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
Amino sugar and nucleotide sugar metabolism
-
-
anhydromuropeptides recycling
-
-
Biosynthesis of antibiotics
-
-
Metabolic pathways
-
-
UDP-N-acetyl-D-galactosamine biosynthesis II
-
-
UDP-N-acetyl-D-glucosamine biosynthesis I
-
-
UDP-N-acetyl-D-glucosamine biosynthesis II
-
-
UDP-GlcNAc biosynthesis
-
-
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
-
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
-
-
-
Manually annotated by BRENDA team
-
-
-
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
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
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
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-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-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
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1-[(2S,3S,4R,5S)-3,4-dihydroxy-5-(hydroxymethyl)tetrahydrofuran-2-yl]dihydropyrimidine-2,4(1H,3H)-dione
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
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
-
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
-
5-Hydroxyuridine
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-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
p-chloromercuribenzoate
pseudouridine
streptomycin
0.5 mg/ml, 74% reduction in activity
UDP-N-acetyl-D-glucosamine
-
slight product inhibition in reverse reaction
UMP
-
inhibits catabolic reaction
uridine
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 - 0.03
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
-
Km values are 3.54 microM/l, 13.9 microM/l, 4.22 microM/l, 13.3 microM/l for isoforms MP I, MP II, MP III, MP IV, respcetively
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
6.21
diphosphate
Sulfolobus tokodaii
-
pH 7.5, 80C
2.54
N-acetyl-alpha-D-glucosamine 1-phosphate
Sulfolobus tokodaii
-
pH 7.5, 80C
0.015 - 330
N-acetyl-D-glucosamine 1-phosphate
8.4
UDP-N-acetyl-alpha-D-glucosamine
Sulfolobus tokodaii
-
pH 7.5, 80C
44.3
UDP-N-acetyl-D-glucosamine
Escherichia coli
-
-
3.04 - 3.53
UTP
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
380
diphosphate
Sulfolobus tokodaii
-
pH 7.5, 80C
17
320
N-acetyl-alpha-D-glucosamine 1-phosphate
Sulfolobus tokodaii
-
pH 7.5, 80C
2569
110 - 160
N-acetyl-D-glucosamine 1-phosphate
1449
530
UDP-N-acetyl-alpha-D-glucosamine
Sulfolobus tokodaii
-
pH 7.5, 80C
1424
15 - 18
UDP-N-acetyl-D-galactosamine
356
220 - 460
UDP-N-acetyl-D-glucosamine
126
120 - 2120
UTP
65
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
0.018
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
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.17
-
purified enzyme, pH 7.4, 37C
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 - 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 OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
28 - 37
-
isoform MP IV
30 - 36
-
isoform MP III
51 - 68
-
isoform MP II
52 - 66
-
isoform MP I
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
-
very high activity
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
-
-
Manually annotated by BRENDA team
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
trimer
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
generation of a three-dimensional model, using human GlcNAc1p nucleotidyltransferase complexed with UDP-GlcNAc, PDB code 1JV1; generation of a three-dimensional model, using human GlcNAc1p nucleotidyltransferase complexed with UDP-GlcNAc, PDB code 1JV1
hanging drop vapour diffusion method
-
sitting-drop vapour-diffusion method
-
to 1.8 A resolution. UAP exhibits the same three-domain global architecture as other UAPs, it appears to lack three alpha-helices at the N-terminus and contains two amino acids in the allosteric pocket that make it appear more like the human enzyme than that from Trypanosoma brucei
recombinant enzyme, hanging drop vapor diffusion method
-
a 1.9 A resolution crystal structure of a synthetic small-molecule inhibitor (4-chloro-N-(3-methoxypropyl)-N-[1-(2-phenylethyl)piperidin-3-yl]benzamide) of GlmU is presented. The determined crystal structure indicate 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
structure-based drug design studies. The molecular recognition of the enzyme with the substrates occurs mainly by hydrogen bonds between ligands and Arg116, Arg383, Gly381, and Lys408 amino acids, and few hydrophobic interactions with Tyr382 and Lys123 residues
hanging drop vapour diffusion method, using 20% PEG 3350, 0.15 M DL-malate pH 7.0
-
recombinant enzyme, hanging drop vapor diffusion method
-
in complex with inhibitor 3-[2-(1,3-benzodioxol-5-yl)-2-oxoethyl]-4-bromo-3-hydroxy-5-methyl-1,3-dihydro-2H-indol-2-one. Only the (R)-enantiomer binds, and it is likely that the kinked shape of the molecule is crucial for its shape-complimentarity to the pocket. The benzo[1,3]dioxole moiety is deeply buried, making close contact with Ala397 and Gly232 at the bottom of the cleft. The indolin-2-one sits at the top of the cleft, with the unsubstituted edge exposed to solvent and the methyl and bromide substituents on making contact with Ala239, Met370, Lys371, and Ala367
homology modeling of structure based on Haemophilus influenzae enzyme, PDB entry 2V0K
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 7.5
-
most stable
643061
6.5 - 7.5
-
most stable
643065
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40
-
5 min, 50% of activity lost in the absence of dithiothreitol, 20% of activity lost in presence of dithiothreitol
80
-
half-life: 180 min
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
completely insensitive to millimolar concentrations of thiol reagents
-
dithiothreitol increases thermal stability
dithiothreitol stabilizes, activity lost during storage can be recovered by addition of dithiothreitol
-
labile toward fractionation with ammonium sulfate, inactivation can not be reversed by dialysis
-
more stable toward ammonium sulfate then calf liver enzyme
-
stable towards ammonium sulfate, unstable in prolonged dialysis
-
substrate binding increases enzyme stability against thermal inactivation
-
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
organic solvents
-
labile to fractionation with
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, 1 month, 10% loss of activity
-
-20C, 1 month, 40% loss of activity
-
-20C, 20 mM Tris-HCl, pH 7.5, 1 mM EDTA, 1 mM 2-mercaptoethanol, 4 months, 10% loss of activity
-
-20C, 30 mM Tris-HCl, pH 7.5, 20% glycerol, 0.1 mM dithiothreitol, 6 months, stable
-
-20C, acetone precipitated enzyme, 3 months, no loss of activity
-
-20C, crude extract, 5-10% loss of activity per day of storage
-
-20C, extremely unstable
-
-20C, phosphate buffer, pH 7.5, stable for at least 2 weeks
-
-20C, purified enzyme or crude extract, 2 months, 10% loss of activity
-
-20C, purified enzyme, 10% loss of activity per week of storage
-
0C, 2 weeks, 50% loss of activity
-
0C, 20 mM Tris-HCl, pH 7.5, 1 mM EDTA, 1 mM 2-mercaptoethanol, 0.05% NaN3, 5 months, 50% loss of activity
-
25C, 1 mM dithiothreitol, 1 mM N-acetyl-D-glucosamine 1-phosphate, 20h, 30% loss of activity
-
4C, phosphate buffer, pH 7.4, 0.1 mM dithiothreitol, stable
-
4C, phosphate buffer, pH 7.5, 0.01 mM dithiothreitol, stable for at least 2 weeks
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
from encysting and non-encysting cells
-
full length and truncated enzymes using His-tag
-
glutathione Sepharose column chromatography and GSTrap column chromatography
-
glutathione Sepharose column chromatography and Superdex 75 gel filtration
-
GST fusion protein from E. coli
His-tag used for purifcation
-
recombinant enzyme
-
recombinant protein using His-tag
-
recombinant proteins using His-tag
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
AGX1 and AGX 2 expressed in Escherichia coli as GST fusion protein
-
AGX1 expressed in Escherichia coli as GST fusion protein
-
expressed as His-tag fusion protein in Escherichia coli M15
-
expressed in Escherichia coli
expressed in Escherichia coli as GST fusion protein, complementation of Saccharomyces cerevisiae deficiency mutant, all recombinant enzymes found to be active
expressed in Escherichia coli BL21 (DE3) cells
-
expressed in Escherichia coli JM109 cells as a glutathione S-transferase fusion protein
-
expressed in M15 cells
-
expression in Escherichia coli
expression in Escherichia coli, wild-type and truncated enzyme form lacking the 170-residues C-terminal domain
-
expression in Escherichia coli; expression in Escherichia coli
native and mutant enzymes expressed as His-tag fusion protein in Escherichia coli M15
-
overexpressed in Escherichia coli, His-tag inserted for purification
-
overexpression in host strain
-
replacement of several amino acids, GST fusion protein
truncated and full length enzyme overexpressed in Escherichia coli, His-tag inserted for purification
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
20-hydroxyecdysone and ecdysteroid agonist halofenozide activate the expression of the UAP1; 20-hydroxyecdysone and ecdysteroid agonist halofenozide activate the expression of the UAP2. Juvenile hormone, juvenile hormone analog pyriproxyfen and an increase in juvenile hormone by RNAi of allatostatin gene AS-C upregulate UAP2
KT282116, KT282117
a decrease in 20-hydroxyecdysone by RNAi of an ecdysteroidogenesis gene SHD and a 20E signaling gene FTZ-F1 repress the expression; a decrease in 20-hydroxyecdysone by RNAi of an ecdysteroidogenesis gene SHD and a 20E signaling gene FTZ-F1 repress the expression. Juvenile hormone, juvenile hormone analog pyriproxyfen and an increase in juvenile hormone by RNAi of allatostatin gene AS-C downregulate UAP1
KT282116, KT282117
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
DELTA1-130
-
deletion of N-terminus, very low activity
DELTA1-182
-
deletion of N-terminus, very low activity
DELTA1-227
-
deletion of N-terminus, very low activity
DELTA1-233
-
deletion of N-terminus, very low activity
DELTA1-250
-
deletion of N-terminus
DELTA1-26
-
deletion of N-terminus
DELTA1-78
-
deletion of N-terminus, very low activity
DELTA227-456
-
deletion of C-terminus
DELTA250-456
-
deletion of C-terminus, low activity
DELTA331-456
-
deletion of C-terminus, roughly 50% of activity
DELTA1-130
-
deletion of N-terminus, very low activity
-
DELTA1-182
-
deletion of N-terminus, very low activity
-
DELTA1-227
-
deletion of N-terminus, very low activity
-
DELTA1-26
-
deletion of N-terminus
-
DELTA1-78
-
deletion of N-terminus, very low activity
-
G108A
-
dramatically reduced activity, significant increase in melting temperature
G210A
-
dramatically reduced activity, significant decrease in melting temperature
G111A
-
very low activity
G222A
-
traces of activity in forward and reverse reaction with N-acetyl-D-glucosamine 1-phosphate and N-acetyl-D-galactosamine 1-phosphate
G224A
-
low activity in forward and reverse reaction with N-acetyl-D-glucosamine 1-phosphate and N-acetyl-D-galactosamine 1-phosphate
P220A
-
only slight changes in activity with N-acetyl-D-glucosamine 1-phosphate and N-acetyl-D-galactosamine 1-phosphate
R115A
-
slight changes in Km
Y227A
-
only slight changes in activity with N-acetyl-D-glucosamine 1-phosphate and N-acetyl-D-galactosamine 1-phosphate
G111A
very low activity
G112A
traces of activity
G114A
25% of activity
K123A
traces of activity
L117A
very low activity
P122 A
35% of activity
R116A
traces of activity
T115A
50% of activity
D208A
-
enhanced UDP-N-acetylglucosamine diphosphorylase activity under optimal conditions; exhibits slightly weaker UDP-N-acetylglucosamine diphosphorylase activity than wild-type enzyme
E146A
-
exhibits slightly weaker UDP-N-acetylglucosamine diphosphorylase activity than wild-type enzyme
G9A
-
enhanced UDP-N-acetylglucosamine diphosphorylase activity under optimal conditions
K147A
-
enhanced UDP-N-acetylglucosamine diphosphorylase activity under optimal conditions
R13A
-
shows the same activity as wild-type protein
T80A
-
enhanced UDP-N-acetylglucosamine diphosphorylase activity under optimal conditions
Y97A
-
enhanced UDP-N-acetylglucosamine diphosphorylase activity under optimal conditions
Y97F
-
enhanced UDP-N-acetylglucosamine diphosphorylase activity under optimal conditions
E146A
-
exhibits slightly weaker UDP-N-acetylglucosamine diphosphorylase activity than wild-type enzyme
-
G9A
-
enhanced UDP-N-acetylglucosamine diphosphorylase activity under optimal conditions
-
K147A
-
enhanced UDP-N-acetylglucosamine diphosphorylase activity under optimal conditions
-
Y97F
-
enhanced UDP-N-acetylglucosamine diphosphorylase activity under optimal conditions
-
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
medicine
synthesis
Show AA Sequence (11018 entries)
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