2.7.7.23: UDP-N-acetylglucosamine diphosphorylase
This is an abbreviated version!
For detailed information about UDP-N-acetylglucosamine diphosphorylase, go to the full flat file.
Word Map on EC 2.7.7.23
Reaction
Synonyms
acetylglucosamine 1-phosphate uridylyltransferase, AGX-1, AGX1, AGX2, amino-sugar-1-phosphate acetyltransferase, bifunctional N-acetyltransferase/uridylyltransferase, BmUAP, CL6EHI_021200, CL6EHI_039830, EcGlmU, EnhiA.01126.a, EnhiA.01126.b, GlcNAc-1-P uridyltransferase, GlcNAc-1-P UTase, GlcNAc-1-phosphate nucleotidylyltransferase, GLCNAC1PUT1, GLCNAC1PUT2, GlmU, GlmUMTB, hiGlmU, LmUAP1, LmUAP2, LOC_Os08g10600, Mmy, More, mummy, N-acetyl-D-glucosamine-1-phosphate uridylyltransferase, N-acetyl-glucosamine-1-phosphate uridyltransferase, N-acetylglucosamine 1-phosphate uridyltransferase, N-acetylglucosamine-1-phosphate uridyltransferase, N-acetylglucosamine-1-phosphate uridylyltransferase, N-acetylglucosamine-1-phosphate-uridyltransferase/glucosamine-1-phosphate-acetyltransferase, Os08g10600, Rv1018c, spl29, spotted leaf 29, ST0452, ST0452 protein, STK_04520, Tb11.02.0120, UAP, UAP enzyme, UAP1, UAP2, UDP N-acetylglucosamine pyrophosphorylases 1, UDP N-acetylglucosamine pyrophosphorylases 2, UDP-GlcNAc pyrophosphorylase, UDP-GlcNAc pyrophosphorylase (UAP), UDP-HexNAc pyrophosphorylase, UDP-N-acetylgalactosamine pyrophosphorylase, UDP-N-acetylglucosamine diphosphorylase 1, UDP-N-acetylglucosamine diphosphorylase 2, UDP-N-acetylglucosamine pyrophosphorylase, UDP-N-acetylglucosamine pyrophosphorylase (UAP), UDP-N-acetylglucosamine pyrophosphorylase 1, UDP-N-acetylglucosamine pyrophosphorylase/glucosamine-1-phosphate N-acetyltransferase, UDP-N-acetylglucosamine-diphosphorylase, UDP-N-acetylhexosamine pyrophosphorylase, UDPacetylglucosamine pyrophosphorylase, UNAcP, uridine diphosphate N-acetylglucosamine pyrophosphorylase, uridine diphosphate-N-acetylglucosamine pyrophosphorylase, uridine diphosphoacetylglucosamine phosphorylase, uridine diphosphoacetylglucosamine pyrophosphorylase, uridine-diphospho-N-acetylglucosamine pyrophosphorylase, UTP:2-acetamido-2-deoxy-alpha-D-glucose-1-phosphate uridylyltransferase, UTP:N-acetylglucosamine-1-P uridylyltransferase, Ydl103c protein
ECTree
2.7.7.23 UDP-N-acetylglucosamine diphosphorylaseAdvanced search results
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results (Inhibitors
Inhibitors on EC 2.7.7.23 - UDP-N-acetylglucosamine diphosphorylase
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INHIBITOR 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
IMAGE
(2S,4R)-N-(4-((6,7-dimethoxyquinazolin-4-yl)amino)phenyl)-4-hydroxypyrrolidine-2-carboxamide
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(3-hydroxyphenyl)[4-(5,6,7,8-tetrahydroquinazolin-4-ylamino)phenyl]methanone
30% inhibition at 0.05 mM
(4-(6,7-dimethoxyquinazolin-4-yl)piperazin-1-yl)(phenyl)-methanone
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(S)-N-(4-((6,7-dimethoxyquinazolin-4-yl)amino)phenyl)pyrrolidine-2-carboxamide
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(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
1-(3-hydroxybenzoyl)-4-(thieno[3,2-d]pyrimidin-4-ylamino)pyridinium
38% inhibition at 0.05 mM
1-[(2S,3S,4R,5S)-3,4-dihydroxy-5-(hydroxymethyl)tetrahydrofuran-2-yl]dihydropyrimidine-2,4(1H,3H)-dione
1-[2,4-dimethoxy-5-(10H-phenoxazin-10-ylsulfonyl) phenylamino]-2-(-4-pyridyl)-1-ethanone
commercial inhibitor
2,3-dihydroxy-5-nitrophenyl 2-acetamido-2-deoxy-alpha-D-xylo-hexopyranoside
forms with UNAcP hydrogen bonds, Pi-cation and hydrophobic interactions
2-(3-((4-((6,7-dimethoxyquinazolin-4-yl)amino)phenyl)carbamoyl)phenoxy)acetic acid
34% inhibition at 0.05 mM
2-amino-N-(4-((6,7-dimethoxyquinazolin-4-yl)amino)phenyl)-benzamide
16% inhibition at 0.05 mM
2-hydroxy-5-nitrophenyl 2-acetamido-2-deoxy-alpha-D-xylo-hexopyranoside
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2-hydroxyphenyl 2-acetamido-2-deoxy-alpha-D-xylo-hexopyranoside
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3,4-dihydroxyphenyl 2-acetamido-2-deoxy-alpha-D-xylo-hexopyranoside
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3-(cyanomethoxy)-N-(4-((6,7-dimethoxyquinazolin-4-yl)amino)-phenyl)benzamide
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3-amino-N-(4-((6,7-dimethoxyquinazolin-4-yl)amino)phenyl)-benzamide
17% inhibition at 0.05 mM
3-hydroxyphenyl 2-acetamido-2-deoxy-alpha-D-xylo-hexopyranoside
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3-nitrophenyl 2-acetamido-2-deoxy-alpha-D-xylo-hexopyranoside
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3-[(2-acetamido-2-deoxy-alpha-D-glucopyranosyl)oxy]-2-hydroxy-N-[2-[(3-hydroxypropyl)carbamoyl]phenyl]benzamide
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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
3-[2-(2,3-dihydro-1,4-benzodioxin-6-yl)-2-oxoethyl]-3-hydroxy-5-methyl-1,3-dihydro-2H-indol-2-one
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3-[2-(2H-1,3-benzodioxol-5-yl)-2-oxoethyl]-3-hydroxy-6,7-dimethyl-1,3-dihydro-2H-indol-2-one
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3-[2-(2H-1,3-benzodioxol-5-yl)-2-oxoethyl]-3-hydroxy-7-methyl-1,3-dihydro-2H-indol-2-one
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3-[2-(2H-1,3-benzodioxol-5-yl)-2-oxoethyl]-4,6-dichloro-3-hydroxy-1,3-dihydro-2H-indol-2-one
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3-[2H-(1,3-benzodioxol-5-yl)-2-oxoethyl]-4-bromo-3-hydroxy-5-methyl-1,3-dihydro-2H-indol-2-one
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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
3-[[2-acetamido-2-deoxy-alpha-D-xylo-hexopyranosyl]oxy]-2-hydroxybenzoic acid
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3-[[2-acetamido-2-deoxy-alpha-L-xylo-hexopyranosyl]oxy]benzoic acid
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4-(5-[(6-nitroquinazolin-4-yl)amino]-1,3,4-thiadiazol-2-yl)phenol
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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
4-chloro-N-[1-[2-(2-fluorophenyl)ethyl]piperidin-3-yl]-N-(3-methoxypropyl)benzamide
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4-chloro-N-[1-[2-(3-fluorophenyl)ethyl]piperidin-3-yl]-N-(3-methoxypropyl)benzamide
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4-chloro-N-[1-[2-(4-fluorophenyl)ethyl]piperidin-3-yl]-N-(3-methoxypropyl)benzamide
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4-fluoro-N-(3-methoxypropyl)-N-[1-(2-phenylethyl)piperidin-3-yl]benzamide
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4-methyl-7-[(6-nitroquinazolin-4-yl)amino]-2H-1-benzopyran-2-one
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4-[(6-nitroquinazolin-4-yl)amino]-N-(pyrimidin-2-yl)benzene-1-sulfonamide
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4-[5-[(6-nitroquinazolin-4-yl)amino]-1,3,4-thiadiazol-2-yl]phenol
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5'-(3-[[2-acetamido-2-deoxy-alpha-L-xylo-hexopyranosyl]oxy]-2-hydroxyanilino)-5'-deoxyuridine
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5'-deoxy-5'-[[4-(3,4-dihydroxyphenyl)-1,3-thiazol-2-yl]amino]uridine
37% inhibition at 2 mM
5'-[N-[2-[[2-(acetylamino)-2-deoxy-D-glucopyranosyl]oxy]acetyl]sulfamoyl]uridine
55% inhibition at 2 mM
5'-[[2-(cyclohexylamino)-2-oxoethyl](2,3-dihydroxybenzoyl)amino]-5'-deoxyuridine
10% inhibition at 2 mM
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
6-nitro-N-(5-phenyl-1,3,4-thiadiazol-2-yl)quinazolin-4-amine
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6-nitro-N-[5-(4-methylphenyl)-1,3,4-thiadiazol-2-yl]quinazolin-4-amine
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6-nitro-N-[5-(trifluoromethyl)-1,3,4-thiadiazol-2-yl]quinazolin-4-amine
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9H-fluoren-9-ylmethyl (2S)-2-([4-[(6,7-dimethoxyquinazolin-4-yl)amino]phenyl]carbamoyl)pyrrolidine-1-carboxylate
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9H-fluoren-9-ylmethyl (2S)-2-[(4-aminophenyl)carbamoyl]pyrrolidine-1-carboxylate
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ATP
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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 enzymesubstrate complex, where it adopts an unusual conformation such that the reaction cannot be catalyzed
cyclohexyl(4-(6,7-dimethoxyquinazolin-4-yl)piperazin-1-yl)-methanone
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luteolin
minimal inhibitory concentration for growth of Xanthomonas oryzae pv. oryzae, 186 microg/ml
N'-[(4-chloro-3,5-dimethylphenoxy)acetyl]-2,4-dihydroxybenzohydrazide
minimal inhibitory concentration for growth of Xanthomonas oryzae pv. oryzae, 420 microg/ml
N'1,N'6-bis[2-(naphthalen-2-yloxy)acetyl]hexanedihydrazide
minimal inhibitory concentration for growth of Xanthomonas oryzae pv. oryzae, 302 microg/ml
N-(2-((6,7-dimethoxyquinazolin-4-yl)amino)cyclohexyl)benzamide
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N-(2-((6,7-dimethoxyquinazolin-4-yl)amino)cyclohexyl)cyclohexane carboxamide
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N-(3,5-dimethoxyphenyl)-2,3-dihydro-4H-1,4-benzothiazine-4-carboxamide
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N-(4-((6,7-dimethoxyquinazolin-4-yl)amino)phenyl)-2-hydroxybenzamide
14% inhibition at 0.05 mM
N-(4-((6,7-dimethoxyquinazolin-4-yl)amino)phenyl)-2-nitrobenzamide
13% inhibition at 0.05 mM
N-(4-((6,7-dimethoxyquinazolin-4-yl)amino)phenyl)-3-(4-fluoro-phenyl)-5-methylisoxazole-4-carboxamide
19% inhibition at 0.05 mM
N-(4-((6,7-dimethoxyquinazolin-4-yl)amino)phenyl)-3-hydroxybenzamide
35% inhibition at 0.05 mM
N-(4-((6,7-dimethoxyquinazolin-4-yl)amino)phenyl)-3-methoxy benzamide
38% inhibition at 0.05 mM
N-(4-((6,7-dimethoxyquinazolin-4-yl)amino)phenyl)-3-nitrobenzamide
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N-(4-((6,7-dimethoxyquinazolin-4-yl)amino)phenyl)-4-fluorobenzamide
21% inhibition at 0.05 mM
N-(4-((6,7-dimethoxyquinazolin-4-yl)amino)phenyl)-4-hydroxybenzamide
18% inhibition at 0.05 mM
N-(4-((6,7-dimethoxyquinazolin-4-yl)amino)phenyl)cyclohexane carboxamide
22% inhibition at 2 mM
N-(4-((6,7-dimethoxyquinazolin-4-yl)amino)phenyl)pyrazine-2-carboxamide
19% inhibition at 0.05 mM
N-(4-[(6-nitroquinazolin-4-yl)amino]benzene-1-sulfonyl)acetamide
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N-(5-methyl-1,3,4-thiadiazol-2-yl)-6-nitroquinazolin-4-amine
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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
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
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
N-[4-[(6,7-dimethoxyquinazolin-4-yl)amino]phenyl]-3-methoxybenzamide
38% inhibition; 38% inhibition at 0.05 mM
N-[4-[(6-nitroquinazolin-4-yl)amino]benzene-1-sulfonyl]acetamide
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N-[5-(2-chlorophenyl)-1,3,4-thiadiazol-2-yl]-6-nitroquinazolin-4-amine
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N1',N3'-bis(2-(1-bromonaphthalen naphthalen-2-yloxy)acetyl)isophthalohydrazide
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N1',N3'-bis(2-(3-bromonaphthalen naphthalen-2-yloxy)acetyl)isophthalohydrazide
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N1',N3'-bis(2-(6-bromonaphthalen naphthalen-2-yloxy)acetyl)isophthalohydrazide
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N1',N3'-bis(2-(naphthalen-2-yloxy)acetyl) isophthalohydrazide
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N1',N4'-bis(2-(1-bromonaphthalen naphthalen-2-yloxy)acetyl)succinohydrazide
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N1',N4'-bis(2-(3-bromonaphthalen naphthalen-2-yloxy)acetyl)succinohydrazide
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N1',N4'-bis(2-(6-bromonaphthalen naphthalen-2-yloxy)acetyl)succinohydrazide
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N1',N6'-bis(2-(1-bromonaphthalen naphthalen-2-yloxy)acetyl)adipohydrazide
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N1',N6'-bis(2-(3-bromonaphthalen naphthalen-2-yloxy)acetyl)adipohydrazide
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N1',N6'-bis(2-(6-bromonaphthalen naphthalen-2-yloxy)acetyl)adipohydrazide
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N1-(6,7-dimethoxyquinazolin-4-yl)benzene-1,4-diamine
14% inhibition at 2 mM
tert-butyl (2S,4S)-2-([4-[(6,7-dimethoxyquinazolin-4-yl)amino]phenyl]carbamoyl)-4-hydroxypyrrolidine-1-carboxylate
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[4-[(6,7-dimethoxyquinazolin-4-yl)amino]phenyl](3-hydroxyphenyl)methanone
7% inhibition at 0.05 mM
1-[(2S,3S,4R,5S)-3,4-dihydroxy-5-(hydroxymethyl)tetrahydrofuran-2-yl]dihydropyrimidine-2,4(1H,3H)-dione
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1-[(2S,3S,4R,5S)-3,4-dihydroxy-5-(hydroxymethyl)tetrahydrofuran-2-yl]dihydropyrimidine-2,4(1H,3H)-dione
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Mercuric chloride
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complete inactivation with 0.5 mM at 30°C, 45 min, reversible by addition of 1 mM dithiothreitol
N-[4-[(6,7-dimethoxyquinazolin-4-yl)amino]phenyl]benzamide
44% inhibition at 2 mM
N-[4-[(6,7-dimethoxyquinazolin-4-yl)amino]phenyl]benzamide
44% inhibition; 44% inhibition at 0.05 mM
N-[4-[(7-hydroxy-6-methoxyquinazolin-4-yl)amino]phenyl]benzamide
36% inhibition at 2 mM
N-[4-[(7-hydroxy-6-methoxyquinazolin-4-yl)amino]phenyl]benzamide
36% inhibition; 36% inhibition at 0.05 mM
uridine
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competitive with diphosphate, noncompetitive with UDP-N-acetyl-D-glucosamine, activity could be restored by dialysis
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
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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
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additional information
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N-acetylglucosamine derivative inhibitors design and synthesis, inhibitor docking studies and simulation, RMS and binding energies, overview
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additional information
N-acetylglucosamine derivative inhibitors design and synthesis, inhibitor docking studies and simulation, RMS and binding energies, overview
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additional information
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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
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additional information
no inhibition by 6624116, 5655606, 5810599, and 6012954
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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
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additional information
dicumarol is unable to inhibit the N-acetylglucosamine-1-phosphate uridyltransferase activity of GlmU
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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
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additional information
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TbUAP inhibitor by high-throughput screening, and structure-activity relationships, overview. No inhibition by 3
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additional information
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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
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