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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
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3'-O-methyl-ATP
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ATP-diphosphate exchange, noncompetitive with respect to ATP
3'-O-Methyladenosine
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ATP-diphosphate exchange, noncompetitive with respect to ATP
3-[(4-[[4-oxo-2-(phenylimino)-1,3-thiazolidin-5-ylidene]methyl]phenoxy) methyl]benzoic acid
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3-[[([[2-(4-chlorophenyl)-4-quinolinyl]carbonyl]amino)carbothioyl]amino]benzoic acid
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4,5,6,7-Tetrafluorotryptophan
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5,7-Difluorotryptophan
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5-hydroxytryptophan
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ATP-diphosphate exchange, weak
5-Methyltryptophan
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ATP-diphosphate exchange, weak
6-methyltryptophan
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ATP-diphosphate exchange, weak
9-(2',3'-Dihydroxypropyl)adenine
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S-isomer
9-(2'-Hydroxyethyl)adenine
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9-(2'-Hydroxyethyl)adenine triphosphate
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9-(3'-Hydroxypropyl)adenine
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9-(3'-Hydroxypropyl)adenine triphosphate
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9-(4'-Hydroxybutyl)adenine
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9-(4'-Hydroxybutyl)adenine triphosphate
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Adenosine-5'-(beta-bromoethane phosphonate)
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Adenosine-5'-(beta-bromoethanediphosphonate)
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Adenosine-5'-(beta-chloroethyl phosphate)
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Adenosine-5'-chloromethylphosphonate
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ATP-diphosphate exchange, reversible, incompetitive
alpha,beta-methylene-ATP
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beta-Indolyl propionic acid
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beta-indolylacetic acid
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beta-Indolylpyruvic acid
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beta-Methyl-DL-tryptophan
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ATP-diphosphate exchange
chuangximycin aldehyde
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strong inhibition
chuangximycin lactone
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chuangximycin nitrile
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diethyl dicarbonate
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substrates protect, completely reactivated by hydroxylamine
DL-Tryptophanyl hydroxamate
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ATP-diphosphate exchange
gamma-(n-Azidoanilide)-ATP
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Mixed anhydride of ADP and mesithylenecarboxylic acid
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Mixed anhydride of AMP and mesithylenecarboxylic acid
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N-acetyl-L-tryptophan
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N-Formyl-L-tryptophan
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p-hydroxymercuribenzoate
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succinylacetone
a heme biosynthesis inhibitor, inhibit cellular TrpRS activity in IFN-gamma-activated cells without affecting TrpRS protein expression
chuangxinmycin
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CAS: 63339-68-4, natural product, first isolated from Actinoplanes tsinanensis, potent and selective inhibition of the aminoacylation
indolmycin
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specifically inhibits enzyme
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
indolmycin
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liver enzyme is affected much less
L-tryptophan
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product inhibition at physiologic concentrations
L-tryptophan
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product inhibition at physiologic concentrations
NEM
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tryptamine
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tryptamine
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competitive, inhibition of the enzyme leads to inhibition of protein biosynthesis, tryptamine stabilizes the enzyme
tryptamine
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a metabolic tryptophan analog that acts as a potent competitive inhibitor of TrpRS, overview
tryptamine
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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
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additional information
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indolmycin and ATP form a ternary complex with BsTrpRS
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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
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additional information
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the full-length-WRS-induced TNF-alpha and MIP-1alpha production is significantly inhibited when TLR4, MD2, and TLR2 (to lesser degree) are suppressed
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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
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additional information
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the full-length-WRS-induced TNF-alpha and MIP-1alpha production is significantly inhibited when TLR4, MD2, and TLR2 (to lesser degree) are suppressed
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additional information
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no inhibition by chuangximycin methyl ester, hydroxamic acid, amide, hydroxymethyl or tetrazole analogue
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additional information
screening for SeWRS inhibitors, binding site mapping and virtual screening, modeling, overview, MIC values, and cytotoxic activities of inhibitors, overview
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additional information
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screening for SeWRS inhibitors, binding site mapping and virtual screening, modeling, overview, MIC values, and cytotoxic activities of inhibitors, overview
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additional information
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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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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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