Information on EC 2.3.1.157 - glucosamine-1-phosphate N-acetyltransferase

Word Map on EC 2.3.1.157
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)


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

EC NUMBER
COMMENTARY hide
2.3.1.157
-
RECOMMENDED NAME
GeneOntology No.
glucosamine-1-phosphate N-acetyltransferase
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
BRENDA Link
KEGG Link
MetaCyc Link
anhydromuropeptides recycling
-
-
UDP-N-acetyl-D-glucosamine biosynthesis I
-
-
UDP-GlcNAc biosynthesis
-
-
Amino sugar and nucleotide sugar metabolism
-
-
Metabolic pathways
-
-
Biosynthesis of antibiotics
-
-
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 Hemophilus 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
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
gene glmU
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
pv. oryzae
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
-
N-acetyl-glucosamine-1-phosphate uridyltransferase, GlmU, is exclusive to prokaryotes, conserved both in Gram positive and Gram negative bacteria
malfunction
-
Deleting the C-terminal tail, i.e. residues 457-495, of GlmUMtb that provides these residues abolishes all acetyltransferase activity
metabolism
-
N-acetyl-glucosamine-1-phosphate uridyltransferase, GlmU, is a bifunctional enzyme involved in bacterial cell wall synthesis
physiological function
additional information
-
analysis of structures of GlmUMtb bound to substrates of the acetyl transfer reaction
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
N-acetyl-D-glucosamine 1-phosphate + UTP
UDP-N-acetylglucosamine + ?
show the reaction diagram
UDP-N-acetyl-d-glucosamine + diphosphate
N-acetyl-alpha-D-glucosamine 1-phosphate + UTP
show the reaction diagram
UDP-N-acetylglucosamine + H2O
N-acetyl-D-glucosamine 1-phosphate + UMP
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
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
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
no metal ion required
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(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
(4Z)-4-(4-benzyloxybenzylidene)-2-(naphthalen-2-yl)-1,3-oxazol-5(4H)-one
-
a oxazolidine derivative that specifically inhibits GlmU. Administration to infected mice results in significant decrease in the bacillary load
(5Z)-2-imino-5-[(2E)-3-(5-nitrofuran-2-yl)prop-2-en-1-ylidene]-1,3-thiazolidin-4-one
-
specific inhibition of acetyltransferase activity, competitive with respect to acetyl-CoA. Compound also exhibits whole cell activity against drug susceptible as well as drug resistant Mycobacterium tuberculosis and increased anti-TB activity when tested in combination with rifampicin, isoniazid and ethambutol. Compound is cytotoxic to eukaryotic cell line
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-amino-2,3-dideoxy-3-fluoro-alpha-D-glucopyranosyl phosphate
-
-
2-nitro-5-thiocyanatobenzoic acid
-
0.5 mM, 5% residual activity
2-Nitro-5-thiocyanobenzoic acid
-
-
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
-
93% inhibition at 0.1 mM, competitive with AcCoA and uncompetitive with alpha-D-glucosamine 1-phosphate. Antibacterial activity of the compound corelates with GlmU inhibition
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-[[(2,6-dimethoxybenzoyl)oxy]imino]cyclohexa-2,5-dien-1-one
-
specific inhibition of acetyltransferase activity, competitive with respect to acetyl-CoA. Compound also exhibits whole cell activity against drug susceptible as well as drug resistant Mycobacterium tuberculosis and increased anti-TB activity when tested in combination with rifampicin, isoniazid and ethambutol
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
5,5'-dithiobis-(2-nitrobenzoic acid)
-
0.1 mM, 33% residual activity
5,7-dichloro-2-hydrazinylquinolin-8-ol
-
98% inhibition at 0.1 mM, competitive with AcCoA and uncompetitive with alpha-D-glucosamine 1-phosphate. Antibacterial activity of the compound corelates with GlmU inhibition
6-chloro-N-[3-(methylsulfanyl)phenyl]-3-oxo-3,4-dihydro-2H-1,4-benzoxazine-7-sulfonamide
-
0.1 mM, 69% inhibition of acetyltransferase activity of GlmU. Molecular dynamics simulation and binding site analysis
alpha-D-glucosamine 1-phosphate
-
substrate inhibition, competitive versus N-[2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]acetamide
Ca2+
-
2 mM, inhibits D-glucosamine-1-phosphate N-acetyltransferase activity
Co2+
-
2 mM, inhibits D-glucosamine-1-phosphate N-acetyltransferase activity
iodoacetamide
-
-
methyl 2-[([[5-(acetylamino)-2,4-dimethoxyphenyl]sulfonyl]amino)methyl]benzoate
Mg2+
-
2 mM, inhibits D-glucosamine-1-phosphate N-acetyltransferase activity
Mn2+
-
2 mM, inhibits D-glucosamine-1-phosphate N-acetyltransferase activity
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-(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
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%
Zn2+
-
2 mM, inhibits D-glucosamine-1-phosphate N-acetyltransferase activity
[2-([2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]amino)-2-oxoethoxy]acetic acid
[[2-([2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]amino)-2-oxoethyl]sulfanyl]acetic acid
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-mercaptoethanol
-
presence required
additional information
-
MtGlmU has acetyltransferase activity in the absence of reducing agent and in the presence of a thiolreactive reagent (N-ethylmaleimide)
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.056 - 1.55
acetyl-CoA
0.008 - 1.69
alpha-D-glucosamine 1-phosphate
0.000009
CoA
-
pH 7.5, 25C
0.07 - 0.25
D-glucosamine 1-phosphate
0.003
N-acetyl-alpha-D-glucosamine 1-phosphate
-
pH 7.5, 25C
0.07
N-acetyl-D-glucosamine 1-phosphate
-
uridyltransferase activity
0.1
UTP
-
uridyltransferase activity
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
82.47 - 853
acetyl-CoA
123.2 - 2311
alpha-D-glucosamine 1-phosphate
12.4
N-acetyl-D-glucosamine 1-phosphate
Escherichia coli
-
GmlU uridyltransferase
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
211 - 1489
alpha-D-glucosamine 1-phosphate
3255
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.042
terreic acid
-
pH 7.3, 37C, substrate alpha-D-glucosamine 1-phosphate
additional information
additional information
-
inhibition kinetics, ping pong bisubstrate rate, overview
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0004 - 0.0059
(1R,2R)-2-[[2,4-dimethoxy-5-(1,2,3,4-tetrahydroquinolin-2-ylsulfonyl)phenyl]carbamoyl]-3-methylcyclopropanecarboxylic acid
0.00038 - 0.00784
(1R,2R)-2-[[4-hydroxy-2-methoxy-5-(1,2,3,4-tetrahydroquinolin-2-ylsulfonyl)phenyl]carbamoyl]-3-methylcyclopropanecarboxylic acid
0.00001 - 0.0053
(1R,2R)-2-[[5-(acridin-10(9H)-ylsulfonyl)-2,4-dimethoxyphenyl]carbamoyl]-3-methylcyclopropanecarboxylic acid
0.00003 - 0.0303
(1R,2R)-2-[[5-(acridin-10(9H)-ylsulfonyl)-4-hydroxy-2-methoxyphenyl]carbamoyl]-3-methylcyclopropanecarboxylic acid
0.0005 - 0.2
(2E)-4-([2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]amino)-4-oxobut-2-enoic acid
0.099
(4Z)-4-(4-benzyloxybenzylidene)-2-(naphthalen-2-yl)-1,3-oxazol-5(4H)-one
Mycobacterium tuberculosis
-
30C, pH not specified in the publication
0.018
(5Z)-2-imino-5-[(2E)-3-(5-nitrofuran-2-yl)prop-2-en-1-ylidene]-1,3-thiazolidin-4-one
Mycobacterium tuberculosis
-
pH not specified in the publication, temperature not specified in the publication
0.0005 - 0.05
1-(2-[[([5-[(3-carboxypropanoyl)amino]-2,4-dimethoxyphenyl]sulfonyl)amino]methyl]phenyl)piperidine-4-carboxylic acid
0.0009 - 0.015
2'-[[([5-[(3-carboxypropanoyl)amino]-2,4-dimethoxyphenyl]sulfonyl)amino]methyl]biphenyl-4-carboxylic acid
0.00067 - 0.01
2-(2-cyanopyridin-4-yl)-N-[2,4-dimethoxy-5-(1,2,3,4-tetrahydroquinolin-2-ylsulfonyl)phenyl]acetamide
0.002 - 0.2
2-([2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]amino)-2-oxoethyl acetate
0.00009 - 0.2
4-([2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]amino)-4-oxobutanoic acid
0.00004 - 0.0084
4-([2,4-dimethoxy-5-[naphthalen-2-yl(phenyl)sulfamoyl]phenyl]amino)-4-oxobutanoic acid
0.000058 - 0.2
4-([4-hydroxy-2-methoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]amino)-4-oxobutanoic acid
0.000018 - 0.2
4-([5-[(4-aminophenyl)(phenyl)sulfamoyl]-2,4-dimethoxyphenyl]amino)-4-oxobutanoic acid
0.00004 - 0.048
4-([5-[bis(4-methylphenyl)sulfamoyl]-2,4-dimethoxyphenyl]amino)-4-oxobutanoic acid
0.003 - 0.2
4-[(2,4-dimethoxy-5-[[2-(piperidin-1-yl)benzyl]sulfamoyl]phenyl)amino]-4-oxobutanoic acid
0.00025 - 0.2
4-[(5-[[2-(4-[[(carboxyacetyl)oxy]methyl]piperidin-1-yl)benzyl]sulfamoyl]-2,4-dimethoxyphenyl)amino]-4-oxobutanoic acid
0.2
4-[2-([2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]amino)-2-oxoethoxy]benzoic acid
0.065
4-[[(2,6-dimethoxybenzoyl)oxy]imino]cyclohexa-2,5-dien-1-one
Mycobacterium tuberculosis
-
pH not specified in the publication, temperature not specified in the publication
0.00009 - 0.0369
4-[[2,4-dimethoxy-5-(10H-phenothiazin-10-ylsulfonyl)phenyl]amino]-4-oxobutanoic acid
0.000007 - 0.2
4-[[2,4-dimethoxy-5-(10H-phenoxazin-10-ylsulfonyl)phenyl]amino]-4-oxobutanoic acid
0.00005 - 0.0466
4-[[4-hydroxy-2-methoxy-5-(1,2,3,4-tetrahydroquinolin-2-ylsulfonyl)phenyl]amino]-4-oxobutanoic acid
0.00003 - 0.055
4-[[5-(dibenzo[b,f][1,4]oxazepin-10(11H)-ylsulfonyl)-2,4-dimethoxyphenyl]amino]-4-oxobutanoic acid
0.00004 - 0.0255
4-[[5-(diphenylsulfamoyl)-2,4-dimethoxyphenyl]amino]-4-oxobutanoic acid
0.0004 - 0.01
4-[[5-([2-[4-(carboxymethyl)piperidin-1-yl]benzyl]sulfamoyl)-2,4-dimethoxyphenyl]amino]-4-oxobutanoic acid
0.003 - 0.2
4-[[5-([2-[4-(hydroxymethyl)piperidin-1-yl]benzyl]sulfamoyl)-2,4-dimethoxyphenyl]amino]-4-oxobutanoic acid
0.0014
5,7-dichloro-2-hydrazinylquinolin-8-ol
Escherichia coli
-
pH not specified in the publication, temperature not specified in the publication
0.015 - 0.2
methyl 2-[([[5-(acetylamino)-2,4-dimethoxyphenyl]sulfonyl]amino)methyl]benzoate
0.11 - 0.2
N-(2,4-dimethoxy-5-[[2-(piperidin-1-yl)benzyl]sulfamoyl]phenyl)acetamide
0.0005 - 0.2
N-([2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]carbamothioyl)glycine
0.005 - 0.2
N-([2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]carbamoyl)glycine
0.00052 - 0.009
N-[2,4-dimethoxy-5-(1,2,3,4-tetrahydroquinolin-2-ylsulfonyl)phenyl]-2-(2-fluoropyridin-4-yl)acetamide
0.00043 - 0.0247
N-[2,4-dimethoxy-5-(1,2,3,4-tetrahydroquinolin-2-ylsulfonyl)phenyl]-3-(2H-tetrazol-5-yl)propanamide
0.02 - 0.2
N-[2,4-dimethoxy-5-(phenylsulfamoyl)phenyl]acetamide
0.08 - 0.2
N-[2,4-dimethoxy-5-(piperidin-1-ylsulfonyl)phenyl]acetamide
0.01 - 0.54
N-[2,4-dimethoxy-5-[(2-methoxybenzyl)sulfamoyl]phenyl]acetamide
0.002 - 0.2
N-[2,4-dimethoxy-5-[(2-methyl-2,3-dihydro-1H-indol-1-yl)sulfonyl]phenyl]acetamide
0.001 - 0.2
N-[2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]-2-(pyridin-4-ylsulfanyl)acetamide
0.0015 - 0.2
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
0.1 - 0.2
N-[2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]methanesulfonamide
0.2
N-[2,4-dimethoxy-5-[(2-methylpyrrolidin-1-yl)sulfonyl]phenyl]acetamide
0.017 - 0.2
N-[2,4-dimethoxy-5-[(3-methylphenyl)sulfamoyl]phenyl]acetamide
0.021 - 0.2
N-[2,4-dimethoxy-5-[(4-methylphenyl)sulfamoyl]phenyl]acetamide
0.003 - 0.2
N-[2,4-dimethoxy-5-[methyl(phenyl)sulfamoyl]phenyl]acetamide
0.002 - 0.2
N-[2,4-dimethoxy-5-[phenyl(propan-2-yl)sulfamoyl]phenyl]acetamide
0.00003 - 0.0099
N-[5-(acridin-10(9H)-ylsulfonyl)-2,4-dimethoxyphenyl]-2-(2-fluoropyridin-4-yl)acetamide
0.00006 - 0.032
N-[5-(acridin-10(9H)-ylsulfonyl)-2,4-dimethoxyphenyl]-2-(pyridin-4-yl)acetamide
0.2
N-[5-(dimethylsulfamoyl)-2,4-dimethoxyphenyl]acetamide
0.04 - 0.2
N-[5-([2-[4-(hydroxymethyl)piperidin-1-yl]benzyl]sulfamoyl)-2,4-dimethoxyphenyl]acetamide
0.2
N-[5-[(1,3-benzodioxol-5-ylmethyl)sulfamoyl]-2,4-dimethoxyphenyl]acetamide
0.004 - 0.2
N-[5-[(2-bromobenzyl)sulfamoyl]-2,4-dimethoxyphenyl]acetamide
0.005 - 0.2
N-[5-[(2-fluorophenyl)sulfamoyl]-2,4-dimethoxyphenyl]acetamide
0.015 - 0.2
N-[5-[(3-fluorophenyl)sulfamoyl]-2,4-dimethoxyphenyl]acetamide
0.025 - 0.2
N-[5-[(4-fluorophenyl)sulfamoyl]-2,4-dimethoxyphenyl]acetamide
0.13 - 0.2
N-[5-[butyl(propan-2-yl)sulfamoyl]-2,4-dimethoxyphenyl]acetamide
0.015 - 0.2
N-[5-[ethyl(2-methylphenyl)sulfamoyl]-2,4-dimethoxyphenyl]acetamide
0.0442
terreic acid
Escherichia coli
-
pH 7.3, 37C
0.0002 - 0.2
[2-([2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]amino)-2-oxoethoxy]acetic acid
0.0001 - 0.2
[[2-([2,4-dimethoxy-5-[(2-methyl-3,4-dihydroquinolin-1(2H)-yl)sulfonyl]phenyl]amino)-2-oxoethyl]sulfanyl]acetic acid
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
0.35
-
pH 7.5, 80C, mutant enzyme H308A
2.2
-
GlcN-1-P acetyltransferase activity
2.85
-
mutant JM83(pFP3-Tr331) + IPTG, uridyltransferase activity
15.1
-
GlcNAc-1-P uridyltransferase activity
23.1
-
pH 7.5, 80C, mutant enzyme N331A
50
-
pH 7.5, 80C, wild-type enzyme enzyme
59.2
-
pH 7.5, 80C, mutant enzyme Y311A
68.9
-
pH 7.5, 80C, mutant enzyme K337A
73.5
-
pH 7.5, 80C, mutant enzyme K340A
75.34
-
pH 7.5, 80C, substrates: acetyl-CoA + alpha-D-glucosamine 1-phosphate
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.3 - 7.4
8.2
-
for both acetyltransferase and uridyltransferase
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7 - 11
-
activity range
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
16 - 80
-
activity range
PDB
SCOP
CATH
ORGANISM
UNIPROT
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Mycobacterium tuberculosis (strain ATCC 25177 / H37Ra)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Streptococcus pneumoniae (strain ATCC BAA-255 / R6)
Streptococcus pneumoniae (strain ATCC BAA-255 / R6)
Yersinia pestis (strain Pestoides F)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
49000
-
gel filtration
54100
-
SDS-PAGE, Western blot
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 54100,, recombinant Histagged GlmU, SDS-PAGE
heterotrimer
homotrimer
-
crystal structure
trimer
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphoprotein
-
GlmU is a substrate of serine/theronine kinase Pkn B of Mycobacterium tuberculosis and is phosphorylated on threonine residues in region 414-439 in its C-terminal region. PknB-mediated phosphorylation signifcantly decreases the acetyltransferase activity of GlmU
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 1922% 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, 20C, 2-7 days, X-ray diffraction structure determination and analysis
-
crystal structures of GlmU in apo form and UDP-N-acetylglucosamine-bound form is determined. The structure shows a two-domain architecture, with an N-terminal domain having an alpha/beta-like fold and with a C-terminal domain that forms a left-handed parallel beta-helix structure
-
crystallized using the hanging drop vapour-diffusion method. Native diffraction data are collected from crystals belonging to space group R32 and processed to a resolution of 2.2 A
-
docking surface representation of the GlmU allosteric site in complex with inhibitor (4Z)-4-(4-benzyloxybenzylidene)-2-(naphthalen-2-yl)-1,3-oxazol-5(4H)-one. Residues Tyr150, Glu250 and Arg 253 are in hydrogen bonding with carbonyl oxygen over the oxazole ring. Leu144, Pro147, Phe148, Tyr150, Ala233, Ala236 and Leu247 participate in strong hydrophobic interactions
-
purified GlmU, sitting drop vapor diffusion method, mixing of 400 nl of 15 mg/ml GlmU in 5 mM acetyl-CoA, 5 mM MgCl2, 5 mM UDP-GlcNAc with 400 nL of 18% PEG 3350, 0.1 M Tris-Cl, pH 8.5, and 2% tacsimate, 7-8 days, for coupling to acetyl-CoA, crystals are soaked in 5 mM GlcN-1-P, 5 mM MgCl2, 5 mM UDP-GlcNAc, 5 mM acetyl-CoA, 18% PEG 3350, 0.1 M Tris-Cl, pH 8.5, and 2% tacsimate, or in 5 mM GlcNAc-1-P, 5 mM MgCl2, 5 mM UDP-GlcNAc, 5 mM CoA, X-ray diffraction structure determination and analysis at 1.98-2.33 A resolution
-
structure of enzyme bound to ATP and N-acetyl-D-glucosamine 1-phosphate
-
the crystal structures of MtGlmU in an unliganded form and in complexes in which either GlcNAc-1-P or UDP-GlcNAc occupies the uridyltransferase active site are determined using the sitting-drop vapour-diffusion method. These structures identify the active-site contacts between protein and ligands and suggest a ternary-complex mechanism of action for the GlmU uridyltransferase reaction
-
using the hanging-drop vapour-diffusion method. GlmU also crystallizes in the cubic space group I432. It diffracts to 3.4 A resolution. This poor diffraction is correlated with a sparse crystal packing leading to the presence of large solvent channels in the crystal, unlike the hexagonal forms. The distinct crystal packing in these two forms may be a result of the involvement of different surfaces in crystal contacts
-
hanging-drop vapour-diffusion method. Crystal structures of the enzyme in unbound form, in complex with acetyl-coenzyme A and in complex with both AcCoA and the end product UDP-GlcNAc, determined and refined to 2.3, 2.5, and 1.75 A, respectively. GlmU molecule is organized in two separate domains connected via a long alpha-helical linker and associates as a trimer, with the 50-A-long left-handed beta-helix (LbH) C-terminal domains packed against each other in a parallel fashion and the C-terminal region extended far away from the LbH core and exchanged with the beta-helix from a neighboring subunit in the trimer. AcCoA binding induces the formation of a long and narrow tunnel, enclosed between two adjacent LbH domains and the interchanged C-terminal region of the third subunit, giving rise to an original active site architecture at the junction of three subunits
-
purified GlmU, hanging drop vapour diffusion method, 20 mg/ml protein in 25 mM TrisHCl, pH 7.5, 50 mM NaCl, 2 mM TCEP, is mixed with 2 mM inhibitor ligand, and incubated on ice for 30 min and centrifuged, then mixed with reservoir solution containing of 18-23% w/v PEG 3350, 200 mM ammonium sulfate and 100 mM PCTP, pH 7.0-8.0, 2-5 days, 20C, X-ray diffraction structure determination and analysis
-
vapor-diffusion method, crystal structure of the enzyme in apo form at 2.33 A resolution, and in complex with UDP-N-acetyl glucosamine and the essential cofactor Mg2+ at 1.96 A resolution. In the crystal, the enzyme forms exact trimers, mainly through contacts between left-handed beta-sheet helix domains. UDP-N-acetylglucosamine and Mg2+ are bound at the uridyltransferase active site, which is in a closed form
-
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
80
-
mutant enzyme DC005 shows the same thermostability as wild-type ST0452 protein, whereas mutant enzyme DC011 denatures and becomes insoluble by 5-min treatment at 80 C. The C-terminal domain of the ST0452 protein, with its LbetaH structure, appears to be essential for the formation of its trimeric form and, in turn, the high stability of the entire ST0452 protein
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
GlmU gene product, bifunctional enzyme with glucosamine-1-phosphate acetyltransferase and uridyltransferase activity
-
recombinant GlmU from Escherichia coli strain BL21(DE3) by anion exchange and hydrophobic interaction chromatography and gel filtration
recombinant GlmU from Escherichia coli strain HMS174(DE3) by anion exchange and hydrophobic interaction chromatography and gel filtration
recombinant N-terminally His-tagged wild-type GlmU and mutant GlmUs from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
-
the recombinant protein by Ni2+ affinity chromatography
-
using a GSTrap glutathione Sepharose column. The GST tag is removed by proteolytic cleavage using recombinant tobacco etch virus protease
-
using gel filtration
-
using Ni-NTA chromatography. The His6 tag is cleaved by incubation with recombinant tobacco etch virus (rTEV) protease
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
-
expressed in Escherichia coli as a GST-fusion protein
-
expressed in Escherichia coli as a His-tagged fusion protein
-
expressed in Escherichia coli strain BL21-Codon Plus(DE3)-RIL
-
expression in Escherichia coli
-
expression in Escherichia coli, expression in Mycobacterium smegmatis ZW-2, a GlmU knoukout strain, activity of GlmU is required for growth of Mycobacterium smegmatis, a gradually reduced enzyme activity in a temperature shift experiment shows that the Mycobacterium smegmatis cells became non-viable and their morphology changes from a normal rod shape to stubby-rounded morphology
-
gene glmU, expression in Escherichia coli strain BL21(DE3)
gene glmU, expression in Escherichia coli strain HMS174(DE3)
gene glmU, expression of GlmU in Lactobacillus casei strain BL309 or PL32, and functional co-overexpression in Lactobacillus casei strain BL23 with genes glmS and glmM encoding GlmS, glucosamine-6-phosphate synthase, and GlmM, phosphoglucosamine mutase, to reconstruct biosynthesis of UDP-N-acetylglucosamine, subcloning in Escherichia coli strain M15 and Lactobacillus lactis strain MG1363
-
gene glmU, expression of N-terminally His-tagged wild-type GlmU and mutant GlmUs in Escherichia coli strain BL21(DE3)
-
GlmU gene cloned from genomic DNA by PCR and inserted into pET3a
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A451R
-
site-directed mutagenesis, neither the single mutants A451R and R439T nor the double mutant A451R/R439T affect the acetyltransferase activity significantly
A451R/R439T
-
site-directed mutagenesis, neither the single mutants A451R and R439T nor the double mutant A451R/R439T affect the acetyltransferase activity significantly
E458A
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme, 86% of wild-type acetyltransferase activity is remaining
K362A
-
site-directed mutagenesis, the enzyme activity of the mutant is abolished by more than 90% of the wild-type acetyltransferase, and the affinity with the two substrates is completely lost
K403A
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme, 27% of wild-type acetyltransferase activity is remaining
K464A
-
site-directed mutagenesis, the mutant shows activity similar to the wild-type enzyme
K464A/W460A
-
site-directed mutagenesis, the mutant shows highly compromised activity compared to the wild-type enzyme
N397A
-
site-directed mutagenesis, the mutant shows highly reduced Vmax in acetyltransfer compared to the wild-type enzyme
N456A
-
site-directed mutagenesis, the mutant shows slightly reduced activity compared to the wild-type enzyme, 67% of wild-type acetyltransferase activity is remaining
R439T
-
site-directed mutagenesis, neither the single mutants A451R and R439T nor the double mutant A451R/R439T affect the acetyltransferase activity significantly
R463A
-
site-directed mutagenesis, the mutant shows unaltered activity compared to the wild-type enzyme
S474A
-
site-directed mutagenesis, the mutant shows unaltered activity compared to the wild-type enzyme
T296A
-
in vitro kinase assays show that the mutant protein is phosphorylated to the same extent as the wild-type GlmU
T308A/T309A/T311A
-
in vitro kinase assays show that the mutant protein is phosphorylated to the same extent as the wild-type GlmU
T324A/T341A/T347A
-
in vitro kinase assays show that the mutant protein is phosphorylated to the same extent as the wild-type GlmU
T365A/T368A/T370A
-
in vitro kinase assays show that the mutant protein is phosphorylated to the same extent as the wild-type GlmU
T376A/T401A/T406A/T407A
-
in vitro kinase assays show that the mutant protein is phosphorylated to the same extent as the wild-type GlmU
T414A/T418A/T425/T432A/T436A
-
in vitro kinase assays show that the mutant protein is not phosphorylated as the wild-type GlmU. These results confine PknB-mediated phosphorylation sites to a smaller region between amino acids 414 and 439 that harbors five threonines
T418A
-
site-directed mutagenesis, T418 is the most abundant phosphorylation site on GlmUMtb, acetyltransferase activity is completely abolishe
T418E
-
site-directed mutagenesis, acetyltransferase activity of T418E mutant that mimics a phosphorylated Thr, is severely compromised compared to wild-type GlmUMtb
T486A/T494A
-
in vitro kinase assays show that the mutant protein is phosphorylated to the same extent as the wild-type GlmU
Y398A
-
site-directed mutagenesis, the enzyme activity of the mutant is abolished by more than 90% of the wild-type acetyltransferase, and the affinity with the two substrates is completely lost
H308A
-
specific activity is 0.7% compared to the wild-type enzyme
K340A
-
specific activity is 147.1% compared to the wild-type enzyme
K377A
-
specific activity is 137.7% compared to the wild-type enzyme
N331A
-
specific activity is 46.1% compared to the wild-type enzyme
Y311A
-
specific activity is 118.4% compared to the wild-type enzyme
H308A
-
specific activity is 0.7% compared to the wild-type enzyme
-
K340A
-
specific activity is 147.1% compared to the wild-type enzyme
-
N331A
-
specific activity is 46.1% compared to the wild-type enzyme
-
Y311A
-
specific activity is 118.4% compared to the wild-type enzyme
-
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
drug development
medicine
Show AA Sequence (946 entries)
Please use the Sequence Search for a certain query.