-dichlorophenylformyloxy)ethoxy)-3-phenylfuran-2(5H)-one
-
-
4-(2-(2-(4-nitrophenyl)hydrazinyl)ethoxy)-3-phenylfuran-2(5H)-one
-
-
4-(2-(2-chlorophenylformyloxy)ethoxy)-3-phenylfuran-2(5H)-one
-
-
4-(2-(2-hydroxyphenylformyloxyl)ethoxy)-3-phenylfuran-2(5H)-one
-
-
4-(2-(2-methoxyphenylformyloxy)ethoxy)-3-phenylfuran-2(5H)-one
-
-
4-(2-(2-methylphenylformyloxy)ethoxy)-3-phenylfuran-2(5H)-one
-
-
4-(2-(2-nitrophenylformyloxyl)ethoxy)-3-phenylfuran-2(5H)-one
-
-
4-(2-(3,4-dichlorophenylformyloxy)ethoxy)-3-phenylfuran-2(5H)-one
-
-
4-(2-(3,4-dihydroxyphenylformyloxy)ethoxy)-3-phenylfuran-2(5H)-one
-
-
4-(2-(3,4-dimethoxyphenylacetyloxy)ethoxy)-3-phenylfuran-2(5H)-one
-
-
4-(2-(3,5-dihydroxyphenylformyloxy)ethoxy)-3-phenylfuran-2(5H)-one
-
-
4-(2-(3-bromophenylacetyloxy)ethoxy)-3-(4-chlorophenyl)furan-2(5H)-one
-
-
4-(2-(3-chlorophenylacetyloxy)ethoxy)-3-(4-chlorophenyl)furan-2(5H)-one
-
-
4-(2-(3-chlorophenylacetyloxy)ethoxy)-3-phenylfuran-2(5H)-one
-
-
4-(2-(3-chlorophenylformyloxy)ethoxy)-3-(4-chlorophenyl)furan-2(5H)-one
-
-
4-(2-(3-methylphenylformyloxy)ethoxy)-3-phenylfuran-2(5H)-one
-
-
4-(2-(3-nitrophenylformyloxy)ethoxy)-3-phenylfuran-2(5H)-one
-
-
4-(2-(3-pyridylformyloxy)ethoxy)-3-phenylfuran-2(5H)-one
-
-
4-(2-(3-trifluoromethylphenylformyoxy)ethoxy)-3-phenylfuran-2(5H)-one
-
-
4-(2-(4-bromophenylacetyloxy)ethoxy)-3-(4-chlorophenyl)furan-2(5H)-one
-
-
4-(2-(4-bromophenylacetyloxy)ethoxy)-3-phenylfuran-2(5H)-one
-
-
4-(2-(4-chlorophenylacetyloxy)ethoxy)-3-(4-chlorophenyl)furan-2(5H)-one
-
-
4-(2-(4-chlorophenylformyloxy)ethoxy)-3-phenylfuran-2(5H)-one
-
-
4-(2-(4-fluorophenylacetyloxy)ethoxy)-3-(4-chlorophenyl)furan-2(5H)-one
-
-
4-(2-(4-fluorophenylacetyloxy)ethoxy)-3-phenylfuran-2(5H)-one
-
-
4-(2-(4-fluorophenylformyloxy)ethoxy)-3-phenylfuran-2(5H)-one
-
-
4-(2-(4-hydroxyphenylacetyloxy)ethoxy)-3-(4-chlorophenyl)furan-2(5H)-one
-
-
4-(2-(4-hydroxyphenylacetyloxy)ethoxy)-3-phenylfuran-2(5H)-one
-
-
4-(2-(4-hydroxyphenylformyloxy)ethoxy)-3-phenylfuran-2(5H)-one
-
-
4-(2-(4-methylphenylformyloxy)ethoxy)-3-phenylfuran-2(5H)-one
-
-
4-(2-(4-methylpiperazin-1-yl)ethoxy)-3-phenylfuran-2(5H)-one
-
-
4-(2-(4-nitrophenylformyloxy)ethoxy)-3-phenylfuran-2(5H)-one
-
-
4-(2-(6-hydroxynaphthalen-2-ylformyloxy)ethoxy)-3-phenylfuran-2(5H)-one
-
-
4-(2-(benzylamino)ethoxy)-3-phenylfuran-2(5H)-one
-
-
4-(2-(butylamino)ethoxy)-3-phenylfuran-2(5H)-one
-
-
4-(2-(cyclohexylamino)ethoxy)-3-(3,4-dimethoxyphenyl)furan-2(5H)-one
-
-
4-(2-(cyclohexylamino)ethoxy)-3-phenylfuran-2(5H)-one
-
-
4-(2-(naphthalen-2-ylformyloxy)ethoxy)-3-phenylfuran-2(5H)-one
-
-
4-(2-butyryloxyethoxy)-3-phenylfuran-2(5H)-one
-
-
4-(2-hexanoyloxyethoxy)-3-phenylfuran-2(5H)-one
-
-
4-(2-morpholinoethoxy)-3-phenylfuran-2(5H)-one
-
-
4-(2-octanoyloxyethoxy)-3-phenylfuran-2(5H)-one
-
-
4-(2-phenylacetyloxylethoxy)-3-phenylfuran-2(5H)-one
-
-
4-[(naphthalen-1-yl)methyl]-5-oxo-2,5-dihydrothiophen-3-yl 2-bromobenzoate
-
-
4-[(naphthalen-1-yl)methyl]-5-oxo-2,5-dihydrothiophen-3-yl 2-chlorobenzoate
-
-
4-[(naphthalen-1-yl)methyl]-5-oxo-2,5-dihydrothiophen-3-yl 2-chloropyridine-3-carboxylate
-
-
4-[(naphthalen-1-yl)methyl]-5-oxo-2,5-dihydrothiophen-3-yl 2-fluorobenzoate
-
-
4-[(naphthalen-1-yl)methyl]-5-oxo-2,5-dihydrothiophen-3-yl 2-methoxybenzoate
-
-
4-[(naphthalen-1-yl)methyl]-5-oxo-2,5-dihydrothiophen-3-yl 2-methylbenzoate
-
-
4-[(naphthalen-1-yl)methyl]-5-oxo-2,5-dihydrothiophen-3-yl 2-nitrobenzoate
-
-
4-[(naphthalen-1-yl)methyl]-5-oxo-2,5-dihydrothiophen-3-yl 3-(3-methylphenyl)propanoate
-
-
4-[(naphthalen-1-yl)methyl]-5-oxo-2,5-dihydrothiophen-3-yl 3-(4-methylphenyl)propanoate
-
-
4-[(naphthalen-1-yl)methyl]-5-oxo-2,5-dihydrothiophen-3-yl 3-aminobenzoate
-
-
4-[(naphthalen-1-yl)methyl]-5-oxo-2,5-dihydrothiophen-3-yl 3-bromobenzoate
-
-
4-[(naphthalen-1-yl)methyl]-5-oxo-2,5-dihydrothiophen-3-yl 3-chlorobenzoate
-
-
4-[(naphthalen-1-yl)methyl]-5-oxo-2,5-dihydrothiophen-3-yl 3-fluorobenzoate
-
-
4-[(naphthalen-1-yl)methyl]-5-oxo-2,5-dihydrothiophen-3-yl 3-hydroxybenzoate
-
-
4-[(naphthalen-1-yl)methyl]-5-oxo-2,5-dihydrothiophen-3-yl 3-methylbenzoate
-
-
4-[(naphthalen-1-yl)methyl]-5-oxo-2,5-dihydrothiophen-3-yl 3-phenylpropanoate
-
-
4-[(naphthalen-1-yl)methyl]-5-oxo-2,5-dihydrothiophen-3-yl 4-aminobenzoate
-
-
4-[(naphthalen-1-yl)methyl]-5-oxo-2,5-dihydrothiophen-3-yl 4-chlorobenzoate
-
-
4-[(naphthalen-1-yl)methyl]-5-oxo-2,5-dihydrothiophen-3-yl 4-fluorobenzoate
-
-
4-[(naphthalen-1-yl)methyl]-5-oxo-2,5-dihydrothiophen-3-yl 4-hydroxybenzoate
-
-
4-[(naphthalen-1-yl)methyl]-5-oxo-2,5-dihydrothiophen-3-yl 4-methylbenzoate
-
-
4-[(naphthalen-1-yl)methyl]-5-oxo-2,5-dihydrothiophen-3-yl 6-chloropyridine-3-carboxylate
-
-
4-[(naphthalen-1-yl)methyl]-5-oxo-2,5-dihydrothiophen-3-yl 6-hydroxypyridine-3-carboxylate
-
-
4-[(naphthalen-1-yl)methyl]-5-oxo-2,5-dihydrothiophen-3-yl benzoate
-
-
4-[(naphthalen-1-yl)methyl]-5-oxo-2,5-dihydrothiophen-3-yl pyridine-3-carboxylate
-
-
4-[(naphthalen-1-yl)methyl]-5-oxo-2,5-dihydrothiophen-3-yl pyridine-4-carboxylate
-
-
5'-O-[N-(L-tyrosyl)sulfamoyl]adenosine
-
i.e. TyrSA, a tyrosyl adenylate analogue,. TyrSA is engaged in many interactions with active site residues occupying the tyrosine and adenine binding pockets. Residues making hydrogen bonds with the TyrSA tyrosyl group in the tyrosine binding pocket (YBP) are Y36, Y163, Q167, D170 and Q185. Residues G38, A72 and F75 are responsible for the hydrophobic interactions between enzyme and tyrosine moiety in the YBP
6-Aminomethyladenosine triphosphate
-
-
epigallocatechin gallate
-
strong inhibition
kaempferide
-
strong inhibition
L-tyrosinyl 1,4-anhydro-D-ribitol-5-O-phosphate
L-tyrosinyl 1-beta-naphthyl-1,4-anhydro-D-ribitol-5-O-phosphate
L-tyrosinyl N6-benzoyl adenylate
-
-
L-tyrosinyl uridine-5'-O-phosphate
L-tyrosinyl-2',3'-O-isopropylidene adenylate
L-tyrosinyl-2'-deoxy adenylate
L-tyrosinyl-3'-deoxy adenylate
N-(2-chlorophenyl)-N2-(phenylacetyl)glycinamide
-
-
N-(3,5-dichlorophenyl)-N2-(phenylacetyl)glycinamide
-
-
N-(3,5-difluorophenyl)-N2-(phenylacetyl)glycinamide
-
-
N-(3,5-dimethoxyphenyl)-N2-(phenylacetyl)glycinamide
-
-
N-(3-chlorophenyl)-N2-(phenylacetyl)glycinamide
-
-
N-(3-nitrophenyl)-N2-(phenylacetyl)glycinamide
-
-
N-(4-bromophenyl)-N2-(phenylacetyl)glycinamide
-
-
N-(4-bromophenyl)-N2-[(2-chlorophenyl)acetyl]glycinamide
-
-
N-(4-bromophenyl)-N2-[(3-bromophenyl)acetyl]glycinamide
-
-
N-(4-bromophenyl)-N2-[(3-chlorophenyl)acetyl]glycinamide
-
-
N-(4-chlorophenyl)-N2-(phenylacetyl)glycinamide
-
-
N-(4-methoxyphenyl)-N2-(phenylacetyl)glycinamide
-
-
N-(4-nitrophenyl)-N2-(phenylacetyl)glycinamide
-
-
N-phenyl-N2-(phenylacetyl)glycinamide
-
-
N2-[(2-chlorophenyl)acetyl]-N-(4-methoxyphenyl)glycinamide
-
-
N2-[(2-chlorophenyl)acetyl]-N-(4-nitrophenyl)glycinamide
-
-
N2-[(2-hydroxyphenyl)acetyl]-N-(4-methoxyphenyl)glycinamide
-
-
N2-[(3,4-dimethoxyphenyl)acetyl]-N-(4-methoxyphenyl)glycinamide
-
-
N2-[(3,4-dimethoxyphenyl)acetyl]-N-(4-nitrophenyl)glycinamide
-
-
N2-[(3-chlorophenyl)acetyl]-N-(4-methoxyphenyl)glycinamide
-
-
N2-[(3-chlorophenyl)acetyl]-N-(4-methylphenyl)glycinamide
-
-
N2-[(3-chlorophenyl)acetyl]-N-(4-nitrophenyl)glycinamide
-
-
N2-[(3-fluorophenyl)acetyl]-N-(4-methoxyphenyl)glycinamide
-
-
N2-[(3-fluorophenyl)acetyl]-N-(4-nitrophenyl)glycinamide
-
-
N2-[(3-hydroxyphenyl)acetyl]-N-(4-methoxyphenyl)glycinamide
-
-
N2-[(3-hydroxyphenyl)acetyl]-N-(4-nitrophenyl)glycinamide
-
-
N2-[(4-chlorophenyl)acetyl]-N-(3,5-dichlorophenyl)glycinamide
-
-
N2-[(4-chlorophenyl)acetyl]-N-(4-methoxyphenyl)glycinamide
-
-
N2-[(4-fluorophenyl)acetyl]-N-(4-methoxyphenyl)glycinamide
-
-
N2-[(4-fluorophenyl)acetyl]-N-(4-nitrophenyl)glycinamide
-
-
N2-[(4-hydroxyphenyl)acetyl]-N-(4-methoxyphenyl)glycinamide
-
-
N2-[(4-hydroxyphenyl)acetyl]-N-(4-nitrophenyl)glycinamide
-
-
N2-[(4-methylphenyl)acetyl]-N-(4-nitrophenyl)glycinamide
-
-
O-(adenosine-5'-O-yl) N-(L-tyrosyl)phosphoramidate
i.e. Tyr-AMPN, a non-hydrolyzable Tyr-AMP analog, binding structure, overview
resveratrol
inhibits the enzyme activity and the growth of promastigotes
tyrosinol
-
binding structure, overview
tyrosyl aryl dipeptides
-
inhibitor interacts with and occupies the key catalytic residues in the tyrosyl binding pocket of the catalytic site
acacetin

-
strong inhibition
acacetin
strong inhibition
acacetin
-
strong inhibition
AMP

-
inhibition is weakened by chloride
AMP
-
inhibition is weakened by chloride
chloride

-
inhibition in presence of 1 mM free Mg2+, no inhibition in presence of 10 mM free Mg2+
chloride
-
inhibition in presence of 1 mM free Mg2+, no inhibition in presence of 10 mM free Mg2+
chrysin

-
strong inhibition
chrysin
strong inhibition
chrysin
-
strong inhibition
diphosphate

-
inhibition is strengthened by chloride
diphosphate
-
inhibition is strengthened by chloride
fisetin

-
-
fisetin
inhibits the enzyme activity and the growth of promastigotes
fisetin
-
binding structure, overview
L-tyrosinyl 1,4-anhydro-D-ribitol-5-O-phosphate

-
-
L-tyrosinyl 1,4-anhydro-D-ribitol-5-O-phosphate
-
-
L-tyrosinyl 1-beta-naphthyl-1,4-anhydro-D-ribitol-5-O-phosphate

-
-
L-tyrosinyl 1-beta-naphthyl-1,4-anhydro-D-ribitol-5-O-phosphate
-
-
L-tyrosinyl uridine-5'-O-phosphate

-
25% inhibition at 0.1 mM
L-tyrosinyl uridine-5'-O-phosphate
-
-
L-tyrosinyl-2',3'-O-isopropylidene adenylate

-
-
L-tyrosinyl-2',3'-O-isopropylidene adenylate
-
-
L-tyrosinyl-2'-deoxy adenylate

-
-
L-tyrosinyl-2'-deoxy adenylate
-
-
L-tyrosinyl-3'-deoxy adenylate

-
-
L-tyrosinyl-3'-deoxy adenylate
-
-
PCMB

-
-
sulfate

-
inhibition in presence of 1 mM free Mg2+
sulfate
-
inhibition in presence of 1 mM free Mg2+
tyrosinyl adenylate

-
-
additional information

-
no inhibition by acetate up to 200 mM in presence of 1 mM free Mg2+
-
additional information
-
natural compounds as inhibitors of tyrosyl-tRNA synthetase, effects of various polyphenols, alkaloids, and terpenes-secondary metabolites produced by higher plants, overview. Most of them act as competitive inhibitors. Structure-activity relationship shows that the most potent flavonoid inhibitors contain hydroxyl group at position 5 and 7 of A ring and a -OCH3 group at position 4' of B ring
-
additional information
-
LdTyrRS specific nanobodies are generated in Lama glama. Nanobodies are the variable domains of camelid heavy chain-only antibodies. The nanobody NbA makes numerous crystal contacts and in addition reduces the flexibility of a loop of LdTyrRS. NbA is cloned in the pMESy4 vector that carries the pelB sequence coding for the secretion signal peptide of PelB and is expressed as His-tagged protein in Escherichia coli for subsequent purification from the bacterial periplasm by affinity chromatography and gel filtration. 4 anti-LdTyrRS nanobodies are tested as crystallization chaperones, crystallization and structure analysis and modeling, overview
-
additional information
-
natural compounds as inhibitors of tyrosyl-tRNA synthetase, effects of various polyphenols, alkaloids, and terpenes-secondary metabolites produced by higher plants, overview. Most of them act as competitive inhibitors. Structure-activity relationship shows that the most potent flavonoid inhibitors contain hydroxyl group at position 5 and 7 of A ring and a -OCH3 group at position 4' of B ring
-
additional information
natural compounds as inhibitors of tyrosyl-tRNA synthetase, effects of various polyphenols, alkaloids, and terpenes-secondary metabolites produced by higher plants, overview. Most of them act as competitive inhibitors. Structure-activity relationship shows that the most potent flavonoid inhibitors contain hydroxyl group at position 5 and 7 of A ring and a -OCH3 group at position 4' of B ring
-
additional information
-
no inhibition by L-tyrosinyl 1-beta-(E)-(3-ethoxycarbonyl-2-methylprop-2-enyl)-1,4-anhydro-D-ribitol-5-O-phosphate, N-(L-tyrosinyl)-N'-(5'-deoxy-5'-adenosinyl)-sulfamide, and 2(S)-amino-3-(4-hydroxyphenyl)propyl 1-(adenine-9-yl)-(E)-5,6-dideoxy-beta-D-ribohept-5-enfuranuronate hydrochloride
-
additional information
-
enzyme-inhibitor complexes
-
additional information
-
synthesis of a series of novel 4-alkoxy-3-arylfuran-2(5H)-ones as tyrosyl-tRNA synthetase inhibitors, binding model and structure-activity relationship, MIC50 values, overview
-
additional information
-
synthesis and evaluation of new tyrosyl-tRNA synthetase inhibitors as antibacterial agents based on a N2-(arylacetyl)glycinanilide scaffold, molecular docking study, antimicrobial activity, overview
-
additional information
-
synthesis and evaluation of a series of novel 4-hydroxy-3-(naphthalen-1-ylmethyl)thiophen-2(5H)-ones as tyrosyl-tRNA synthetase inhibitors, molecular docking, structure-activity relationships, overview
-
additional information
-
natural compounds as inhibitors of tyrosyl-tRNA synthetase, effects of various polyphenols, alkaloids, and terpenes-secondary metabolites produced by higher plants, overview. Most of them act as competitive inhibitors. Structure-activity relationship shows that the most potent flavonoid inhibitors contain hydroxyl group at position 5 and 7 of A ring and a -OCH3 group at position 4' of B ring
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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2.04 - 2.43
3-chloro-L-tyrosine
0.625 - 1.3
3-fluoro-D,L-tyrosine
0.13 - 1.15
3-iodo-L-tyrosine
1.6
A22G mutated tRNATyr transcript
-
-
-
0.8
G15A mutated tRNATyr transcript
-
-
-
0.56 - 1.84
L-3,4-dihydroxyphenylalanine
0.018 - 0.038
L-beta-(5-hydroxy-2-pyridyl)-alanine
0.002
native yeast tRNATyr
-
pH 7.5, 30°C
-
0.00068 - 0.039
tRNATyr(G34C)
-
0.00035 - 0.0014
tRNATyr(wild-type)
-
0.0002
tyrosyl-tRNATyr
-
deacylation
-
2.2
U54C mutated tRNATyr transcript
-
-
-
additional information
additional information
-
2.04
3-chloro-L-tyrosine

-
pH 7.6, 30°C, wild-type enzyme
2.43
3-chloro-L-tyrosine
-
pH 7.6, 30°C, mutant Y43G
0.625
3-fluoro-D,L-tyrosine

-
pH 7.6, 30°C, wild-type enzyme
1.3
3-fluoro-D,L-tyrosine
-
pH 7.6, 30°C, mutant Y43G
0.13
3-iodo-L-tyrosine

-
pH 7.6, 37°C, mutant Y73V/Q195C
1.15
3-iodo-L-tyrosine
-
pH 7.6, 30°C, mutant Y43G
0.00043
ATP

-
pH 7.2, 37°C, Tyr activation activity, recombinant wild-type enzyme
0.00045
ATP
-
pH 7.2, 37°C, Tyr activation activity, recombinant lysine acetylated enzyme mutant 144AcK
0.00049
ATP
-
pH 7.2, 37°C, Tyr activation activity, recombinant lysine acetylated enzyme mutant 355AcK
0.00071
ATP
-
pH 7.2, 37°C, Tyr activation activity, recombinant lysine acetylated enzyme mutant 235AcK
0.00223
ATP
-
pH 7.2, 37°C, Tyr activation activity, recombinant lysine acetylated enzyme mutant 85AcK
0.07
ATP
-
phosphate exchange reaction, pH 8.0, wild-type enzyme
0.13
ATP
-
aminoacylation reaction, pH 8.0, wild-type enzyme
0.217
ATP
-
ATP-diphosphate exchange reaction
0.5
ATP
-
ATP-diphosphate exchange reaction
1.7
ATP
-
ATP-diphosphate exchange reaction
2
ATP
-
mutant M55L, pH 7.8, 25°C
2.1
ATP
-
wild-type enzyme, pH 7.8, 25°C
2.4
ATP
-
mutant I52L, pH 7.8, 25°C
2.7
ATP
-
mutant L105V, pH 7.8, 25°C
3
ATP
-
pH 7.5, 25°C, mutant S225A and mutant K231A
4
ATP
-
pH 7.5, 25°C, wild-type enzyme and mutant S224A
4.1
ATP
-
pH 7.5, 25°C, mutant S226A
0.46
D-tyrosine

-
pH 7.6, 30°C, wild-type enzyme
14
D-tyrosine
-
pH 7.6, 30°C, mutant Y43G
22
K+

-
pH 7.5, 25°C, mutant S226A
24
K+
-
pH 7.5, 25°C, mutant S224A
30
K+
-
pH 7.5, 25°C, mutant S225A
32
K+
-
pH 7.5, 25°C, wild-type enzyme
0.56
L-3,4-dihydroxyphenylalanine

-
pH 7.6, 30°C, mutant Y43G
1.84
L-3,4-dihydroxyphenylalanine
-
pH 7.6, 30°C, wild-type enzyme
0.018
L-beta-(5-hydroxy-2-pyridyl)-alanine

-
wild-type enzyme, pH 7.5, 30°C
0.038
L-beta-(5-hydroxy-2-pyridyl)-alanine
-
mutant F130S, pH 7.5, 30°C
0.0003
L-tyrosine

-
30°C, purified recombinant His-tagged enzyme
0.0014
L-tyrosine
-
mutant M55L, pH 7.8, 25°C
0.0015
L-tyrosine
-
mutant TyrRS, KMGCA
0.0018
L-tyrosine
-
mutant I52L, pH 7.8, 25°C
0.0021
L-tyrosine
-
wild-type enzyme and mutant L105V, pH 7.8, 25°C
0.0033
L-tyrosine
-
wild-type enzyme, pH 7.5, 30°C
0.0043
L-tyrosine
-
mutant TyrRS, RMSSS; wild-type TyrRS, KMSSS
0.0044
L-tyrosine
-
mutant TyrRS, AMSSS
0.0049
L-tyrosine
-
chloroplasts
0.0053
L-tyrosine
-
pH 7.6, 37°C, wild-type enzyme
0.00669
L-tyrosine
-
pH 7.2, 37°C, Tyr activation activity, recombinant lysine acetylated enzyme mutant 355AcK
0.00678
L-tyrosine
-
pH 7.2, 37°C, Tyr activation activity, recombinant lysine acetylated enzyme mutant 85AcK
0.0068
L-tyrosine
-
cytoplasm
0.00713
L-tyrosine
-
pH 7.2, 37°C, Tyr activation activity, recombinant wild-type enzyme
0.00728
L-tyrosine
-
pH 7.2, 37°C, Tyr activation activity, recombinant lysine acetylated enzyme mutant 144AcK
0.00845
L-tyrosine
-
pH 7.2, 37°C, Tyr activation activity, recombinant lysine acetylated enzyme mutant 235AcK
0.012
L-tyrosine
-
pH 7.6, 30°C, wild-type enzyme, radioisotopic assay
0.014
L-tyrosine
-
pH 7.6, 30°C, wild-type enzyme, spectrophotometric assay
0.021
L-tyrosine
-
phosphate exchange reaction, pH 8.0, wild-type enzyme
0.021
L-tyrosine
-
pH 7.5, 25°C, mutant S225A
0.027
L-tyrosine
-
aminoacylation reaction, pH 8.0, wild-type enzyme
0.03
L-tyrosine
-
pH 7.5, 25°C, mutant K231A
0.034
L-tyrosine
-
pH 7.5, 25°C, wild-type enzyme
0.042
L-tyrosine
-
pH 7.5, 25°C, mutant S226A
0.05
L-tyrosine
-
pH 7.5, 25°C, mutant S224A
0.066
L-tyrosine
-
mutant F130S, pH 7.5, 30°C
0.14
L-tyrosine
-
pH 7.6, 37°C, mutant Y73V/Q195C
0.146
L-tyrosine
recombinant wild-type enzyme, pH 7.8, 25°C
0.16
L-tyrosine
recombinant truncated mutant enzyme, pH 7.8, 25°C
1.19
L-tyrosine
-
pH 7.6, 30°C, mutant Y43G
0.000022
tRNATyr

-
chloroplasts
0.000022
tRNATyr
-
in absence of KCl, pH 7.4, 30°C
0.000037
tRNATyr
-
in presence of 50 mM KCl, pH 7.4, 30°C
0.0000898
tRNATyr
-
cytoplasm
0.000093
tRNATyr
-
in presence of 100 mM KCl, pH 7.4, 30°C
0.00022
tRNATyr
-
55°C, pH 8.0; wild type enzyme, at 55°C, in 100 mM HEPES-NaOH (pH 8.0), 10 mM MgCl2, 10 mM KCl
0.00024
tRNATyr
-
in presence of 150 mM KCl, pH 7.4, 30°C
0.00037
tRNATyr
-
pH 7.2, 37°C, tRNATyr aminoacylation activity, recombinant wild-type enzyme
0.00042
tRNATyr
-
pH 7.2, 37°C, tRNATyr aminoacylation activity, recombinant lysine acetylated enzyme mutant 144AcK
0.00045
tRNATyr
-
pH 7.2, 37°C, tRNATyr aminoacylation activity, recombinant lysine acetylated enzyme mutant 85AcK
0.00048
tRNATyr
-
pH 7.2, 37°C, tRNATyr aminoacylation activity, recombinant lysine acetylated enzyme mutant 355AcK
0.00052
tRNATyr
-
acylation
0.00052
tRNATyr
pH 7.6, 37°C, native Escherichia coli tRNATyr
0.0009
tRNATyr
-
30°C, purified recombinant His-tagged enzyme
0.0025
tRNATyr
-
aminoacylation reaction, pH 8.0, wild-type enzyme
0.0048
tRNATyr
pH 7.6, 37°C, human mitochondrial tRNATyr
0.00068
tRNATyr(G34C)

-
37°C, pH 7.5, mutant enzyme D268R
-
0.039
tRNATyr(G34C)
-
37°C, pH 7.5, wild-type enzyme
-
0.00035
tRNATyr(wild-type)

-
37°C, pH 7.5, wild-type enzyme
-
0.0014
tRNATyr(wild-type)
-
37°C, pH 7.5, mutant enzyme D268R
-
0.002
tyrosine

-
-
0.008
tyrosine
-
acylation
0.012
tyrosine
-
ATP-diphosphate exchange reaction
0.013
tyrosine
-
ATP-diphosphate exchange reaction and aminoacylation
additional information
additional information

-
kinetics
-
additional information
additional information
-
role of threonine 234 in catalysis
-
additional information
additional information
-
role of lysine 233 in catalysis
-
additional information
additional information
-
kinetic analysis of mutation
-
additional information
additional information
-
kinetics
-
additional information
additional information
-
-
-
additional information
additional information
-
role of a mobile loop, corresponding to KMSKS signature sequence in catalytic mechanism
-
additional information
additional information
-
values for mutant strains
-
additional information
additional information
-
stoichiometry of substrate binding
-
additional information
additional information
-
kinetics, influence of assay conditions, Km for diverse tRNA variants, overview
-
additional information
additional information
-
kinetics
-
additional information
additional information
-
kinetics
-
additional information
additional information
-
mutants
-
additional information
additional information
-
fluorescence emission measurement for determination of steady-state kinetics for the His-tagged and the non-His-tagged recombinant enzyme
-
additional information
additional information
-
energy profiles for wild-type and mutant enzymes, kinetics for the second reaction step: wild-type enzyme and mutants D78A, Y169A, Q173A, D194A, and Q195A, kinetics for the first reaction step: wild-type enzyme, and mutants D194A and Q195A
-
additional information
additional information
-
the C-terminal His-tag of the recombinant enzyme has little effect on the catalytic activity
-
additional information
additional information
kinetics with Escherichia coli tRNATyr, Plasmodium falciparum tRNATyr, and diverse wild-type and mutant Saccharomyces cerevisiae tRNATyrs, overview
-
additional information
additional information
-
kinetic parameters for anticodon mutants of tRNATyr and for for acceptor stem mutants of tRNATyr
-
additional information
additional information
-
Michaelis-Menten steady-state kinetics. Steady-state kinetic constants for ATP-[32P]PPi exchange for CHO cytosolic full length wild-type and variant TyrRS
-
additional information
additional information
Michaelis-Menten steady-state kinetics. Steady-state kinetic constants for ATP-[32P]PPi exchange for CHO cytosolic full length wild-type and variant TyrRS
-
additional information
additional information
-
calculation of the L-Tyr/D-Tyr binding free energy difference. Michaelis-Menten kinetics of wild-type and mutant enzymes
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.13 - 6.08
3-chloro-L-tyrosine
0.62 - 6.08
3-fluoro-D,L-tyrosine
0.43 - 0.48
3-iodo-L-tyrosine
0.00003
A22G mutated tRNATyr transcript
-
-
-
0.0002
G15A mutated tRNATyr transcript
-
-
-
0.67 - 6.08
L-3,4-dihydroxyphenylalanine
0.042 - 0.11
L-beta-(5-hydroxy-2-pyridyl)-alanine
1.5
native yeast tRNATyr
-
pH 7.5, 30°C
-
0.07 - 0.079
tRNATyr(G34C)
-
0.12 - 0.19
tRNATyr(wild-type)
-
0.012
U54C mutated tRNATyr transcript
-
-
-
additional information
additional information
-
0.13
3-chloro-L-tyrosine

-
pH 7.6, 30°C, wild-type enzyme
1.46
3-chloro-L-tyrosine
-
pH 7.6, 30°C, mutant Y43G
6.08
3-chloro-L-tyrosine
-
pH 7.6, 30°C, mutant Y43G
0.62
3-fluoro-D,L-tyrosine

-
pH 7.6, 30°C, mutant Y43G
3.3
3-fluoro-D,L-tyrosine
-
pH 7.6, 30°C, wild-type enzyme
4.96
3-fluoro-D,L-tyrosine
-
pH 7.6, 30°C, wild-type enzyme
6.08
3-fluoro-D,L-tyrosine
-
pH 7.6, 30°C, mutant Y43G
0.43
3-iodo-L-tyrosine

-
pH 7.6, 37°C, mutant Y73V/Q195C
0.48
3-iodo-L-tyrosine
-
pH 7.6, 30°C, mutant Y43G
0.1
ATP

-
pH 7.2, 37°C, Tyr activation activity, recombinant lysine acetylated enzyme mutant 235AcK
2
ATP
-
pH 7.2, 37°C, Tyr activation activity, recombinant lysine acetylated enzyme mutant 85AcK
3.3
ATP
-
phosphate exchange reaction, pH 8.0, wild-type enzyme
4.6
ATP
-
mutant M55L, pH 7.8, 25°C
5.29
ATP
-
phosphate exchange reaction, pH 8.0, wild-type enzyme
6.8
ATP
-
mutant I52L, pH 7.8, 25°C
7.7
ATP
-
aminoacylation reaction, pH 8.0, wild-type enzyme
7.7
ATP
-
wild-type enzyme, pH 7.8, 25°C
11.9
ATP
-
pH 7.2, 37°C, Tyr activation activity, recombinant lysine acetylated enzyme mutant 355AcK
12
ATP
-
mutant L105V, pH 7.8, 25°C
12.3
ATP
-
pH 7.2, 37°C, Tyr activation activity, recombinant lysine acetylated enzyme mutant 144AcK
14.2
ATP
-
pH 7.2, 37°C, Tyr activation activity, recombinant wild-type enzyme
0.37
D-tyrosine

-
pH 7.6, 30°C, mutant Y43G
1.2
D-tyrosine
-
pH 7.6, 30°C, wild-type enzyme
0.67
L-3,4-dihydroxyphenylalanine

-
pH 7.6, 30°C, mutant Y43G
1.65
L-3,4-dihydroxyphenylalanine
-
pH 7.6, 30°C, wild-type enzyme
6.08
L-3,4-dihydroxyphenylalanine
-
pH 7.6, 30°C, mutant Y43G
0.042
L-beta-(5-hydroxy-2-pyridyl)-alanine

-
mutant F130S, pH 7.5, 30°C
0.11
L-beta-(5-hydroxy-2-pyridyl)-alanine
-
wild-type enzyme, pH 7.5, 30°C
0.01
L-tyrosine

-
mutant TyrRS, RMSSS
0.012
L-tyrosine
-
mutant TyrRS, AMSSS
0.025
L-tyrosine
-
mutant TyrRS, KMGCA
0.045
L-tyrosine
-
pH 7.6, 37°C, mutant Y73V/Q195C
0.1
L-tyrosine
-
pH 7.2, 37°C, Tyr activation activity, recombinant lysine acetylated enzyme mutant 235AcK
0.53
L-tyrosine
-
wild-type TyrRS, KMSSS
0.74
L-tyrosine
-
wild-type enzyme, pH 7.5, 30°C
0.78
L-tyrosine
-
pH 7.5, 25°C, mutant S226A
0.95
L-tyrosine
-
pH 7.6, 30°C, mutant Y43G
1.4
L-tyrosine
-
mutant F130S, pH 7.5, 30°C
1.49
L-tyrosine
-
30°C, purified recombinant His-tagged enzyme
2
L-tyrosine
-
pH 7.2, 37°C, Tyr activation activity, recombinant lysine acetylated enzyme mutant 85AcK
2.5
L-tyrosine
-
mutant M55L, pH 7.8, 25°C
3.3
L-tyrosine
-
phosphate exchange reaction, pH 8.0, wild-type enzyme
3.6
L-tyrosine
-
mutant I52L, pH 7.8, 25°C
4.4
L-tyrosine
-
pH 7.6, 30°C, wild-type enzyme, radioisotopic assay
4.6
L-tyrosine
-
pH 7.6, 30°C, wild-type enzyme, spectrophotometric assay
4.9
L-tyrosine
-
mutant L105V, pH 7.8, 25°C
5.29
L-tyrosine
-
phosphate exchange reaction, pH 8.0, wild-type enzyme
5.4
L-tyrosine
-
wild-type enzyme, pH 7.8, 25°C
6
L-tyrosine
-
pH 7.5, 25°C, mutant S224A
6.08
L-tyrosine
-
wild-type enzyme, pH 7.5, 30°C
6.08
L-tyrosine
-
pH 7.5, 25°C, mutant S226A
6.08
L-tyrosine
-
30°C, purified recombinant His-tagged enzyme
7.7
L-tyrosine
-
aminoacylation reaction, pH 8.0, wild-type enzyme
11.9
L-tyrosine
-
pH 7.2, 37°C, Tyr activation activity, recombinant lysine acetylated enzyme mutant 355AcK
12
L-tyrosine
-
pH 7.6, 37°C, wild-type enzyme
12.3
L-tyrosine
-
pH 7.2, 37°C, Tyr activation activity, recombinant lysine acetylated enzyme mutant 144AcK
12.5
L-tyrosine
recombinant wild-type enzyme, pH 7.8, 25°C
14.2
L-tyrosine
-
pH 7.2, 37°C, Tyr activation activity, recombinant wild-type enzyme
15
L-tyrosine
recombinant truncated mutant enzyme, pH 7.8, 25°C
30
L-tyrosine
-
pH 7.5, 25°C, mutant K231A
31
L-tyrosine
-
pH 7.5, 25°C, mutant S225A
45
L-tyrosine
-
pH 7.5, 25°C, wild-type enzyme
0.046
tRNATyr

-
-
0.15
tRNATyr
-
pH 7.2, 37°C, tRNATyr aminoacylation activity, recombinant lysine acetylated enzyme mutant 85AcK
0.29
tRNATyr
-
55°C, pH 8.0; wild type enzyme, at 55°C, in 100 mM HEPES-NaOH (pH 8.0), 10 mM MgCl2, 10 mM KCl
1.09
tRNATyr
-
pH 7.2, 37°C, tRNATyr aminoacylation activity, recombinant lysine acetylated enzyme mutant 355AcK
1.17
tRNATyr
-
pH 7.2, 37°C, tRNATyr aminoacylation activity, recombinant lysine acetylated enzyme mutant 144AcK
1.32
tRNATyr
-
pH 7.2, 37°C, tRNATyr aminoacylation activity, recombinant wild-type enzyme
0.07
tRNATyr(G34C)

-
37°C, pH 7.5, wild-type enzyme
-
0.079
tRNATyr(G34C)
-
37°C, pH 7.5, mutant enzyme D268R
-
0.12
tRNATyr(wild-type)

-
37°C, pH 7.5, mutant enzyme D268R
-
0.19
tRNATyr(wild-type)
-
37°C, pH 7.5, wild-type enzyme
-
additional information
additional information

-
influence of assay conditions, kcat for diverse tRNA variants, overview
-
additional information
additional information
-
mutants
-
additional information
additional information
-
the C-terminal His-tag of the recombinant enzyme has little effect on the catalytic activity
-
additional information
additional information
-
-
additional information
additional information
-
kinetic parameters for anticodon mutants of tRNATyr and for for acceptor stem mutants of tRNATyr
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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0.05117
1-[4-[([4-[(naphthalen-1-yl)methyl]-5-oxo-2,5-dihydrothiophen-3-yl]oxy)carbonyl]phenyl]dibroman-1-ium
Staphylococcus aureus
-
pH 7.9, 37°C, recombinant enzyme
-
0.1
3-(3,4-dichlorophenyl)-4-(2-(4-methylpiperazin-1-yl)ethoxy)furan-2(5H)-one
Staphylococcus aureus
-
above, pH not specified in the publication, temperature not specified in the publication
0.1
3-(3,4-difluorophenyl)-4-(2-(piperidin-1-yl)ethoxy)furan-2(5H)-one
Staphylococcus aureus
-
above, pH not specified in the publication, temperature not specified in the publication
0.1
3-(3,4-dimethoxyphenyl)-4-(2-(4-methylpiperazin-1-yl)ethoxy)furan-2(5H)-one
Staphylococcus aureus
-
above, pH not specified in the publication, temperature not specified in the publication
0.1
3-(3,4-dimethoxyphenyl)-4-(2-(piperidin-1-yl)ethoxy)furan-2(5H)-one
Staphylococcus aureus
-
above, pH not specified in the publication, temperature not specified in the publication
0.0243
3-(3-bromophenyl)-4-(2-morpholinoethoxy)furan-2(5H)-one
Staphylococcus aureus
-
pH not specified in the publication, temperature not specified in the publication
0.0205
3-(3-chlorophenyl)-4-(2-morpholinoethoxy)furan-2(5H)-one
Staphylococcus aureus
-
pH not specified in the publication, temperature not specified in the publication
0.0256
3-(3-hydroxyphenyl)-4-(2-morpholinoethoxy)furan-2(5H)-one
Staphylococcus aureus
-
pH not specified in the publication, temperature not specified in the publication
0.0375
3-(3-methoxyphenyl)-4-(2-morpholinoethoxy)furan-2(5H)-one
Staphylococcus aureus
-
pH not specified in the publication, temperature not specified in the publication
0.0024
3-(4-bromophenyl)-4-(2-morpholinoethoxy)furan-2(5H)-one
Staphylococcus aureus
-
pH not specified in the publication, temperature not specified in the publication
0.00062
3-(4-chlorophenyl)-4-(2-morpholinoethoxy)furan-2(5H)-one
Staphylococcus aureus
-
pH not specified in the publication, temperature not specified in the publication
0.0001
3-(4-hydroxyphenyl)-4-(2-morpholinoethoxy)furan-2(5H)-one
Staphylococcus aureus
-
pH not specified in the publication, temperature not specified in the publication
0.0328
3-(4-methoxyphenyl)-4-(2-morpholinoethoxy)furan-2(5H)-one
Staphylococcus aureus
-
pH not specified in the publication, temperature not specified in the publication
0.0536
3-phenyl-4-(2-(piperidin-1-yl)ethoxy)furan-2(5H)-one
Staphylococcus aureus
-
pH not specified in the publication, temperature not specified in the publication
0.0291
3-phenyl-4-(2-(propylamino)ethoxy)furan-2(5H)-one
Staphylococcus aureus
-
pH not specified in the publication, temperature not specified in the publication
0.0355
3-phenyl-4-(2-(pyrrolidin-1-yl)ethoxy)furan-2(5H)-one
Staphylococcus aureus
-
pH not specified in the publication, temperature not specified in the publication
0.0165
4-(2-(2,4-dichlorophenylformyloxy)ethoxy)-3-phenylfuran-2(5H)-one
Staphylococcus aureus
-
in 100 mM Tris/Cl pH 7.9, 50 mM KCl, 16 mM MgCl2, at 37°C
0.0502
4-(2-(2,4-dihydroxyphenylformyloxy)ethoxy)-3-phenylfuran-2(5H)-one
Staphylococcus aureus
-
in 100 mM Tris/Cl pH 7.9, 50 mM KCl, 16 mM MgCl2, at 37°C
0.0052
4-(2-(2,5-dichlorophenylformyloxy)ethoxy)-3-phenylfuran-2(5H)-one
Staphylococcus aureus
-
in 100 mM Tris/Cl pH 7.9, 50 mM KCl, 16 mM MgCl2, at 37°C
0.1
4-(2-(2-(4-nitrophenyl)hydrazinyl)ethoxy)-3-phenylfuran-2(5H)-one
Staphylococcus aureus
-
above, pH not specified in the publication, temperature not specified in the publication
0.0568
4-(2-(2-chlorophenylformyloxy)ethoxy)-3-phenylfuran-2(5H)-one
Staphylococcus aureus
-
in 100 mM Tris/Cl pH 7.9, 50 mM KCl, 16 mM MgCl2, at 37°C
0.0414
4-(2-(2-hydroxyphenylformyloxyl)ethoxy)-3-phenylfuran-2(5H)-one
Staphylococcus aureus
-
in 100 mM Tris/Cl pH 7.9, 50 mM KCl, 16 mM MgCl2, at 37°C
0.0647
4-(2-(2-methoxyphenylformyloxy)ethoxy)-3-phenylfuran-2(5H)-one
Staphylococcus aureus
-
in 100 mM Tris/Cl pH 7.9, 50 mM KCl, 16 mM MgCl2, at 37°C
0.1
4-(2-(2-methylphenylformyloxy)ethoxy)-3-phenylfuran-2(5H)-one
Staphylococcus aureus
-
IC50 above 0.1 mM, in 100 mM Tris/Cl pH 7.9, 50 mM KCl, 16 mM MgCl2, at 37°C
0.0182
4-(2-(2-nitrophenylformyloxyl)ethoxy)-3-phenylfuran-2(5H)-one
Staphylococcus aureus
-
in 100 mM Tris/Cl pH 7.9, 50 mM KCl, 16 mM MgCl2, at 37°C
0.0334
4-(2-(3,4-dichlorophenylformyloxy)ethoxy)-3-phenylfuran-2(5H)-one
Staphylococcus aureus
-
in 100 mM Tris/Cl pH 7.9, 50 mM KCl, 16 mM MgCl2, at 37°C
0.0753
4-(2-(3,4-dihydroxyphenylformyloxy)ethoxy)-3-phenylfuran-2(5H)-one
Staphylococcus aureus
-
in 100 mM Tris/Cl pH 7.9, 50 mM KCl, 16 mM MgCl2, at 37°C
0.0838
4-(2-(3,4-dimethoxyphenylacetyloxy)ethoxy)-3-phenylfuran-2(5H)-one
Staphylococcus aureus
-
in 100 mM Tris/Cl pH 7.9, 50 mM KCl, 16 mM MgCl2, at 37°C
0.0067
4-(2-(3,5-dihydroxyphenylformyloxy)ethoxy)-3-phenylfuran-2(5H)-one
Staphylococcus aureus
-
in 100 mM Tris/Cl pH 7.9, 50 mM KCl, 16 mM MgCl2, at 37°C
0.0035
4-(2-(3-bromophenylacetyloxy)ethoxy)-3-(4-chlorophenyl)furan-2(5H)-one
Staphylococcus aureus
-
in 100 mM Tris/Cl pH 7.9, 50 mM KCl, 16 mM MgCl2, at 37°C
0.0011
4-(2-(3-chlorophenylacetyloxy)ethoxy)-3-(4-chlorophenyl)furan-2(5H)-one
Staphylococcus aureus
-
in 100 mM Tris/Cl pH 7.9, 50 mM KCl, 16 mM MgCl2, at 37°C
0.1
4-(2-(3-chlorophenylacetyloxy)ethoxy)-3-phenylfuran-2(5H)-one
Staphylococcus aureus
-
IC50 above 0.1 mM, in 100 mM Tris/Cl pH 7.9, 50 mM KCl, 16 mM MgCl2, at 37°C
0.0009
4-(2-(3-chlorophenylformyloxy)ethoxy)-3-(4-chlorophenyl)furan-2(5H)-one
Staphylococcus aureus
-
in 100 mM Tris/Cl pH 7.9, 50 mM KCl, 16 mM MgCl2, at 37°C
0.081
4-(2-(3-methylphenylformyloxy)ethoxy)-3-phenylfuran-2(5H)-one
Staphylococcus aureus
-
in 100 mM Tris/Cl pH 7.9, 50 mM KCl, 16 mM MgCl2, at 37°C
0.1
4-(2-(3-nitrophenylformyloxy)ethoxy)-3-phenylfuran-2(5H)-one
Staphylococcus aureus
-
IC50 above 0.1 mM, in 100 mM Tris/Cl pH 7.9, 50 mM KCl, 16 mM MgCl2, at 37°C
0.026
4-(2-(3-pyridylformyloxy)ethoxy)-3-phenylfuran-2(5H)-one
Staphylococcus aureus
-
in 100 mM Tris/Cl pH 7.9, 50 mM KCl, 16 mM MgCl2, at 37°C
0.0043
4-(2-(3-trifluoromethylphenylformyoxy)ethoxy)-3-phenylfuran-2(5H)-one
Staphylococcus aureus
-
in 100 mM Tris/Cl pH 7.9, 50 mM KCl, 16 mM MgCl2, at 37°C
0.0167
4-(2-(4-bromophenylacetyloxy)ethoxy)-3-(4-chlorophenyl)furan-2(5H)-one
Staphylococcus aureus
-
in 100 mM Tris/Cl pH 7.9, 50 mM KCl, 16 mM MgCl2, at 37°C
0.0481
4-(2-(4-bromophenylacetyloxy)ethoxy)-3-phenylfuran-2(5H)-one
Staphylococcus aureus
-
in 100 mM Tris/Cl pH 7.9, 50 mM KCl, 16 mM MgCl2, at 37°C
0.0093
4-(2-(4-chlorophenylacetyloxy)ethoxy)-3-(4-chlorophenyl)furan-2(5H)-one
Staphylococcus aureus
-
in 100 mM Tris/Cl pH 7.9, 50 mM KCl, 16 mM MgCl2, at 37°C
0.0088
4-(2-(4-chlorophenylformyloxy)ethoxy)-3-phenylfuran-2(5H)-one
Staphylococcus aureus
-
in 100 mM Tris/Cl pH 7.9, 50 mM KCl, 16 mM MgCl2, at 37°C
0.0057
4-(2-(4-fluorophenylacetyloxy)ethoxy)-3-(4-chlorophenyl)furan-2(5H)-one
Staphylococcus aureus
-
in 100 mM Tris/Cl pH 7.9, 50 mM KCl, 16 mM MgCl2, at 37°C
0.0936
4-(2-(4-fluorophenylacetyloxy)ethoxy)-3-phenylfuran-2(5H)-one
Staphylococcus aureus
-
in 100 mM Tris/Cl pH 7.9, 50 mM KCl, 16 mM MgCl2, at 37°C
0.0075
4-(2-(4-fluorophenylformyloxy)ethoxy)-3-phenylfuran-2(5H)-one
Staphylococcus aureus
-
in 100 mM Tris/Cl pH 7.9, 50 mM KCl, 16 mM MgCl2, at 37°C
0.0079
4-(2-(4-hydroxyphenylacetyloxy)ethoxy)-3-(4-chlorophenyl)furan-2(5H)-one
Staphylococcus aureus
-
in 100 mM Tris/Cl pH 7.9, 50 mM KCl, 16 mM MgCl2, at 37°C
0.1
4-(2-(4-hydroxyphenylacetyloxy)ethoxy)-3-phenylfuran-2(5H)-one
Staphylococcus aureus
-
IC50 above 0.1 mM, in 100 mM Tris/Cl pH 7.9, 50 mM KCl, 16 mM MgCl2, at 37°C
0.0112
4-(2-(4-hydroxyphenylformyloxy)ethoxy)-3-phenylfuran-2(5H)-one
Staphylococcus aureus
-
in 100 mM Tris/Cl pH 7.9, 50 mM KCl, 16 mM MgCl2, at 37°C
0.0178
4-(2-(4-methylphenylformyloxy)ethoxy)-3-phenylfuran-2(5H)-one
Staphylococcus aureus
-
in 100 mM Tris/Cl pH 7.9, 50 mM KCl, 16 mM MgCl2, at 37°C
0.0086
4-(2-(4-methylpiperazin-1-yl)ethoxy)-3-phenylfuran-2(5H)-one
Staphylococcus aureus
-
pH not specified in the publication, temperature not specified in the publication
0.0052
4-(2-(4-nitrophenylformyloxy)ethoxy)-3-phenylfuran-2(5H)-one
Staphylococcus aureus
-
in 100 mM Tris/Cl pH 7.9, 50 mM KCl, 16 mM MgCl2, at 37°C
0.0168
4-(2-(6-hydroxynaphthalen-2-ylformyloxy)ethoxy)-3-phenylfuran-2(5H)-one
Staphylococcus aureus
-
in 100 mM Tris/Cl pH 7.9, 50 mM KCl, 16 mM MgCl2, at 37°C
0.1
4-(2-(benzylamino)ethoxy)-3-phenylfuran-2(5H)-one
Staphylococcus aureus
-
above, pH not specified in the publication, temperature not specified in the publication
0.0719
4-(2-(butylamino)ethoxy)-3-phenylfuran-2(5H)-one
Staphylococcus aureus
-
pH not specified in the publication, temperature not specified in the publication
0.1
4-(2-(cyclohexylamino)ethoxy)-3-(3,4-dimethoxyphenyl)furan-2(5H)-one
Staphylococcus aureus
-
above, pH not specified in the publication, temperature not specified in the publication
0.0874
4-(2-(cyclohexylamino)ethoxy)-3-phenylfuran-2(5H)-one
Staphylococcus aureus
-
pH not specified in the publication, temperature not specified in the publication
0.0177
4-(2-(naphthalen-2-ylformyloxy)ethoxy)-3-phenylfuran-2(5H)-one
Staphylococcus aureus
-
in 100 mM Tris/Cl pH 7.9, 50 mM KCl, 16 mM MgCl2, at 37°C
0.0846
4-(2-butyryloxyethoxy)-3-phenylfuran-2(5H)-one
Staphylococcus aureus
-
in 100 mM Tris/Cl pH 7.9, 50 mM KCl, 16 mM MgCl2, at 37°C
0.0478
4-(2-hexanoyloxyethoxy)-3-phenylfuran-2(5H)-one
Staphylococcus aureus
-
in 100 mM Tris/Cl pH 7.9, 50 mM KCl, 16 mM MgCl2, at 37°C
0.0062
4-(2-morpholinoethoxy)-3-phenylfuran-2(5H)-one
Staphylococcus aureus
-
pH not specified in the publication, temperature not specified in the publication
0.041
4-(2-octanoyloxyethoxy)-3-phenylfuran-2(5H)-one
Staphylococcus aureus
-
in 100 mM Tris/Cl pH 7.9, 50 mM KCl, 16 mM MgCl2, at 37°C
0.0128
4-(2-phenylacetyloxylethoxy)-3-phenylfuran-2(5H)-one
Staphylococcus aureus
-
in 100 mM Tris/Cl pH 7.9, 50 mM KCl, 16 mM MgCl2, at 37°C
0.1
4-[(naphthalen-1-yl)methyl]-5-oxo-2,5-dihydrothiophen-3-yl 2-bromobenzoate
Staphylococcus aureus
-
above, pH 7.9, 37°C, recombinant enzyme
0.1
4-[(naphthalen-1-yl)methyl]-5-oxo-2,5-dihydrothiophen-3-yl 2-chlorobenzoate
Staphylococcus aureus
-
above, pH 7.9, 37°C, recombinant enzyme
0.1
4-[(naphthalen-1-yl)methyl]-5-oxo-2,5-dihydrothiophen-3-yl 2-chloropyridine-3-carboxylate
Staphylococcus aureus
-
above, pH 7.9, 37°C, recombinant enzyme
0.1
4-[(naphthalen-1-yl)methyl]-5-oxo-2,5-dihydrothiophen-3-yl 2-fluorobenzoate
Staphylococcus aureus
-
above, pH 7.9, 37°C, recombinant enzyme
0.0921
4-[(naphthalen-1-yl)methyl]-5-oxo-2,5-dihydrothiophen-3-yl 2-methoxybenzoate
Staphylococcus aureus
-
pH 7.9, 37°C, recombinant enzyme
0.08862
4-[(naphthalen-1-yl)methyl]-5-oxo-2,5-dihydrothiophen-3-yl 2-methylbenzoate
Staphylococcus aureus
-
pH 7.9, 37°C, recombinant enzyme
0.1
4-[(naphthalen-1-yl)methyl]-5-oxo-2,5-dihydrothiophen-3-yl 2-nitrobenzoate
Staphylococcus aureus
-
above, pH 7.9, 37°C, recombinant enzyme
0.01898
4-[(naphthalen-1-yl)methyl]-5-oxo-2,5-dihydrothiophen-3-yl 3-(3-methylphenyl)propanoate
Staphylococcus aureus
-
pH 7.9, 37°C, recombinant enzyme
0.0111
4-[(naphthalen-1-yl)methyl]-5-oxo-2,5-dihydrothiophen-3-yl 3-(4-methylphenyl)propanoate
Staphylococcus aureus
-
pH 7.9, 37°C, recombinant enzyme
0.07109
4-[(naphthalen-1-yl)methyl]-5-oxo-2,5-dihydrothiophen-3-yl 3-aminobenzoate
Staphylococcus aureus
-
pH 7.9, 37°C, recombinant enzyme
0.08313
4-[(naphthalen-1-yl)methyl]-5-oxo-2,5-dihydrothiophen-3-yl 3-bromobenzoate
Staphylococcus aureus
-
pH 7.9, 37°C, recombinant enzyme
0.08613
4-[(naphthalen-1-yl)methyl]-5-oxo-2,5-dihydrothiophen-3-yl 3-chlorobenzoate
Staphylococcus aureus
-
pH 7.9, 37°C, recombinant enzyme
0.08214
4-[(naphthalen-1-yl)methyl]-5-oxo-2,5-dihydrothiophen-3-yl 3-fluorobenzoate
Staphylococcus aureus
-
pH 7.9, 37°C, recombinant enzyme
0.07211
4-[(naphthalen-1-yl)methyl]-5-oxo-2,5-dihydrothiophen-3-yl 3-hydroxybenzoate
Staphylococcus aureus
-
pH 7.9, 37°C, recombinant enzyme
0.069
4-[(naphthalen-1-yl)methyl]-5-oxo-2,5-dihydrothiophen-3-yl 3-methylbenzoate
Staphylococcus aureus
-
pH 7.9, 37°C, recombinant enzyme
0.083
4-[(naphthalen-1-yl)methyl]-5-oxo-2,5-dihydrothiophen-3-yl 3-phenylpropanoate
Staphylococcus aureus
-
pH 7.9, 37°C, recombinant enzyme
0.04894
4-[(naphthalen-1-yl)methyl]-5-oxo-2,5-dihydrothiophen-3-yl 4-aminobenzoate
Staphylococcus aureus
-
pH 7.9, 37°C, recombinant enzyme
0.05523
4-[(naphthalen-1-yl)methyl]-5-oxo-2,5-dihydrothiophen-3-yl 4-chlorobenzoate
Staphylococcus aureus
-
pH 7.9, 37°C, recombinant enzyme
0.06514
4-[(naphthalen-1-yl)methyl]-5-oxo-2,5-dihydrothiophen-3-yl 4-fluorobenzoate
Staphylococcus aureus
-
pH 7.9, 37°C, recombinant enzyme
0.04476
4-[(naphthalen-1-yl)methyl]-5-oxo-2,5-dihydrothiophen-3-yl 4-hydroxybenzoate
Staphylococcus aureus
-
pH 7.9, 37°C, recombinant enzyme
0.05008
4-[(naphthalen-1-yl)methyl]-5-oxo-2,5-dihydrothiophen-3-yl 4-methylbenzoate
Staphylococcus aureus
-
pH 7.9, 37°C, recombinant enzyme
0.1
4-[(naphthalen-1-yl)methyl]-5-oxo-2,5-dihydrothiophen-3-yl 6-chloropyridine-3-carboxylate
Staphylococcus aureus
-
above, pH 7.9, 37°C, recombinant enzyme
0.1
4-[(naphthalen-1-yl)methyl]-5-oxo-2,5-dihydrothiophen-3-yl 6-hydroxypyridine-3-carboxylate
Staphylococcus aureus
-
above, pH 7.9, 37°C, recombinant enzyme
0.04332
4-[(naphthalen-1-yl)methyl]-5-oxo-2,5-dihydrothiophen-3-yl benzoate
Staphylococcus aureus
-
pH 7.9, 37°C, recombinant enzyme
0.1
4-[(naphthalen-1-yl)methyl]-5-oxo-2,5-dihydrothiophen-3-yl pyridine-3-carboxylate
Staphylococcus aureus
-
above, pH 7.9, 37°C, recombinant enzyme
0.1
4-[(naphthalen-1-yl)methyl]-5-oxo-2,5-dihydrothiophen-3-yl pyridine-4-carboxylate
Staphylococcus aureus
-
above, pH 7.9, 37°C, recombinant enzyme
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Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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