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Information on EC 2.3.1.157 - glucosamine-1-phosphate N-acetyltransferase and Organism(s) Escherichia coli and UniProt Accession P0ACC7

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EC Tree
IUBMB Comments
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 2.7.7.23, UDP-N-acetylglucosamine diphosphorylase.
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This record set is specific for:
Escherichia coli
UNIPROT: P0ACC7
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The taxonomic range for the selected organisms is: Escherichia coli
The enzyme appears in selected viruses and cellular organisms
Synonyms
n-acetylglucosamine-1-phosphate uridyltransferase, st0452 protein, glmu acetyltransferase, udp-glcnac pyrophosphorylase, st0452, glmu enzyme, glucosamine-1-phosphate acetyltransferase, glmu uridyltransferase, glcn-1-p actase, rv1018c, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
N-acetylglucosamine-1-phosphate uridyltransferase
bifunctional enzyme also possesses the activity of EC 2.7.7.23, UDP-N-acetylglucosamine diphosphorylase
N-acetylglucosamine-1-phosphate-uridyltransferase/glucosamine-1-phosphate-acetyltransferase
-
bifunctional GlmU protein
-
-
GlcNAc-1-P uridyltransferase
-
-
GlmU acetyltransferase
-
-
GlmU enzyme
-
-
GlmU uridyltransferase
-
-
N-acetylglucosamine-1-phosphate pyrophosphorylase
-
-
N-acetylglucosamine-1-phosphate uridyltransferase
-
-
N-acetylglucosamine-1-phosphate-uridyltransferase/glucosamine-1-phosphate-acetyltransferase
-
-
N-acetylglucosamine-1-phosphate-uridylyltransferase/glucosamine-1-phosphate-acetyltransferase
-
-
UDP-GlcNAc pyrophosphorylase
-
-
additional information
bifunctional enzyme, cf. EC 2.7.7.23
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
acetyl-CoA + alpha-D-glucosamine 1-phosphate = CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Acyl group transfer
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -
SYSTEMATIC NAME
IUBMB Comments
acetyl-CoA:alpha-D-glucosamine-1-phosphate N-acetyltransferase
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 2.7.7.23, UDP-N-acetylglucosamine diphosphorylase.
CAS REGISTRY NUMBER
COMMENTARY hide
9023-06-7
-
9031-91-8
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
acetyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
show the reaction diagram
D-glucosamine 1-phosphate + acetyl-CoA
N-acetyl-D-glucosamine 1-phosphate + CoA
show the reaction diagram
acetyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
show the reaction diagram
D-glucosamine 1-phosphate + acetyl-CoA
N-acetyl-D-glucosamine 1-phosphate + CoA
show the reaction diagram
-
-
-
-
?
N-acetyl-D-glucosamine 1-phosphate + UTP
UDP-N-acetylglucosamine + ?
show the reaction diagram
-
glmU gene product, bifunctional enzyme catalyzing 2 subsequent steps in the pathway for UDP-GlcNAc synthesis
-
-
r
UDP-N-acetyl-alpha-D-glucosamine + H2O
N-acetyl-D-glucosamine 1-phosphate + UMP
show the reaction diagram
-
-
-
-
r
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
acetyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
show the reaction diagram
D-glucosamine 1-phosphate + acetyl-CoA
N-acetyl-D-glucosamine 1-phosphate + CoA
show the reaction diagram
the bifunctional enzyme also possesses the activity of EC 2.7.7.23, UDP-N-acetylglucosamine diphosphorylase and performs the last two steps in the synthesis of UDP-N-acetylglucosamine
-
-
?
acetyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
show the reaction diagram
D-glucosamine 1-phosphate + acetyl-CoA
N-acetyl-D-glucosamine 1-phosphate + CoA
show the reaction diagram
-
-
-
-
?
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
acetyl-CoA
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
-
absolute requirement for both activities in the sharp range from 1-10 mM with an optimal value of 3 mM
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(2E)-4-[[2,4-dimethoxy-5-(10H-phenoxazin-10-ylsulfonyl)phenyl]amino]-4-oxobut-2-enoic acid
-
(E)-N-(2,5-dimethylphenyl)-1-(5-nitrofuran-2-yl)methanimine
specific inhibitor, 93.82% inhibition at 0.1 mM
(E)-N-(2-fluoro-5-nitrophenyl)-1-(5-nitrofuran-2-yl)methanimine
specific inhibitor, 97.47% inhibition at 0.1 mM
1-butyl-2-[(E)-2-(5-nitrofuran-2-yl)ethenyl]-1H-benzimidazole
unspecific inhibitor, 84.26% inhibition at 0.1 mM
1-[2,4-dimethoxy-5-(10H-phenoxazin-10-ylsulfonyl)phenylamino]-2-(-4-pyridyl)-1-ethanone
commercial inhibitor
1-[2,4-dimethoxy-5-(10H-phenoxazin-10-ylsulfonyl)phenylamino]-2-(4-pyridyl)-1-ethanone
3-fluoro-N-[1-(2-methylpropanoyl)-1,2,3,4-tetrahydroquinolin-6-yl]benzenesulfonamide
3-hydrazinylquinoline-2-thiol
specific inhibitor, 92.68% inhibition at 0.1 mM
3-[(2,4-dimethoxyphenyl)amino]-4-phenylcyclobut-3-ene-1,2-dione
40.0% inhibition at 0.1 mM
4-[[2,4-dimethoxy-5-(10H-phenoxazin-10-ylsulfonyl)phenyl]amino]-4-oxobutanoic acid
-
5,7-dichloro-2-hydrazinylquinolin-8-ol
specific inhibitor, 98.25% inhibition at 0.1 mM
5-(1,2-oxazol-5-yl)-N-(pyridin-3-ylmethyl)furan-2-sulfonamide
44.7% inhibition at 0.1 mM
6-chloro-N-[3-(methylsulfanyl)phenyl]-3-oxo-3,4-dihydro-2H-1,4-benzoxazine-7-sulfonamide
ethyl (2-[(Z)-[2-(ethylsulfanyl)-5-oxo-1,3-thiazol-4(5H)-ylidene]methyl]phenoxy)acetate
45.3% inhibition at 0.1 mM
N-(2,5-dimethoxyphenyl)-N-(phenylsulfonyl)glycine
42.01% inhibition at 0.1 mM
-
N-(3-chlorophenyl)-2-methoxy-5-(2-methyl-1,3-oxazol-5-yl)benzenesulfonamide
406% inhibition at 0.1 mM
N-(5-chloro-2-methoxyphenyl)-N-(phenylsulfonyl)glycine
45.15% inhibition at 0.1 mM
N-[2,4-dimethoxy-5-(10H-phenoxazin-10-ylsulfonyl)phenyl]-2-(pyridin-4-yl)acetamide
-
terreic acid
(1R,2R)-2-[[2,4-dimethoxy-5-(1,2,3,4-tetrahydroquinolin-2-ylsulfonyl)phenyl]carbamoyl]-3-methylcyclopropanecarboxylic acid
-
-
(1R,2R)-2-[[4-hydroxy-2-methoxy-5-(1,2,3,4-tetrahydroquinolin-2-ylsulfonyl)phenyl]carbamoyl]-3-methylcyclopropanecarboxylic acid
-
-
(1R,2R)-2-[[5-(acridin-10(9H)-ylsulfonyl)-2,4-dimethoxyphenyl]carbamoyl]-3-methylcyclopropanecarboxylic acid
-
-
(1R,2R)-2-[[5-(acridin-10(9H)-ylsulfonyl)-4-hydroxy-2-methoxyphenyl]carbamoyl]-3-methylcyclopropanecarboxylic acid
-
-
(2E)-4-([2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]amino)-4-oxobut-2-enoic acid
-
-
(5-[(E)-[(2,5-dimethylphenyl)imino]methyl]furan-2-yl)(hydroxy)oxoammonium
-
0.1 mM, 93.82% inhibition, competitive inhibition versus acetyl-CoA, uncompetitive inhibition versus glucose 1-phosphate
1-(2-[[([5-[(3-carboxypropanoyl)amino]-2,4-dimethoxyphenyl]sulfonyl)amino]methyl]phenyl)piperidine-4-carboxylic acid
-
-
2'-[[([5-[(3-carboxypropanoyl)amino]-2,4-dimethoxyphenyl]sulfonyl)amino]methyl]biphenyl-4-carboxylic acid
-
-
2-(2-cyanopyridin-4-yl)-N-[2,4-dimethoxy-5-(1,2,3,4-tetrahydroquinolin-2-ylsulfonyl)phenyl]acetamide
-
-
2-([2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]amino)-2-oxoethyl acetate
-
-
2-Nitro-5-thiocyanobenzoic acid
-
-
3-fluoro-N-[1-(2-methylpropanoyl)-1,2,3,4-tetrahydroquinolin-6-yl]benzene-1-sulfonamide
-
0.1 mM, 82.87% inhibition, competitive inhibition versus acetyl-CoA, uncompetitive inhibition versus glucose 1-phosphate
3-fluoro-N-[1-(2-methylpropanoyl)-1,2,3,4-tetrahydroquinolin-6-yl]benzenesulfonamide
0.1 mM, 83% inhibition of acetyltransferase activity of GlmU
3-hydrazinylquinoline-2-thiol
4-([2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]amino)-4-oxobutanoic acid
-
-
4-([2,4-dimethoxy-5-[naphthalen-2-yl(phenyl)sulfamoyl]phenyl]amino)-4-oxobutanoic acid
-
-
4-([4-hydroxy-2-methoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]amino)-4-oxobutanoic acid
-
-
4-([5-[(4-aminophenyl)(phenyl)sulfamoyl]-2,4-dimethoxyphenyl]amino)-4-oxobutanoic acid
-
-
4-([5-[bis(4-methylphenyl)sulfamoyl]-2,4-dimethoxyphenyl]amino)-4-oxobutanoic acid
-
-
4-[(2,4-dimethoxy-5-[[2-(piperidin-1-yl)benzyl]sulfamoyl]phenyl)amino]-4-oxobutanoic acid
-
-
4-[(5-[[2-(4-[[(carboxyacetyl)oxy]methyl]piperidin-1-yl)benzyl]sulfamoyl]-2,4-dimethoxyphenyl)amino]-4-oxobutanoic acid
-
-
4-[2-([2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]amino)-2-oxoethoxy]benzoic acid
-
-
4-[[2,4-dimethoxy-5-(10H-phenothiazin-10-ylsulfonyl)phenyl]amino]-4-oxobutanoic acid
-
-
4-[[2,4-dimethoxy-5-(10H-phenoxazin-10-ylsulfonyl)phenyl]amino]-4-oxobutanoic acid
-
-
4-[[4-hydroxy-2-methoxy-5-(1,2,3,4-tetrahydroquinolin-2-ylsulfonyl)phenyl]amino]-4-oxobutanoic acid
-
-
4-[[5-(dibenzo[b,f][1,4]oxazepin-10(11H)-ylsulfonyl)-2,4-dimethoxyphenyl]amino]-4-oxobutanoic acid
-
-
4-[[5-(diphenylsulfamoyl)-2,4-dimethoxyphenyl]amino]-4-oxobutanoic acid
-
-
4-[[5-([2-[4-(carboxymethyl)piperidin-1-yl]benzyl]sulfamoyl)-2,4-dimethoxyphenyl]amino]-4-oxobutanoic acid
-
-
4-[[5-([2-[4-(hydroxymethyl)piperidin-1-yl]benzyl]sulfamoyl)-2,4-dimethoxyphenyl]amino]-4-oxobutanoic acid
-
-
5,7-dichloro-2-hydrazinylquinolin-8-ol
6-chloro-N-[3-(methylsulfanyl)phenyl]-3-oxo-3,4-dihydro-2H-1,4-benzoxazine-7-sulfonamide
iodoacetamide
-
-
methyl 2-[([[5-(acetylamino)-2,4-dimethoxyphenyl]sulfonyl]amino)methyl]benzoate
-
-
N-(2,4-dimethoxy-5-[[2-(piperidin-1-yl)benzyl]sulfamoyl]phenyl)acetamide
-
-
N-([2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]carbamothioyl)glycine
-
-
N-([2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]carbamoyl)glycine
-
-
N-acetylglucosamine-1-phosphate
-
acetyltransferase activity inhibited by its reaction product
N-ethylmaleimide
-
-
N-[2,4-dimethoxy-5-(1,2,3,4-tetrahydroquinolin-2-ylsulfonyl)phenyl]-2-(2-fluoropyridin-4-yl)acetamide
-
-
N-[2,4-dimethoxy-5-(1,2,3,4-tetrahydroquinolin-2-ylsulfonyl)phenyl]-3-(2H-tetrazol-5-yl)propanamide
-
-
N-[2,4-dimethoxy-5-(10H-phenoxazine-10-sulfonyl)phenyl]-2-(pyridin-4-yl)acetamide
-
-
N-[2,4-dimethoxy-5-(phenylsulfamoyl)phenyl]acetamide
-
-
N-[2,4-dimethoxy-5-(piperidin-1-ylsulfonyl)phenyl]acetamide
-
-
N-[2,4-dimethoxy-5-[(2-methoxybenzyl)sulfamoyl]phenyl]acetamide
-
-
N-[2,4-dimethoxy-5-[(2-methyl-2,3-dihydro-1H-indol-1-yl)sulfonyl]phenyl]acetamide
-
the inhibitor binds at the C-terminal domain of GlmU engaging the A, B and C subunits of the trimer
N-[2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]-2-(pyridin-4-ylsulfanyl)acetamide
-
-
N-[2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]acetamide
-
-
N-[2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]benzamide
-
-
N-[2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]methanesulfonamide
-
-
N-[2,4-dimethoxy-5-[(2-methylpyrrolidin-1-yl)sulfonyl]phenyl]acetamide
-
-
N-[2,4-dimethoxy-5-[(3-methylphenyl)sulfamoyl]phenyl]acetamide
-
-
N-[2,4-dimethoxy-5-[(4-methylphenyl)sulfamoyl]phenyl]acetamide
-
-
N-[2,4-dimethoxy-5-[methyl(phenyl)sulfamoyl]phenyl]acetamide
-
-
N-[2,4-dimethoxy-5-[phenyl(propan-2-yl)sulfamoyl]phenyl]acetamide
-
-
N-[5-(acridin-10(9H)-ylsulfonyl)-2,4-dimethoxyphenyl]-2-(2-fluoropyridin-4-yl)acetamide
-
-
N-[5-(acridin-10(9H)-ylsulfonyl)-2,4-dimethoxyphenyl]-2-(pyridin-4-yl)acetamide
-
-
N-[5-(dimethylsulfamoyl)-2,4-dimethoxyphenyl]acetamide
-
-
N-[5-([2-[4-(hydroxymethyl)piperidin-1-yl]benzyl]sulfamoyl)-2,4-dimethoxyphenyl]acetamide
-
-
N-[5-[(1,3-benzodioxol-5-ylmethyl)sulfamoyl]-2,4-dimethoxyphenyl]acetamide
-
-
N-[5-[(2-bromobenzyl)sulfamoyl]-2,4-dimethoxyphenyl]acetamide
-
-
N-[5-[(2-fluorophenyl)sulfamoyl]-2,4-dimethoxyphenyl]acetamide
-
-
N-[5-[(3-fluorophenyl)sulfamoyl]-2,4-dimethoxyphenyl]acetamide
-
-
N-[5-[(4-fluorophenyl)sulfamoyl]-2,4-dimethoxyphenyl]acetamide
-
-
N-[5-[butyl(propan-2-yl)sulfamoyl]-2,4-dimethoxyphenyl]acetamide
-
-
N-[5-[ethyl(2-methylphenyl)sulfamoyl]-2,4-dimethoxyphenyl]acetamide
-
-
p-hydroxymercuribenzoate
-
-
terreic acid
isolated from Aspergillus terreus, inhibits the acetyltransferase domain. Terreic acid is competitive with acetyl-CoA and uncompetitive with alpha-D-glucosamine 1-phosphate and exhibits concentration-dependent killing of Escherichia coli ATCC 25922 up to 4-times minimum inhibitory concentration and inhibits the growth of biofilms generated by Escherichia coli
UDP-MurNAc
-
1 mM, relative enzyme activity 2%
[2-([2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]amino)-2-oxoethoxy]acetic acid
-
-
[4-fluoro-3-[(E)-([5-[hydroxy(oxo)azaniumyl]furan-2-yl]methylidene)amino]phenyl](hydroxy)oxoammonium
-
0.1 mM, 97.47% inhibition, competitive inhibition versus acetyl-CoA, uncompetitive inhibition versus glucose 1-phosphate
[5-[(E)-2-(1-butyl-1H-benzimidazol-2-yl)ethenyl]furan-2-yl](hydroxy)oxoammonium
-
0.1 mM, 84.26% inhibition, competitive inhibition versus acetyl-CoA, uncompetitive inhibition versus glucose 1-phosphate
[[2-([2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]amino)-2-oxoethyl]sulfanyl]acetic acid
-
-
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.09 - 0.6
acetyl-CoA
0.07 - 0.25
D-glucosamine 1-phosphate
0.07
N-acetyl-D-glucosamine 1-phosphate
-
uridyltransferase activity
0.1
UTP
-
uridyltransferase activity
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
12.4
N-acetyl-D-glucosamine 1-phosphate
-
GmlU uridyltransferase
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.04029 - 0.04194
terreic acid
0.042
terreic acid
pH 7.3, 37°C, substrate alpha-D-glucosamine 1-phosphate
additional information
additional information
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00001
(2E)-4-[[2,4-dimethoxy-5-(10H-phenoxazin-10-ylsulfonyl)phenyl]amino]-4-oxobut-2-enoic acid
Escherichia coli
pH 7.6, 30°C, recombinant His6-tagged enzyme
0.0211
(E)-N-(2,5-dimethylphenyl)-1-(5-nitrofuran-2-yl)methanimine
Escherichia coli
pH 7.6, 30°C, recombinant His6-tagged enzyme
0.0041
(E)-N-(2-fluoro-5-nitrophenyl)-1-(5-nitrofuran-2-yl)methanimine
Escherichia coli
pH 7.6, 30°C, recombinant His6-tagged enzyme
0.0249
3-fluoro-N-[1-(2-methylpropanoyl)-1,2,3,4-tetrahydroquinolin-6-yl]benzenesulfonamide
Escherichia coli
pH 7.6, 30°C, recombinant His6-tagged enzyme
0.0038
3-hydrazinylquinoline-2-thiol
Escherichia coli
pH 7.6, 30°C, recombinant His6-tagged enzyme
0.00001
4-[[2,4-dimethoxy-5-(10H-phenoxazin-10-ylsulfonyl)phenyl]amino]-4-oxobutanoic acid
Escherichia coli
pH 7.6, 30°C, recombinant His6-tagged enzyme
0.0014
5,7-dichloro-2-hydrazinylquinolin-8-ol
Escherichia coli
pH 7.6, 30°C, recombinant His6-tagged enzyme
0.54
N-[2,4-dimethoxy-5-(10H-phenoxazin-10-ylsulfonyl)phenyl]-2-(pyridin-4-yl)acetamide
Escherichia coli
pH 7.6, 30°C, recombinant His6-tagged enzyme
0.04424
terreic acid
0.0004
(1R,2R)-2-[[2,4-dimethoxy-5-(1,2,3,4-tetrahydroquinolin-2-ylsulfonyl)phenyl]carbamoyl]-3-methylcyclopropanecarboxylic acid
Escherichia coli
-
pH and temperature not specified in the publication
0.00048
(1R,2R)-2-[[4-hydroxy-2-methoxy-5-(1,2,3,4-tetrahydroquinolin-2-ylsulfonyl)phenyl]carbamoyl]-3-methylcyclopropanecarboxylic acid
Escherichia coli
-
pH and temperature not specified in the publication
0.00003
(1R,2R)-2-[[5-(acridin-10(9H)-ylsulfonyl)-2,4-dimethoxyphenyl]carbamoyl]-3-methylcyclopropanecarboxylic acid
Escherichia coli
-
pH and temperature not specified in the publication
0.00006
(1R,2R)-2-[[5-(acridin-10(9H)-ylsulfonyl)-4-hydroxy-2-methoxyphenyl]carbamoyl]-3-methylcyclopropanecarboxylic acid
Escherichia coli
-
pH and temperature not specified in the publication
0.0005
(2E)-4-([2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]amino)-4-oxobut-2-enoic acid
Escherichia coli
-
pH 7.35, 22°C
0.02105
(5-[(E)-[(2,5-dimethylphenyl)imino]methyl]furan-2-yl)(hydroxy)oxoammonium
Escherichia coli
-
pH 7.3, 37°C
0.0005
1-(2-[[([5-[(3-carboxypropanoyl)amino]-2,4-dimethoxyphenyl]sulfonyl)amino]methyl]phenyl)piperidine-4-carboxylic acid
Escherichia coli
-
pH 7.35, 22°C
0.0009
2'-[[([5-[(3-carboxypropanoyl)amino]-2,4-dimethoxyphenyl]sulfonyl)amino]methyl]biphenyl-4-carboxylic acid
Escherichia coli
-
pH 7.35, 22°C
0.00068
2-(2-cyanopyridin-4-yl)-N-[2,4-dimethoxy-5-(1,2,3,4-tetrahydroquinolin-2-ylsulfonyl)phenyl]acetamide
Escherichia coli
-
pH and temperature not specified in the publication
0.002
2-([2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]amino)-2-oxoethyl acetate
Escherichia coli
-
pH 7.35, 22°C
0.0249
3-fluoro-N-[1-(2-methylpropanoyl)-1,2,3,4-tetrahydroquinolin-6-yl]benzene-1-sulfonamide
Escherichia coli
-
pH 7.3, 37°C
0.00376
3-hydrazinylquinoline-2-thiol
Escherichia coli
-
pH 7.3, 37°C
0.00009
4-([2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]amino)-4-oxobutanoic acid
Escherichia coli
-
pH 7.35, 22°C
0.00004
4-([2,4-dimethoxy-5-[naphthalen-2-yl(phenyl)sulfamoyl]phenyl]amino)-4-oxobutanoic acid
Escherichia coli
-
pH and temperature not specified in the publication
0.000058
4-([4-hydroxy-2-methoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]amino)-4-oxobutanoic acid
Escherichia coli
-
pH 7.2, temperature not specified in the publication
0.000018 - 0.00002
4-([5-[(4-aminophenyl)(phenyl)sulfamoyl]-2,4-dimethoxyphenyl]amino)-4-oxobutanoic acid
0.00004
4-([5-[bis(4-methylphenyl)sulfamoyl]-2,4-dimethoxyphenyl]amino)-4-oxobutanoic acid
Escherichia coli
-
pH and temperature not specified in the publication
0.003
4-[(2,4-dimethoxy-5-[[2-(piperidin-1-yl)benzyl]sulfamoyl]phenyl)amino]-4-oxobutanoic acid
Escherichia coli
-
pH 7.35, 22°C
0.00025
4-[(5-[[2-(4-[[(carboxyacetyl)oxy]methyl]piperidin-1-yl)benzyl]sulfamoyl]-2,4-dimethoxyphenyl)amino]-4-oxobutanoic acid
Escherichia coli
-
pH 7.35, 22°C
0.2
4-[2-([2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]amino)-2-oxoethoxy]benzoic acid
Escherichia coli
-
above, pH 7.35, 22°C
0.00009
4-[[2,4-dimethoxy-5-(10H-phenothiazin-10-ylsulfonyl)phenyl]amino]-4-oxobutanoic acid
Escherichia coli
-
pH and temperature not specified in the publication
0.000007 - 0.00001
4-[[2,4-dimethoxy-5-(10H-phenoxazin-10-ylsulfonyl)phenyl]amino]-4-oxobutanoic acid
0.00005
4-[[4-hydroxy-2-methoxy-5-(1,2,3,4-tetrahydroquinolin-2-ylsulfonyl)phenyl]amino]-4-oxobutanoic acid
Escherichia coli
-
pH and temperature not specified in the publication
0.00003
4-[[5-(dibenzo[b,f][1,4]oxazepin-10(11H)-ylsulfonyl)-2,4-dimethoxyphenyl]amino]-4-oxobutanoic acid
Escherichia coli
-
pH and temperature not specified in the publication
0.00004
4-[[5-(diphenylsulfamoyl)-2,4-dimethoxyphenyl]amino]-4-oxobutanoic acid
Escherichia coli
-
pH and temperature not specified in the publication
0.0004
4-[[5-([2-[4-(carboxymethyl)piperidin-1-yl]benzyl]sulfamoyl)-2,4-dimethoxyphenyl]amino]-4-oxobutanoic acid
Escherichia coli
-
pH 7.35, 22°C
0.003
4-[[5-([2-[4-(hydroxymethyl)piperidin-1-yl]benzyl]sulfamoyl)-2,4-dimethoxyphenyl]amino]-4-oxobutanoic acid
Escherichia coli
-
pH 7.35, 22°C
0.0014
5,7-dichloro-2-hydrazinylquinolin-8-ol
0.015
methyl 2-[([[5-(acetylamino)-2,4-dimethoxyphenyl]sulfonyl]amino)methyl]benzoate
Escherichia coli
-
pH 7.35, 22°C
0.2
N-(2,4-dimethoxy-5-[[2-(piperidin-1-yl)benzyl]sulfamoyl]phenyl)acetamide
Escherichia coli
-
above, pH 7.35, 22°C
0.0005
N-([2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]carbamothioyl)glycine
Escherichia coli
-
pH 7.35, 22°C
0.0005
N-([2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]carbamoyl)glycine
Escherichia coli
-
pH 7.35, 22°C
0.0008
N-[2,4-dimethoxy-5-(1,2,3,4-tetrahydroquinolin-2-ylsulfonyl)phenyl]-2-(2-fluoropyridin-4-yl)acetamide
Escherichia coli
-
pH and temperature not specified in the publication
0.00043
N-[2,4-dimethoxy-5-(1,2,3,4-tetrahydroquinolin-2-ylsulfonyl)phenyl]-3-(2H-tetrazol-5-yl)propanamide
Escherichia coli
-
pH and temperature not specified in the publication
0.00054
N-[2,4-dimethoxy-5-(10H-phenoxazine-10-sulfonyl)phenyl]-2-(pyridin-4-yl)acetamide
Escherichia coli
-
pH 7.3, 37°C
0.02
N-[2,4-dimethoxy-5-(phenylsulfamoyl)phenyl]acetamide
Escherichia coli
-
pH 7.35, 22°C
0.08
N-[2,4-dimethoxy-5-(piperidin-1-ylsulfonyl)phenyl]acetamide
Escherichia coli
-
pH 7.35, 22°C
0.01
N-[2,4-dimethoxy-5-[(2-methoxybenzyl)sulfamoyl]phenyl]acetamide
Escherichia coli
-
pH 7.35, 22°C
0.002
N-[2,4-dimethoxy-5-[(2-methyl-2,3-dihydro-1H-indol-1-yl)sulfonyl]phenyl]acetamide
Escherichia coli
-
pH 7.35, 22°C
0.001
N-[2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]-2-(pyridin-4-ylsulfanyl)acetamide
Escherichia coli
-
pH 7.35, 22°C
0.0015 - 0.0021
N-[2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]acetamide
0.2
N-[2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]benzamide
Escherichia coli
-
above, pH 7.35, 22°C
0.1
N-[2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]methanesulfonamide
Escherichia coli
-
pH 7.35, 22°C
0.2
N-[2,4-dimethoxy-5-[(2-methylpyrrolidin-1-yl)sulfonyl]phenyl]acetamide
Escherichia coli
-
pH 7.35, 22°C
0.017
N-[2,4-dimethoxy-5-[(3-methylphenyl)sulfamoyl]phenyl]acetamide
Escherichia coli
-
pH 7.35, 22°C
0.021
N-[2,4-dimethoxy-5-[(4-methylphenyl)sulfamoyl]phenyl]acetamide
Escherichia coli
-
pH 7.35, 22°C
0.003 - 0.0033
N-[2,4-dimethoxy-5-[methyl(phenyl)sulfamoyl]phenyl]acetamide
0.002
N-[2,4-dimethoxy-5-[phenyl(propan-2-yl)sulfamoyl]phenyl]acetamide
Escherichia coli
-
pH 7.35, 22°C
0.00009
N-[5-(acridin-10(9H)-ylsulfonyl)-2,4-dimethoxyphenyl]-2-(2-fluoropyridin-4-yl)acetamide
Escherichia coli
-
pH and temperature not specified in the publication
0.00006
N-[5-(acridin-10(9H)-ylsulfonyl)-2,4-dimethoxyphenyl]-2-(pyridin-4-yl)acetamide
Escherichia coli
-
pH and temperature not specified in the publication
0.2
N-[5-(dimethylsulfamoyl)-2,4-dimethoxyphenyl]acetamide
Escherichia coli
-
above, pH 7.35, 22°C
0.04
N-[5-([2-[4-(hydroxymethyl)piperidin-1-yl]benzyl]sulfamoyl)-2,4-dimethoxyphenyl]acetamide
Escherichia coli
-
pH 7.35, 22°C
0.2
N-[5-[(1,3-benzodioxol-5-ylmethyl)sulfamoyl]-2,4-dimethoxyphenyl]acetamide
Escherichia coli
-
above, pH 7.35, 22°C
0.004
N-[5-[(2-bromobenzyl)sulfamoyl]-2,4-dimethoxyphenyl]acetamide
Escherichia coli
-
pH 7.35, 22°C
0.005
N-[5-[(2-fluorophenyl)sulfamoyl]-2,4-dimethoxyphenyl]acetamide
Escherichia coli
-
pH 7.35, 22°C
0.015
N-[5-[(3-fluorophenyl)sulfamoyl]-2,4-dimethoxyphenyl]acetamide
Escherichia coli
-
pH 7.35, 22°C
0.025
N-[5-[(4-fluorophenyl)sulfamoyl]-2,4-dimethoxyphenyl]acetamide
Escherichia coli
-
pH 7.35, 22°C
0.13
N-[5-[butyl(propan-2-yl)sulfamoyl]-2,4-dimethoxyphenyl]acetamide
Escherichia coli
-
pH 7.35, 22°C
0.015
N-[5-[ethyl(2-methylphenyl)sulfamoyl]-2,4-dimethoxyphenyl]acetamide
Escherichia coli
-
pH 7.35, 22°C
0.0442
terreic acid
Escherichia coli
pH 7.3, 37°C
0.0002
[2-([2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]amino)-2-oxoethoxy]acetic acid
Escherichia coli
-
pH 7.35, 22°C
0.00405
[4-fluoro-3-[(E)-([5-[hydroxy(oxo)azaniumyl]furan-2-yl]methylidene)amino]phenyl](hydroxy)oxoammonium
Escherichia coli
-
pH 7.3, 37°C
0.0001
[[2-([2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]amino)-2-oxoethyl]sulfanyl]acetic acid
Escherichia coli
-
pH 7.35, 22°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.004
-
mutant JM83(pFP3-Tr331), acetyltransferase activity
0.014
-
mutant JM83(pTrcHis30), uridyltransferase activity
0.11
-
mutant JM83(pTrcHis30), acetyltransferase activity
0.12
-
mutant JM83(pFP3-Tr331), uridyltransferase activity
15.1
-
GlcNAc-1-P uridyltransferase activity
2.2
-
GlcN-1-P acetyltransferase activity
2.85
-
mutant JM83(pFP3-Tr331) + IPTG, uridyltransferase activity
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.2
-
assay at
7.3 - 7.4
-
assay at
8.2
-
for both acetyltransferase and uridyltransferase
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
22
-
assay at romm temperature
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
pathway and metabolism of UDP-N-acetylglucosamine in prokaryotes and eukaryotes, overview
metabolism
-
the enzyme is involved in the cell wall biosynthesis of Gram-negative organisms
physiological function
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
24700
-
1 * 37100 + 1 * 24700, uridyltransferase and acetyltransferase in separate domains, SDS-PAGE
37100
-
1 * 37100 + 1 * 24700, uridyltransferase and acetyltransferase in separate domains, SDS-PAGE
49000
-
gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 52000, SDS-PAGE
heterotrimer
-
-
trimer
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method. X-ray crystal structure of the bifunctional enzyme in complex with UDP-GlcNAc and CoA, determined to 2.1 A resolution and reveals a two-domain architecture that is responsible for the two reactions of EC 2.3.1.157 and EC 2.7.7.23. The C-terminal domain is responsible for the CoA-dependent acetylation of Glc-1-phosphate to GlcNAc-1-phosphate and displays the longest left-handed parallel alpha-helix observed to date. The acetyltransferase active site defined by the binding site for CoA makes use of residues from all three subunits and is positioned beneath an open cavity large enough to accommodate the Glc-1-PO4 acetyl acceptor. The N-terminal domain catalyzes uridyl transfer from UTP to GlcNAc-1-phosphate to form the final products UDP-GlcNAc and pyrophosphate
in complex with acetyl-CoA, CoA and glucosamine-1-phosphate, and with desulfo-CoA and N-acetylglucosamine-1-phosphate. The 2-amino group of glucosamine-1-phosphate is positioned in proximity to the acetyl-CoA to facilitate direct attack on its thioester by a ternary complex mechanism
-
purified GlmU, hanging drop vapour diffusion method, mixing of 8 mg/ml enzyme in 50 mM Tris/HCl, pH 8.0, 150 mM NaCl, 2 mM EDTA, 2 mM TCEP, with 2 mM inhibitor ligand, and with reservoir solution containing 19–22% w/v PEG 3350 and either 100 mM PCTP, pH 5.0, 100-200 mM ammonium sulfate or 100 mM MMT, pH 6.0-7.0, and 400 mM ammonium sulfate, 20°C, 2-7 days, X-ray diffraction structure determination and analysis
-
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
acetyl-CoA protects from inactivation
-
acetyltransferase activity rapidly lost when the enzyme is stored in the absence of reducing thiols or acetyl coenzyme A or is treated with thiol-alkylating agents
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Ni-NTA His-binding column chromatography
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
recombinant His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
GlmU gene product, bifunctional enzyme with glucosamine-1-phosphate acetyltransferase and uridyltransferase activity
-
recombinant GlmU from Escherichia coli strain HMS174(DE3) by anion exchange and hydrophobic interaction chromatography and gel filtration
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
gene glmU, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)
gene glmU, recombinant expression of His6-tagged enzyme in Escherichia coli strain BL21(DE3)
expression in Escherichia coli
-
gene glmU, expression in Escherichia coli strain HMS174(DE3)
-
GlmU gene cloned from genomic DNA by PCR and inserted into pET3a
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
drug development
-
GlmU is a target for inhibitor design
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Mengin-Lecreulx, D.; van Heijenoort, J.
Copurification of glucosamine-1-phosphate acetyltransferase and N-acetylglucosamine-1-phosphate uridyltransferase activities of Escherichia coli: characterization of the glmU gene product as a bifunctional enzyme catalyzing two subsequent steps in the pathway for UDP-N-acetylglucosamine synthesis
J. Bacteriol.
176
5788-5795
1994
Bacillus subtilis, Escherichia coli, Escherichia coli JM83
Manually annotated by BRENDA team
Pompeo, F.; Van Heijenoort, J.; Mengin-Lecreulx, D.
Probing the role of cysteine residues in glucosamine-1-phosphate acetyltransferase activity of the bifunctional GlmU protein from Escherichia coli: site-directed mutagenesis and characterization of the mutant enzymes
J. Bacteriol.
180
4799-4803
1998
Bacillus subtilis, Escherichia coli, Escherichia coli JM83, Neisseria gonorrhoeae
Manually annotated by BRENDA team
Olsen, L.R.; Tian, Y.; Roderick, S.L.
Purification, crystallization and preliminary x-ray data for Escherichia coli GlmU: a bifunctional acetyltransferase/uridyltransferase
Acta Crystallogr. Sect. D
57
296-297
2001
Escherichia coli
Manually annotated by BRENDA team
Pompeo, F.; Bourne, Y.; Van Heijenoort, J.; Fassy, F.; Mengin-Lecreulx, D.
Dissection of the bifunctional Escherichia coli N-acetylglucosamine-1-phosphate uridyltransferase enzyme into autonomously functional domains and evidence that trimerization is absolutely required for glucosamine-1-phosphate acetyltransferase activity and cell growth
J. Biol. Chem.
276
3833-3839
2001
Escherichia coli, Escherichia coli JM83
Manually annotated by BRENDA team
Olsen, L.R.; Roderick, S.L.
Structure of the Escherichia coli GlmU pyrophosphorylase and acetyltransferase active sites
Biochemistry
40
1913-1921
2001
Escherichia coli (P0ACC7)
Manually annotated by BRENDA team
Olsen, L.R.; Vetting, M.W.; Roderick, S.L.
Structure of the E. coli bifunctional GlmU acetyltransferase active site with substrates and products
Protein Sci.
16
1230-1235
2007
Escherichia coli
Manually annotated by BRENDA team
Green, O.M.; McKenzie, A.R.; Shapiro, A.B.; Otterbein, L.; Ni, H.; Patten, A.; Stokes, S.; Albert, R.; Kawatkar, S.; Breed, J.
Inhibitors of acetyltransferase domain of N-acetylglucosamine-1-phosphate-uridyltransferase/glucosamine-1-phosphate-acetyltransferase (GlmU). Part 1: Hit to lead evaluation of a novel arylsulfonamide series
Bioorg. Med. Chem. Lett.
22
1510-1519
2012
Streptococcus pneumoniae, Escherichia coli, Haemophilus influenzae, Staphylococcus aureus
Manually annotated by BRENDA team
Stokes, S.S.; Albert, R.; Buurman, E.T.; Andrews, B.; Shapiro, A.B.; Green, O.M.; McKenzie, A.R.; Otterbein, L.R.
Inhibitors of the acetyltransferase domain of N-acetylglucosamine-1-phosphate-uridylyltransferase/glucosamine-1-phosphate-acetyltransferase (GlmU). Part 2: Optimization of physical properties leading to antibacterial aryl sulfonamides
Bioorg. Med. Chem. Lett.
22
7019-7023
2012
Streptococcus pneumoniae, Escherichia coli, Haemophilus influenzae
Manually annotated by BRENDA team
Buurman, E.T.; Andrews, B.; Gao, N.; Hu, J.; Keating, T.A.; Lahiri, S.; Otterbein, L.R.; Patten, A.D.; Stokes, S.S.; Shapiro, A.B.
In vitro validation of acetyltransferase activity of GlmU as an antibacterial target in Haemophilus influenzae
J. Biol. Chem.
286
40734-40742
2011
Escherichia coli, Escherichia coli ATCC 27325, Haemophilus influenzae, Haemophilus influenzae ATCC 51907, Staphylococcus aureus, Staphylococcus aureus RN4220, Streptococcus pneumoniae, Streptococcus pneumoniae NCTC 7466
Manually annotated by BRENDA team
Sharma, R.; Rani, C.; Mehra, R.; Nargotra, A.; Chib, R.; Rajput, V.; Kumar, S.; Singh, S.; Sharma, P.; Khan, I.
Identification and characterization of novel small molecule inhibitors of the acetyltransferase activity of Escherichia coli N-acetylglucosamine-1-phosphate-uridyltransferase/glucosamine-1-phosphate-acetyltransferase (GlmU)
Appl. Microbiol. Biotechnol.
100
3071-3085
2015
Escherichia coli, Escherichia coli (P0ACC7), Escherichia coli ATCC 25922, Escherichia coli ATCC 25922 (P0ACC7), Haemophilus influenzae (P43889), Haemophilus influenzae ATCC 51907 (P43889)
Manually annotated by BRENDA team
Mehra, R.; Sharma, R.; Khan, I.; Nargotra, A.
Identification and optimization of Escherichia coli GlmU inhibitors: An in silico approach with validation thereof
Eur. J. Med. Chem.
92
78-90
2014
Escherichia coli, Escherichia coli (P0ACC7), Escherichia coli ATCC 25922 (P0ACC7)
Manually annotated by BRENDA team
Sharma, R.; Lambu, M.R.; Jamwal, U.; Rani, C.; Chib, R.; Wazir, P.; Mukherjee, D.; Chaubey, A.; Khan, I.A.
Escherichia coli N-acetylglucosamine-1-phosphate-uridyltransferase/glucosamine-1-phosphate-acetyltransferase (GlmU) inhibitory activity of terreic acid isolated from Aspergillus terreus
J. Biomol. Screen.
21
342-353
2016
Escherichia coli, Escherichia coli (P0ACC7), Escherichia coli ATCC 25922, Escherichia coli ATCC 25922 (P0ACC7)
Manually annotated by BRENDA team
Sharma, R.; Rani, C.; Mehra, R.; Nargotra, A.; Chib, R.; Rajput, V.; Kumar, S.; Singh, S.; Sharma, P.; Khan, I.
Identification and characterization of novel small molecule inhibitors of the acetyltransferase activity of Escherichia coli N-acetylglucosamine-1-phosphate-uridyltransferase/glucosamine-1-phosphate-acetyltransferase (GlmU)
Appl. Microbiol. Biotechnol.
100
3071-3085
2016
Escherichia coli, Escherichia coli ATCC 25922, Haemophilus influenzae
Manually annotated by BRENDA team
Sharma, R.; Lambu, M.R.; Jamwal, U.; Rani, C.; Chib, R.; Wazir, P.; Mukherjee, D.; Chaubey, A.; Khan, I.A.
Escherichia coli N-acetylglucosamine-1-phosphate-uridyltransferase/glucosamine-1-phosphate-acetyltransferase (GlmU) inhibitory activity of terreic acid isolated from Aspergillus terreus
J. Biomol. Screen.
21
342-353
2016
Escherichia coli (P0ACC7), Escherichia coli, Escherichia coli ATCC 25922 (P0ACC7), Haemophilus influenzae
Manually annotated by BRENDA team
Wang, M.; Huang, M.; Gu, H.; Li, S.; Ma, Y.; Wang, J.
Mutational analysis to identify the residues essential for the acetyltransferase activity of GlmU in Bacillus subtilis
RSC Adv.
7
13858-13867
2017
Escherichia coli (P0ACC7), Bacillus subtilis (P14192), Bacillus subtilis 168 (P14192)
-
Manually annotated by BRENDA team