Information on EC 2.7.7.23 - UDP-N-acetylglucosamine diphosphorylase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea

EC NUMBER
COMMENTARY hide
2.7.7.23
-
RECOMMENDED NAME
GeneOntology No.
UDP-N-acetylglucosamine diphosphorylase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate = diphosphate + UDP-N-acetyl-alpha-D-glucosamine
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
nucleotidyl group transfer
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
UDP-N-acetyl-D-glucosamine biosynthesis I
-
-
anhydromuropeptides recycling I
-
-
UDP-N-acetyl-D-glucosamine biosynthesis II
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-
UDP-N-acetyl-D-galactosamine biosynthesis II
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-
UDP-GlcNAc biosynthesis
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Amino sugar and nucleotide sugar metabolism
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Metabolic pathways
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Biosynthesis of antibiotics
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SYSTEMATIC NAME
IUBMB Comments
UTP:N-acetyl-alpha-D-glucosamine-1-phosphate uridylyltransferase
Part of the pathway for acetamido sugar biosynthesis in bacteria and archaea. The enzyme from several bacteria (e.g., Escherichia coli, Bacillus subtilis and Haemophilus influenzae) has been shown to be bifunctional and also to possess the activity of EC 2.3.1.157, glucosamine-1-phosphate N-acetyltransferase [3,4,6]. The enzyme from plants and animals is also active toward N-acetyl-alpha-D-galactosamine 1-phosphate (cf. EC 2.7.7.83, UDP-N-acetylgalactosamine diphosphorylase) [5,7], while the bacterial enzyme shows low activity toward that substrate [4].
CAS REGISTRY NUMBER
COMMENTARY hide
9023-06-7
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
calf
-
-
Manually annotated by BRENDA team
Escherichia coli K-12
Uniprot
Manually annotated by BRENDA team
-
KT282116, KT282117
Genbank
Manually annotated by BRENDA team
strains MS11-A42 and MS11-F3
SwissProt
Manually annotated by BRENDA team
strain IFO 6178
-
-
Manually annotated by BRENDA team
; SPL29; cvs. Guangzhan63s, 10N056, Yuehui9113, and Zhonghua 11
UniProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
bifunctional UDP-N-acetylglucosamine diphosphorylase, EC 2.7.7.23, and glucosamine-1-phosphate N-acetyltransferase, EC 2.3.1.157
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
CTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + CDP-N-acetyl-alpha-D-glucosamine
show the reaction diagram
-
-
-
-
?
diphosphate + UDP-glucose
UTP + D-glucose 1-phosphate
show the reaction diagram
diphosphate + UDP-N-acetyl-D-galactosamine
UTP + N-acetyl-alpha-D-galactosamine 1-phosphate
show the reaction diagram
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
show the reaction diagram
N-acetyl-4-deoxy-alpha-D-glucosamine 1-phosphate + UTP
UDP-N-acetyl-4-deoxy-alpha-D-glucosamine + diphosphate
show the reaction diagram
-
-
yield: 59%
-
?
N-acetyl-6-deoxy-6-azido-alpha-D-glucosamine 1-phosphate + UTP
UDP-N-acetyl-6-deoxy-6-azido-alpha-D-glucosamine + diphosphate
show the reaction diagram
-
-
yield: 20%
-
?
N-acetyl-6-deoxy-alpha-D-galactosamine 1-phosphate + UTP
UDP-N-acetyl-6-deoxy-alpha-D-galactosamine + diphosphate
show the reaction diagram
-
-
yield: 55%
-
?
N-acetyl-6-deoxy-alpha-D-glucosamine 1-phosphate + UTP
UDP-N-acetyl-6-deoxy-alpha-D-glucosamine + diphosphate
show the reaction diagram
-
-
yield: 50%
-
?
N-acetyl-alpha-D-allopyranosylamine 1-phosphate + UTP
UDP-N-acetyl-alpha-D-allopyranosylamine + diphosphate
show the reaction diagram
-
-
yield: 20%
-
?
N-acetyl-alpha-D-galactosamine 1-phosphate + UTP
UDP-N-acetyl-alpha-D-galactosamine + diphosphate
show the reaction diagram
-
-
yield: 65%
-
?
N-acetyl-alpha-D-glucosamine 1-phosphate + UTP
UDP-N-acetyl-alpha-D-glucosamine + diphosphate
show the reaction diagram
N-acetyl-D-glucosamine 1-phosphate + UTP
UDP-N-acetyl-D-glucosamine + diphosphate
show the reaction diagram
N-acetylglucosamine 1-phosphate + uridine 5'-triphosphate
uridine-diphospho-N-acetylglucosamine + diphosphate
show the reaction diagram
-
-
-
-
r
N-azidoacetyl-alpha-D-glucosamine 1-phosphate + UTP
UDP-N-azidoacetyl-alpha-D-glucosamine + diphosphate
show the reaction diagram
-
-
yield: 44%
-
?
N-butanoyl-alpha-D-glucosamine 1-phosphate + UTP
UDP-N-butanoyl-alpha-D-glucosamine + diphosphate
show the reaction diagram
-
-
yield: 27%
-
?
N-propanoyl-alpha-D-galactosamine 1-phosphate + UTP
UDP-N-propanoyl-alpha-D-galactosamine + diphosphate
show the reaction diagram
-
-
yield: 10%
-
?
N-propanoyl-alpha-D-glucosamine 1-phosphate + UTP
UDP-N-propanoyl-alpha-D-glucosamine + diphosphate
show the reaction diagram
-
-
yield: 57%
-
?
UDP-N-acetyl-D-galactosamine + diphosphate
N-acetyl-D-galactosamine 1-phosphate + UTP
show the reaction diagram
-
-
-
r
UDP-N-acetyl-D-glucosamine + diphosphate
N-acetyl-D-glucosamine 1-phosphate + UTP
show the reaction diagram
-
-
-
r
UTP + N-acetyl-alpha-D-galactosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-galactosamine
show the reaction diagram
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
show the reaction diagram
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-D-glucosamine
show the reaction diagram
UTP + N-acetylglucosamine 1-phosphate
diphosphate + UDP-N-acetyl-D-glucosamine
show the reaction diagram
-
-
-
?
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
show the reaction diagram
N-acetyl-D-glucosamine 1-phosphate + UTP
UDP-N-acetyl-D-glucosamine + diphosphate
show the reaction diagram
-
-
-
-
?
N-acetylglucosamine 1-phosphate + uridine 5'-triphosphate
uridine-diphospho-N-acetylglucosamine + diphosphate
show the reaction diagram
-
-
-
-
r
UTP + N-acetyl-alpha-D-galactosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-galactosamine
show the reaction diagram
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
show the reaction diagram
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-D-glucosamine
show the reaction diagram
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(2S,4R)-N-(4-((6,7-dimethoxyquinazolin-4-yl)amino)phenyl)-4-hydroxypyrrolidine-2-carboxamide
-
-
(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
-
-
-
(S)-N-(4-((6,7-dimethoxyquinazolin-4-yl)amino)phenyl)pyrrolidine-2-carboxamide
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1-(3-hydroxybenzoyl)-4-(thieno[3,2-d]pyrimidin-4-ylamino)pyridinium
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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
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
-
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
-
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
-
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
-
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
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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-(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
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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
-
4-chloro-N-[1-[2-(4-fluorophenyl)ethyl]piperidin-3-yl]-N-(3-methoxypropyl)benzamide
-
4-fluoro-N-(3-methoxypropyl)-N-[1-(2-phenylethyl)piperidin-3-yl]benzamide
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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
5-Hydroxyuridine
6,7-dimethoxy-4-(piperazin-1-yl)quinazoline
-
-
9H-fluoren-9-ylmethyl (2S)-2-([4-[(6,7-dimethoxyquinazolin-4-yl)amino]phenyl]carbamoyl)pyrrolidine-1-carboxylate
-
-
9H-fluoren-9-ylmethyl (2S)-2-[(4-aminophenyl)carbamoyl]pyrrolidine-1-carboxylate
-
-
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 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
-
-
diphosphate
fluoride
hygromycin
0.5 mg/ml, 36% reduction in activity
luteolin
minimal inhibitory concentration for growth of Xanthomonas oryzae pv. oryzae, 186 microg/ml
Mercuric chloride
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
-
-
N-(2-((6,7-dimethoxyquinazolin-4-yl)amino)cyclohexyl)cyclohexane carboxamide
-
-
N-(3,5-dimethoxyphenyl)-2,3-dihydro-4H-1,4-benzothiazine-4-carboxamide
-
-
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
-
-
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-ethylmaleimide
-
-
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]benzamide
-
44% inhibition at 2 mM
N-[4-[(7-hydroxy-6-methoxyquinazolin-4-yl)amino]phenyl]benzamide
-
36% inhibition at 2 mM
N1',N3'-bis(2-(1-bromonaphthalen naphthalen-2-yloxy)acetyl)isophthalohydrazide
-
-
N1',N3'-bis(2-(3-bromonaphthalen naphthalen-2-yloxy)acetyl)isophthalohydrazide
-
-
N1',N3'-bis(2-(6-bromonaphthalen naphthalen-2-yloxy)acetyl)isophthalohydrazide
-
-
N1',N3'-bis(2-(naphthalen-2-yloxy)acetyl) isophthalohydrazide
-
-
N1',N4'-bis(2-(1-bromonaphthalen naphthalen-2-yloxy)acetyl)succinohydrazide
-
-
N1',N4'-bis(2-(3-bromonaphthalen naphthalen-2-yloxy)acetyl)succinohydrazide
-
-
N1',N4'-bis(2-(6-bromonaphthalen naphthalen-2-yloxy)acetyl)succinohydrazide
-
-
N1',N4'-bis(2-(naphthalen-2-yloxy)acetyl) succinohydrazide
-
-
N1',N6'-bis(2-(1-bromonaphthalen naphthalen-2-yloxy)acetyl)adipohydrazide
-
-
N1',N6'-bis(2-(3-bromonaphthalen naphthalen-2-yloxy)acetyl)adipohydrazide
-
-
N1',N6'-bis(2-(6-bromonaphthalen naphthalen-2-yloxy)acetyl)adipohydrazide
-
-
N1',N6'-bis(2-(naphthalen-2-yloxy)acetyl)adipohydrazide
-
-
N1-(6,7-dimethoxyquinazolin-4-yl)benzene-1,4-diamine
-
14% inhibition at 2 mM
N1-(6,7-dimethoxyquinazolin-4-yl)cyclohexane-1,2-diamine
-
-
p-chloromercuribenzoate
pseudouridine
streptomycin
0.5 mg/ml, 74% reduction in activity
tert-butyl (2S,4S)-2-([4-[(6,7-dimethoxyquinazolin-4-yl)amino]phenyl]carbamoyl)-4-hydroxypyrrolidine-1-carboxylate
-
-
UDP-N-acetyl-D-glucosamine
-
slight product inhibition in reverse reaction
UMP
-
inhibits catabolic reaction
uridine
[4-[(6,7-dimethoxyquinazolin-4-yl)amino]phenyl](3-hydroxyphenyl)methanone
-
7% inhibition at 0.05 mM
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-mercaptoethanol
-
slight stimulation
D-glucosamine 6-phosphate
-
allosteric, 0.003 mM, 5fold increase of activity, reversible by dialysis
dithioerythritol
dithiothreitol
glutathione
-
slight stimulation
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
5.8
D-glucose 1-phosphate
-
pH 7.5, 37C, 5 mM UTP
0.016 - 5.4
diphosphate
0.008 - 0.061
N-acetyl-alpha-D-glucosamine 1-phosphate
0.38 - 1.3
N-acetyl-D-galactosamine 1-phosphate
0.011 - 2.25
N-acetyl-D-glucosamine 1-phosphate
6.3
UDP-D-glucose
-
pH 8.5, 37C, 5 mM diphosphate
0.016
UDP-N-acetyl-alpha-D-glucosamine
-
pH 7.5, 80C
0.808 - 2.768
UDP-N-acetyl-D-galactosamine
0.065 - 6.1
UDP-N-acetyl-D-glucosamine
0.0017 - 1.21
UTP
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
6.21
diphosphate
-
pH 7.5, 80C
0.95 - 2.54
N-acetyl-alpha-D-glucosamine 1-phosphate
0.015 - 330
N-acetyl-D-glucosamine 1-phosphate
8.4
UDP-N-acetyl-alpha-D-glucosamine
-
pH 7.5, 80C
44.3
UDP-N-acetyl-D-glucosamine
-
-
0.75 - 3.53
UTP
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
380
diphosphate
-
pH 7.5, 80C
320
N-acetyl-alpha-D-glucosamine 1-phosphate
-
pH 7.5, 80C
110 - 160
N-acetyl-D-glucosamine 1-phosphate
530
UDP-N-acetyl-alpha-D-glucosamine
-
pH 7.5, 80C
15 - 18
UDP-N-acetyl-D-galactosamine
220 - 460
UDP-N-acetyl-D-glucosamine
120 - 2120
UTP
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00044 - 0.00099
luteolin
0.0089 - 0.0194
N'-[(4-chloro-3,5-dimethylphenoxy)acetyl]-2,4-dihydroxybenzohydrazide
0.0081
N'1,N'6-bis[2-(naphthalen-2-yloxy)acetyl]hexanedihydrazide
substrate N-acetyl-alpha-D-glucosamine 1-phosphate, pH 7.5, 37C; substrate UTP, pH 7.5, 37C
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.037
3-[2-(1,3-benzodioxol-5-yl)-2-oxoethyl]-4-bromo-3-hydroxy-5-methyl-1,3-dihydro-2H-indol-2-one
Trypanosoma brucei brucei
Q386Q8
pH not specified in the publication, temperature not specified in the publication
0.037
3-[2H-(1,3-benzodioxol-5-yl)-2-oxoethyl]-4-bromo-3-hydroxy-5-methyl-1,3-dihydro-2H-indol-2-one
Trypanosoma brucei
-
pH 7.5, temperature not specified in the publication
-
0.00996
4-(4-(benzyloxy)benzylidene-2)-(naphthalen-1-yl)oxazol-5(4H)-one
Mycobacterium tuberculosis
-
pH 7.4, 37C
-
0.018
4-chloro-N-(3-methoxypropyl)-N-[1-(2-phenylethyl)piperidin-3-yl]benzamide
Haemophilus influenzae
P43889
-
0.1
4-chloro-N-[1-[2-(2-fluorophenyl)ethyl]piperidin-3-yl]-N-(3-methoxypropyl)benzamide
Haemophilus influenzae
P43889
value above
0.1
4-chloro-N-[1-[2-(3-fluorophenyl)ethyl]piperidin-3-yl]-N-(3-methoxypropyl)benzamide
Haemophilus influenzae
P43889
value above
0.089
4-chloro-N-[1-[2-(4-fluorophenyl)ethyl]piperidin-3-yl]-N-(3-methoxypropyl)benzamide
Haemophilus influenzae
P43889
-
0.02
4-fluoro-N-(3-methoxypropyl)-N-[1-(2-phenylethyl)piperidin-3-yl]benzamide
Haemophilus influenzae
P43889
-
0.00081
luteolin
Xanthomonas oryzae pv. oryzae
Q2P7P9
pH 7.5, 37C
0.023
N'-[(4-chloro-3,5-dimethylphenoxy)acetyl]-2,4-dihydroxybenzohydrazide
Xanthomonas oryzae pv. oryzae
Q2P7P9
pH 7.5, 37C
0.014
N'1,N'6-bis[2-(naphthalen-2-yloxy)acetyl]hexanedihydrazide
Xanthomonas oryzae pv. oryzae
Q2P7P9
pH 7.5, 37C
0.049
N-(3,5-dimethoxyphenyl)-2,3-dihydro-4H-1,4-benzothiazine-4-carboxamide
Trypanosoma brucei
-
pH 7.5, temperature not specified in the publication
0.074
N-(4-((6,7-dimethoxyquinazolin-4-yl)amino)phenyl)-3-hydroxybenzamide
Mycobacterium tuberculosis
-
pH 7.6, 37C
0.0108
N1',N3'-bis(2-(1-bromonaphthalen naphthalen-2-yloxy)acetyl)isophthalohydrazide
Xanthomonas oryzae pv. oryzae
-
pH 7.5, 37C
0.0184
N1',N3'-bis(2-(3-bromonaphthalen naphthalen-2-yloxy)acetyl)isophthalohydrazide
Xanthomonas oryzae pv. oryzae
-
pH 7.5, 37C
0.0134
N1',N3'-bis(2-(6-bromonaphthalen naphthalen-2-yloxy)acetyl)isophthalohydrazide
Xanthomonas oryzae pv. oryzae
-
pH 7.5, 37C
0.0138
N1',N3'-bis(2-(naphthalen-2-yloxy)acetyl) isophthalohydrazide
Xanthomonas oryzae pv. oryzae
-
pH 7.5, 37C
0.0154
N1',N4'-bis(2-(1-bromonaphthalen naphthalen-2-yloxy)acetyl)succinohydrazide
Xanthomonas oryzae pv. oryzae
-
pH 7.5, 37C
0.0194
N1',N4'-bis(2-(3-bromonaphthalen naphthalen-2-yloxy)acetyl)succinohydrazide
Xanthomonas oryzae pv. oryzae
-
pH 7.5, 37C
0.0112
N1',N4'-bis(2-(6-bromonaphthalen naphthalen-2-yloxy)acetyl)succinohydrazide
Xanthomonas oryzae pv. oryzae
-
pH 7.5, 37C
0.0171
N1',N4'-bis(2-(naphthalen-2-yloxy)acetyl) succinohydrazide
Xanthomonas oryzae pv. oryzae
-
pH 7.5, 37C
0.0233
N1',N6'-bis(2-(1-bromonaphthalen naphthalen-2-yloxy)acetyl)adipohydrazide
Xanthomonas oryzae pv. oryzae
-
pH 7.5, 37C
0.022
N1',N6'-bis(2-(3-bromonaphthalen naphthalen-2-yloxy)acetyl)adipohydrazide
Xanthomonas oryzae pv. oryzae
-
pH 7.5, 37C
0.0125
N1',N6'-bis(2-(6-bromonaphthalen naphthalen-2-yloxy)acetyl)adipohydrazide
Xanthomonas oryzae pv. oryzae
-
pH 7.5, 37C
0.0332
N1',N6'-bis(2-(naphthalen-2-yloxy)acetyl)adipohydrazide
Xanthomonas oryzae pv. oryzae
-
pH 7.5, 37C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.17
-
purified enzyme, pH 7.4, 37C
2
-
N-acetyl-alpha-D-glucosamine 1-phosphate substrate, pH 7.5, 80C, recombinant mutant D005 protein
2.2
-
N-acetyl-alpha-D-glucosamine 1-phosphate substrate, pH 7.5, 80C, recombinant wild-type ST0452 protein
2.6
-
N-acetyl-alpha-D-glucosamine 1-phosphate substrate, pH 7.5, 80C, recombinant mutant D011 protein
3.4
-
purified enzyme, 30C
6.42
-
pH 7.5, 80C, substrates: UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
8.66
-
purified enzyme, pH 7.5, 30C
14.9
-
purified enzyme
16.34
-
pH 7.5, 80C, substrates: diphosphate + UDP-N-acetyl-alpha-D-glucosamine
20.4
-
purified enzyme
39.3
-
purified recombinant enzyme
72
-
purified recombinant native enzyme, pH 7.5, 37C
330
-
purified enzyme, pH 7.4, 37C
2390
-
purified enzyme, pH 7.4, 37C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.9 - 7.7
-
isoform MP IV
7 - 7.5
-
isoform MP III
7.3 - 8.3
-
isoform MP I
7.4 - 8.4
-
isoform MP II
7.5
-
assay at
7.5 - 8
-
both directions
7.5 - 8.5
-
more active with Tris than with phosphate buffer
8.5 - 9
-
UTP formation
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7 - 9.5
-
-
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
65
-
inactivation
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.64
sequence calculation
5.74
sequence calculation
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
-
Manually annotated by BRENDA team
expression early in embryogenesis, expression occurs ubiquitously and uniformly in the cellular blastoderm and accumulates in the developing mesoderm, gut primordia, and trachea; temporal profile of mmy transcription in early embryogenesis, overview
Manually annotated by BRENDA team
KT282116, KT282117
;
Manually annotated by BRENDA team
KT282116, KT282117
;
Manually annotated by BRENDA team
KT282116, KT282117
;
Manually annotated by BRENDA team
KT282116, KT282117
ventral; ventral
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
KT282116, KT282117
;
Manually annotated by BRENDA team
KT282116, KT282117
;
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
KT282116, KT282117
;
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
KT282116, KT282117
;
Manually annotated by BRENDA team
KT282116, KT282117
thoracic; thoracic
Manually annotated by BRENDA team
-
very high activity
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
KT282116, KT282117
;
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
-
-
Manually annotated by BRENDA team
additional information
PDB
SCOP
CATH
ORGANISM
UNIPROT
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100)
Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
24700
-
SDS-PAGE, enzyme variant del233
25600
-
SDS-PAGE, enzyme variant del227
28600
-
SDS-PAGE, enzyme variant Tr250
33000
-
SDS-PAGE
36200
-
SDS-PAGE, enzyme variant del130
37100
-
SDS-PAGE, Tr331
40000
-
SDS-PAGE
41800
-
SDS-PAGE, enyzme variant del78
47000
-
gel filtration
48290
-
calculated from the deduced amino acid sequence
48800
predicted from DNA sequence
49000
-
SDS-PAGE, corresponds very well with molecular weight expected from DNA sequence
50100
-
SDS-PAGE, calculated from DNA sequence
52922
-
x * 52922, calculated
53000
-
SDS-PAGE, His-Tag contributed with 3900 Da
58300
1 * 58300, SDS-PAGE
60000
gel filtration; x * 60000, SDS-PAGE
66000
-
gel filtration
125000
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hexamer
-
trimer/hexamer equilibrium, sedimentation equilibrium analytical ultracentrifugation. Two trimers assemble through their N-terminal domains. The interaction is mediated by a loop that undergoes a large conformational change in the uridyl transferase reaction
monomer
additional information