2.7.7.23 (2S,4R)-N-(4-((6,7-dimethoxyquinazolin-4-yl)amino)phenyl)-4-hydroxypyrrolidine-2-carboxamide - 215925 2.7.7.23 (3-hydroxyphenyl)[4-(5,6,7,8-tetrahydroquinazolin-4-ylamino)phenyl]methanone 30% inhibition at 0.05 mM 215940 2.7.7.23 (4-(6,7-dimethoxyquinazolin-4-yl)piperazin-1-yl)(phenyl)-methanone - 216023 2.7.7.23 (S)-N-(4-((6,7-dimethoxyquinazolin-4-yl)amino)phenyl)pyrrolidine-2-carboxamide - 216081 2.7.7.23 (Z)-4-(4-(benzyloxy)benzylidene)-2-(naphthalen-1-yl)oxazol-5(4H)-one i.e. Oxa33, synthesis of a specific GlmU inhibitor, molecular docking study, the inhibitor binds to an allosteric site of the uridyltransferase domain, overview. Oxa33 fails to inhibit cell growth even at concentrations as high as 0.150 mM. Tyr150, Glu250 and Arg 253 are in hydrogen bonding with carbonyl oxygen over the oxazole ring, while Leu144, Pro147, Phe148, Tyr150, Ala233, Ala236 and Leu247 participate in strong hydrophobic interactions with Oxa33 217820 2.7.7.23 1-(3-hydroxybenzoyl)-4-(thieno[3,2-d]pyrimidin-4-ylamino)pyridinium 38% inhibition at 0.05 mM 216137 2.7.7.23 1-[(2S,3S,4R,5S)-3,4-dihydroxy-5-(hydroxymethyl)tetrahydrofuran-2-yl]dihydropyrimidine-2,4(1H,3H)-dione - 51409 2.7.7.23 1-[2,4-dimethoxy-5-(10H-phenoxazin-10-ylsulfonyl) phenylamino]-2-(-4-pyridyl)-1-ethanone commercial inhibitor 256874 2.7.7.23 2,3-dihydroxy-5-nitrophenyl 2-acetamido-2-deoxy-alpha-D-xylo-hexopyranoside forms with UNAcP hydrogen bonds, Pi-cation and hydrophobic interactions 216286 2.7.7.23 2-(3-((4-((6,7-dimethoxyquinazolin-4-yl)amino)phenyl)carbamoyl)phenoxy)acetic acid 34% inhibition at 0.05 mM 216194 2.7.7.23 2-2-[(6-nitroquinazolin-4-yl)amino]ethoxy)-ethan-1-ol - 255152 2.7.7.23 2-amino-N-(4-((6,7-dimethoxyquinazolin-4-yl)amino)phenyl)-benzamide 16% inhibition at 0.05 mM 216255 2.7.7.23 2-hydroxy-5-nitrophenyl 2-acetamido-2-deoxy-alpha-D-xylo-hexopyranoside - 216275 2.7.7.23 2-hydroxyphenyl 2-acetamido-2-deoxy-alpha-D-xylo-hexopyranoside - 217822 2.7.7.23 2-[2-[(6-nitroquinazolin-4-yl)amino]ethoxy]-ethan-1-ol - 255276 2.7.7.23 3,4-dihydroxyphenyl 2-acetamido-2-deoxy-alpha-D-xylo-hexopyranoside - 216433 2.7.7.23 3-(cyanomethoxy)-N-(4-((6,7-dimethoxyquinazolin-4-yl)amino)-phenyl)benzamide - 216331 2.7.7.23 3-amino-N-(4-((6,7-dimethoxyquinazolin-4-yl)amino)phenyl)-benzamide 17% inhibition at 0.05 mM 216402 2.7.7.23 3-hydroxyphenyl 2-acetamido-2-deoxy-alpha-D-xylo-hexopyranoside - 216413 2.7.7.23 3-nitrophenyl 2-acetamido-2-deoxy-alpha-D-xylo-hexopyranoside - 216427 2.7.7.23 3-[(2-acetamido-2-deoxy-alpha-D-glucopyranosyl)oxy]-2-hydroxy-N-[2-[(3-hydroxypropyl)carbamoyl]phenyl]benzamide - 216335 2.7.7.23 3-[2-(1,3-benzodioxol-5-yl)-2-oxoethyl]-4-bromo-3-hydroxy-5-methyl-1,3-dihydro-2H-indol-2-one competitive inhibitor with selectivity over the human counterpart, binds at an allosteric site absent in the human homologue that prevents the conformational rearrangement required to bind UTP 212290 2.7.7.23 3-[2-(2,3-dihydro-1,4-benzodioxin-6-yl)-2-oxoethyl]-3-hydroxy-5-methyl-1,3-dihydro-2H-indol-2-one - 216383 2.7.7.23 3-[2-(2H-1,3-benzodioxol-5-yl)-2-oxoethyl]-3-hydroxy-6,7-dimethyl-1,3-dihydro-2H-indol-2-one - 217179 2.7.7.23 3-[2-(2H-1,3-benzodioxol-5-yl)-2-oxoethyl]-3-hydroxy-7-methyl-1,3-dihydro-2H-indol-2-one - 217180 2.7.7.23 3-[2-(2H-1,3-benzodioxol-5-yl)-2-oxoethyl]-4,6-dichloro-3-hydroxy-1,3-dihydro-2H-indol-2-one - 217178 2.7.7.23 3-[2H-(1,3-benzodioxol-5-yl)-2-oxoethyl]-4-bromo-3-hydroxy-5-methyl-1,3-dihydro-2H-indol-2-one UTP-competitive inhibitor with selectivity over the human counterpart despite the high level of conservation of active site residues. The inhibitor binds at an allosteric site 217823 2.7.7.23 3-[[2-acetamido-2-deoxy-alpha-D-xylo-hexopyranosyl]oxy]-2-hydroxybenzoic acid - 216353 2.7.7.23 3-[[2-acetamido-2-deoxy-alpha-L-xylo-hexopyranosyl]oxy]benzoic acid - 216354 2.7.7.23 4-(5-[(6-nitroquinazolin-4-yl)amino]-1,3,4-thiadiazol-2-yl)phenol - 255554 2.7.7.23 4-(6-nitroquinazolin-4-ylamino)benzoic acid - 255559 2.7.7.23 4-chloro-N-(3-methoxypropyl)-N-[1-(2-phenylethyl)piperidin-3-yl]benzamide a 1.9 A resolution crystal structure of this synthetic small-molecule inhibitor of GlmU is presented. The determined crystal structure indicates that the inhibitor occupies an allosteric site adjacent to the GlcNAc-1-P substrate-binding region, thus, preventing structural rearrangements that are required for the enzymatic reaction 76235 2.7.7.23 4-chloro-N-[1-[2-(2-fluorophenyl)ethyl]piperidin-3-yl]-N-(3-methoxypropyl)benzamide - 76237 2.7.7.23 4-chloro-N-[1-[2-(3-fluorophenyl)ethyl]piperidin-3-yl]-N-(3-methoxypropyl)benzamide - 76238 2.7.7.23 4-chloro-N-[1-[2-(4-fluorophenyl)ethyl]piperidin-3-yl]-N-(3-methoxypropyl)benzamide - 76239 2.7.7.23 4-fluoro-N-(3-methoxypropyl)-N-[1-(2-phenylethyl)piperidin-3-yl]benzamide - 76236 2.7.7.23 4-methyl-7-[(6-nitroquinazolin-4-yl)amino]-2H-1-benzopyran-2-one - 255607 2.7.7.23 4-[(6-nitroquinazolin-4-yl)amino]-N-(pyrimidin-2-yl)benzene-1-sulfonamide - 255635 2.7.7.23 4-[5-[(6-nitroquinazolin-4-yl)amino]-1,3,4-thiadiazol-2-yl]phenol - 255653 2.7.7.23 5'-(3-[[2-acetamido-2-deoxy-alpha-L-xylo-hexopyranosyl]oxy]-2-hydroxyanilino)-5'-deoxyuridine - 216600 2.7.7.23 5'-deoxy-5'-[[4-(3,4-dihydroxyphenyl)-1,3-thiazol-2-yl]amino]uridine 37% inhibition at 2 mM 216605 2.7.7.23 5'-[N-[2-[[2-(acetylamino)-2-deoxy-D-glucopyranosyl]oxy]acetyl]sulfamoyl]uridine 55% inhibition at 2 mM 216603 2.7.7.23 5'-[[2-(cyclohexylamino)-2-oxoethyl](2,3-dihydroxybenzoyl)amino]-5'-deoxyuridine 10% inhibition at 2 mM 216601 2.7.7.23 5'-[[N-[2-[[2-(acetylamino)-2-deoxy-alpha-D-glucopyranosyl]oxy]acetyl]-L-alpha-aspartyl-L-alpha-aspartyl]amino]-5'-deoxyuridine 60% inhibition at 2 mM 216602 2.7.7.23 5-Hydroxyuridine - 20043 2.7.7.23 6,7-dimethoxy-4-(piperazin-1-yl)quinazoline - 216744 2.7.7.23 6-nitro-N-(1,3-thiazol-2-yl)quinazolin-4-amine - 255785 2.7.7.23 6-nitro-N-(3,4,5-trimethoxyphenyl)quinazolin-4-amine - 255786 2.7.7.23 6-nitro-N-(5-phenyl-1,3,4-thiadiazol-2-yl)quinazolin-4-amine - 255787 2.7.7.23 6-nitro-N-(pyridin-2-ylmethyl)quinazolin-4-amine - 255788 2.7.7.23 6-nitro-N-[5-(4-methylphenyl)-1,3,4-thiadiazol-2-yl]quinazolin-4-amine - 255789 2.7.7.23 6-nitro-N-[5-(trifluoromethyl)-1,3,4-thiadiazol-2-yl]quinazolin-4-amine - 255790 2.7.7.23 9H-fluoren-9-ylmethyl (2S)-2-([4-[(6,7-dimethoxyquinazolin-4-yl)amino]phenyl]carbamoyl)pyrrolidine-1-carboxylate - 216773 2.7.7.23 9H-fluoren-9-ylmethyl (2S)-2-[(4-aminophenyl)carbamoyl]pyrrolidine-1-carboxylate - 216774 2.7.7.23 ATP the enzyme binds three magnesium ions and ATP at the active site, but shows no activity with ATP. ATP binding results in an inactive pre-catalytic enzyme–substrate complex, where it adopts an unusual conformation such that the reaction cannot be catalyzed 4 2.7.7.23 cyclohexyl(4-(6,7-dimethoxyquinazolin-4-yl)piperazin-1-yl)-methanone - 216777 2.7.7.23 diphosphate slight inhibition above 8 mM 17 2.7.7.23 diphosphate above 75 mM 17 2.7.7.23 diphosphate 0.5 mM, 56% reduction in activity 17 2.7.7.23 EDTA not reversible by addition of Mg2+ 21 2.7.7.23 EDTA 5 mM, 11% residual activity 21 2.7.7.23 EDTA - 21 2.7.7.23 fluoride inhibits Mg2+ but not Mn2+ activated enzyme 407 2.7.7.23 fluoride slight inhibition 407 2.7.7.23 hygromycin 0.5 mg/ml, 36% reduction in activity 49120 2.7.7.23 luteolin minimal inhibitory concentration for growth of Xanthomonas oryzae pv. oryzae, 186 microg/ml 436 2.7.7.23 Mercuric chloride - 5577 2.7.7.23 Mercuric chloride complete inactivation with 0.5 mM at 30°C, 45 min, reversible by addition of 1 mM dithiothreitol 5577 2.7.7.23 additional information N-acetylglucosamine derivative inhibitors design and synthesis, inhibitor docking studies and simulation, RMS and binding energies, overview 2 2.7.7.23 additional information displacement of MgB 2+ from its usual catalytically competent position, as noted in the crystal structure of RNA polymerase in an inactive state, is considered to be a key factor inhibiting the reaction. The entire metal-substrate complex renders the enzyme catalytically inactive 2 2.7.7.23 additional information no inhibition with terreic acid, isolated from Aspergillus terreus, the compound inhibits the acetyltransferase activity of Escherichia coli GlmU but not the uridinyltransferase activity 2 2.7.7.23 additional information no inhibition by 6624116, 5655606, 5810599, and 6012954 2 2.7.7.23 additional information TbUAP inhibitor by high-throughput screening, and structure-activity relationships, overview. No inhibition by 3 2 2.7.7.23 additional information design of bisubstrate and transition-state based inhibitors of GlmU uridyltransferase, the potential inhibitors against GlmU are initially prepared leading to the discovery of active minoquinazoline-based compounds with inhibitory potential against the uridyltransferase activity, compound synthesis, overview. No inhibition by 10, 11, 15, 16, 17, 32, and 34 2 2.7.7.23 additional information for development of potent and selective inhibitors of the uridyltransferase activity of Xanthomonas oryzae pv. oryzae GlmU, three types of target compounds are optimized and synthesized based on the Xo-GlmU structure, docking stud, and biological activity evaluation, overview 2 2.7.7.23 additional information dicumarol is unable to inhibit the N-acetylglucosamine-1-phosphate uridyltransferase activity of GlmU 2 2.7.7.23 additional information docking analysis of inhibitors, overview 2 2.7.7.23 additional information inhibitory potential of 4-aminoquinazolines as Mycobacterium tuberculosis N-acetylglucosamine-1-phosphate uridyltransferase (GlmUMTB) inhibitors, overview. Molecular docking using the crystal structure of GlmUMTB (PDB ID 3ST8), with bound substrates, N-acetylglucosamine-1-phosphate (NAcGlc-1-P) and uridine diphosphate-N-cetylglucosamine (UDP-GlcNAc). Analysis of inhibition of Mycobacterium tuberculosis wild-type strain H37Rv and of multiresistant strain MDR-MTB, antimycobacterial activity, MIC values for both strains; not inhibited by isoniazid 2 2.7.7.23 additional information terreic acid inhibits the glucosamine-1-phosphate-acetyltransferase activity of the bifunctional enzyme. Mode of inhibition studies reveal that terreic acid is competitive with AcCoA and uncompetitive with GlcN-1-phosphate. It also exhibits concentration-dependent killing of Escherichia coli strain ATCC 25922 and inhibits the growth of biofilms generated by Escherichia coli. GlmU acetyltransferase is a molecular target of terreic acid, resulting in its antibacterial activity. Terreic acid is isolated from Aspergillus terreus strain MRCJ-356. Molecular modeling 2 2.7.7.23 N'-[(4-chloro-3,5-dimethylphenoxy)acetyl]-2,4-dihydroxybenzohydrazide minimal inhibitory concentration for growth of Xanthomonas oryzae pv. oryzae, 420 microg/ml 28909 2.7.7.23 N'1,N'6-bis[2-(naphthalen-2-yloxy)acetyl]hexanedihydrazide minimal inhibitory concentration for growth of Xanthomonas oryzae pv. oryzae, 302 microg/ml 28910 2.7.7.23 N-(1-benzylpiperidin-4-yl)-6-nitroquinazolin-4-amine - 256005 2.7.7.23 N-(2,4-dimethylphenyl)-6-nitroquinazolin-4-amine - 256010 2.7.7.23 N-(2-((6,7-dimethoxyquinazolin-4-yl)amino)cyclohexyl)benzamide - 216831 2.7.7.23 N-(2-((6,7-dimethoxyquinazolin-4-yl)amino)cyclohexyl)cyclohexane carboxamide - 216832 2.7.7.23 N-(3,5-dimethoxyphenyl)-2,3-dihydro-4H-1,4-benzothiazine-4-carboxamide - 216902 2.7.7.23 N-(3-methylpiperazin-1-yl)-6-nitroquinazolin-4-amine - 256033 2.7.7.23 N-(4-((6,7-dimethoxyquinazolin-4-yl)amino)phenyl)-2-hydroxybenzamide 14% inhibition at 0.05 mM 216904 2.7.7.23 N-(4-((6,7-dimethoxyquinazolin-4-yl)amino)phenyl)-2-nitrobenzamide 13% inhibition at 0.05 mM 216905 2.7.7.23 N-(4-((6,7-dimethoxyquinazolin-4-yl)amino)phenyl)-3-(4-fluoro-phenyl)-5-methylisoxazole-4-carboxamide 19% inhibition at 0.05 mM 217821 2.7.7.23 N-(4-((6,7-dimethoxyquinazolin-4-yl)amino)phenyl)-3-hydroxybenzamide 35% inhibition at 0.05 mM 216906 2.7.7.23 N-(4-((6,7-dimethoxyquinazolin-4-yl)amino)phenyl)-3-methoxy benzamide 38% inhibition at 0.05 mM 216907 2.7.7.23 N-(4-((6,7-dimethoxyquinazolin-4-yl)amino)phenyl)-3-nitrobenzamide - 216908 2.7.7.23 N-(4-((6,7-dimethoxyquinazolin-4-yl)amino)phenyl)-4-fluorobenzamide 21% inhibition at 0.05 mM 216909 2.7.7.23 N-(4-((6,7-dimethoxyquinazolin-4-yl)amino)phenyl)-4-hydroxybenzamide 18% inhibition at 0.05 mM 216910 2.7.7.23 N-(4-((6,7-dimethoxyquinazolin-4-yl)amino)phenyl)cyclohexane carboxamide 22% inhibition at 2 mM 216911 2.7.7.23 N-(4-((6,7-dimethoxyquinazolin-4-yl)amino)phenyl)pyrazine-2-carboxamide 19% inhibition at 0.05 mM 216912 2.7.7.23 N-(4-[(6-nitroquinazolin-4-yl)amino]benzene-1-sulfonyl)acetamide - 256103 2.7.7.23 N-(5-methyl-1,3,4-thiadiazol-2-yl)-6-nitroquinazolin-4-amine - 256129 2.7.7.23 N-carbamimidoyl-4-[(6-nitroquinazolin-4-yl)-amino]benzene-1-sulfonamide compound with sulfaguanidine moiety at 4th position of quinazoline forms polar hydrogen bond with Glu 166 and Gln 205 via guanidine moiety. Lys 26 forms pi-pi stacking with the phenyl ring of sulfaguanidine and hydrogen bonding with the nitro functional g 256143 2.7.7.23 N-cyclohexyl-6-nitroquinazolin-4-amine - 256144 2.7.7.23 N-cyclopropyl-6-nitroquinazolin-4-amine - 256145 2.7.7.23 N-ethylmaleimide - 49 2.7.7.23 N-[(1R,2R,4R,6S)-6-(2,3-dihydroxy-5-nitrophenoxy)-2,3-dihydroxy-4-(hydroxymethyl)cyclohexyl]acetamide inhibitor identified by strucutre-based drug design, best binding energy of ?95.2 kcal/mol among the compounds analyzed 212289 2.7.7.23 N-[(2R,3R,4R,6R)-2-(2,3-dihydroxy-5-nitrophenoxy)-4,5-dihydroxy-6-(hydroxymethyl)tetrahydro-2H-pyran-3-yl]acetamide most active inhibitor among compounds tested, forms a hydrogen bonding network with residues Arg116, Gly381, Arg383 and Lys408, with the distance ranging from 2.9 A to and 3.14 A. The hydrophobic interaction is observed with the aromatic ring of Tyr382 with a distance of 3.85 A. The aromatic ring of the inhibitor also interacts with the Lys123 through a pi-cation interaction, with a distance of 3.99 A 172237 2.7.7.23 N-[4-[(6,7-dimethoxyquinazolin-4-yl)amino]phenyl]-3-methoxybenzamide 38% inhibition; 38% inhibition at 0.05 mM 256203 2.7.7.23 N-[4-[(6,7-dimethoxyquinazolin-4-yl)amino]phenyl]benzamide 44% inhibition at 2 mM 216967 2.7.7.23 N-[4-[(6,7-dimethoxyquinazolin-4-yl)amino]phenyl]benzamide 44% inhibition; 44% inhibition at 0.05 mM 216967 2.7.7.23 N-[4-[(6-nitroquinazolin-4-yl)amino]benzene-1-sulfonyl]acetamide - 256204 2.7.7.23 N-[4-[(7-hydroxy-6-methoxyquinazolin-4-yl)amino]phenyl]benzamide 36% inhibition at 2 mM 216968 2.7.7.23 N-[4-[(7-hydroxy-6-methoxyquinazolin-4-yl)amino]phenyl]benzamide 36% inhibition; 36% inhibition at 0.05 mM 216968 2.7.7.23 N-[5-(2-chlorophenyl)-1,3,4-thiadiazol-2-yl]-6-nitroquinazolin-4-amine - 256220 2.7.7.23 N1',N3'-bis(2-(1-bromonaphthalen naphthalen-2-yloxy)acetyl)isophthalohydrazide - 217029 2.7.7.23 N1',N3'-bis(2-(3-bromonaphthalen naphthalen-2-yloxy)acetyl)isophthalohydrazide - 217030 2.7.7.23 N1',N3'-bis(2-(6-bromonaphthalen naphthalen-2-yloxy)acetyl)isophthalohydrazide - 217031 2.7.7.23 N1',N3'-bis(2-(naphthalen-2-yloxy)acetyl) isophthalohydrazide - 217032 2.7.7.23 N1',N4'-bis(2-(1-bromonaphthalen naphthalen-2-yloxy)acetyl)succinohydrazide - 217033 2.7.7.23 N1',N4'-bis(2-(3-bromonaphthalen naphthalen-2-yloxy)acetyl)succinohydrazide - 217034 2.7.7.23 N1',N4'-bis(2-(6-bromonaphthalen naphthalen-2-yloxy)acetyl)succinohydrazide - 217035 2.7.7.23 N1',N4'-bis(2-(naphthalen-2-yloxy)acetyl) succinohydrazide - 217036 2.7.7.23 N1',N6'-bis(2-(1-bromonaphthalen naphthalen-2-yloxy)acetyl)adipohydrazide - 217037 2.7.7.23 N1',N6'-bis(2-(3-bromonaphthalen naphthalen-2-yloxy)acetyl)adipohydrazide - 217038 2.7.7.23 N1',N6'-bis(2-(6-bromonaphthalen naphthalen-2-yloxy)acetyl)adipohydrazide - 217039 2.7.7.23 N1',N6'-bis(2-(naphthalen-2-yloxy)acetyl)adipohydrazide - 217040 2.7.7.23 N1-(6,7-dimethoxyquinazolin-4-yl)benzene-1,4-diamine 14% inhibition at 2 mM 217026 2.7.7.23 N1-(6,7-dimethoxyquinazolin-4-yl)cyclohexane-1,2-diamine - 217027 2.7.7.23 N1-(6-nitroquinazolin-4-yl)benzene-1,2-diamine - 256226 2.7.7.23 p-chloromercuribenzoate completely reversible with cysteine 43 2.7.7.23 p-chloromercuribenzoate - 43 2.7.7.23 pseudouridine - 7276 2.7.7.23 rifampicin - 3669 2.7.7.23 streptomycin 0.5 mg/ml, 74% reduction in activity 2358 2.7.7.23 tert-butyl (2S,4S)-2-([4-[(6,7-dimethoxyquinazolin-4-yl)amino]phenyl]carbamoyl)-4-hydroxypyrrolidine-1-carboxylate - 217049 2.7.7.23 UDP-N-acetyl-D-glucosamine slight product inhibition in reverse reaction 126 2.7.7.23 UMP inhibits catabolic reaction 133 2.7.7.23 uridine - 261 2.7.7.23 uridine competitive with diphosphate, noncompetitive with UDP-N-acetyl-D-glucosamine, activity could be restored by dialysis 261 2.7.7.23 ZINC70672706 interaction analysis 256878 2.7.7.23 ZINC85867098 interaction analysis 256875 2.7.7.23 ZINC95098775 interaction analysis 256879 2.7.7.23 ZINC95098837 interaction analysis 256876 2.7.7.23 ZINC95098867 interaction analysis 256877 2.7.7.23 [4-[(6,7-dimethoxyquinazolin-4-yl)amino]phenyl](3-hydroxyphenyl)methanone 7% inhibition at 0.05 mM 216121