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Information on EC 2.7.7.64 - UTP-monosaccharide-1-phosphate uridylyltransferase
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EC Tree
2.7.7.64 UTP-monosaccharide-1-phosphate uridylyltransferaseSpecify your search results
Word Map
- 2.7.7.64
- udp-sugars
-
salvage
- pollen
-
udp-glucuronic
-
glucuronic
- myo-inositol
- galactokinase
- udp-glca
-
bifidobacterium
-
glc-1-p
- l-arabinose
-
galacturonic
- ugpase
- glucose-1-phosphate
- infantis
- synthesis
-
sugar-1-phosphates
- galactose-1-phosphate
- molecular biology
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
AtUSP, GL50803_29307, PsUSP, TcSloppy, UDP-Gal/Glc PPase, UDP-galactose/glucose pyrophosphorylase, UDP-sugar pyrophosphorylase, UGGPase, USP, USPase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
AtUSP
GL50803_29307
UDP-sugar pyrophosphorylase
USP
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
UTP + a monosaccharide 1-phosphate = diphosphate + UDP-monosaccharide
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
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CAS REGISTRY NUMBER
COMMENTARY
223918-15-8
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
4-azido-D-galactose 1-phosphate + UTP
UDP-4-azido-D-galactose + diphosphate
-
-
43% conversion rate
-
?
6-deoxy-D-galactose 1-phosphate + UTP
UDP-6-deoxy-D-galactose + diphosphate
-
-
29% conversion rate
-
?
D-galactose 1-phosphate + TTP
TDP-D-galactose + diphosphate
-
-
-
?
D-galacturonate 1-phosphate + UTP
UDP-D-galacturonate + diphosphate
-
-
-
?
D-glucuronic acid 1-phosphate + UTP
UDP-glucuronic acid + diphosphate
-
-
-
?
diphosphate + UDP-D-glucose
UTP + alpha-D-glucose 1-phosphate
-
-
-
r
L-arabinopyranose 1-phosphate + UTP
UDP-L-arabinopyranose + diphosphate
-
-
-
?
L-arabinose 1-phosphate + UTP
UDP-L-arabinose + diphosphate
-
-
-
?
N-acetylglucosamine 1-phosphate + UTP
UDP-N-acetylglucosamine + diphosphate
poorly catalysed reaction
-
-
?
TTP + alpha-D-glucose 1-phosphate
diphosphate + TDP-D-glucose
-
-
-
?
UDP-galacturonic acid + diphosphate
galacturonic acid 1-phosphate + UTP
-
reduced activity in floret extracts depleted for AtUSP by immunprecipitation: only endogenous UDP-galacturonic acid-utilizing pyrophosphorylase activity and final step in myo-inositol oxidation pathway
-
-
?
UDP-monosaccharide + diphosphate
monosaccharide 1-phosphate + UTP
salvage pathway
-
-
r
UTP + a monosaccharide 1-phosphate
diphosphate + UDP-monosaccharide
the enzyme catalyzes the formation of various UDP-sugars at the end of salvage pathways
-
-
?
UTP + alpha-D-galacturonate
diphosphate + UDP-alpha-D-galacturonate
-
-
-
r
UTP + alpha-D-galacturonate 1-phosphate
diphosphate + UDP-D-galacturonate
-
-
-
-
?
UTP + alpha-D-glucuronate 1-phosphate
diphosphate + UDP-D-glucuronate
-
-
-
?
UTP + arabinose 1-phosphate
diphosphate + UDP-arabinose
70.5% of enzyme activity with glucose 1-phosphate
-
-
r
UTP + beta-L-arabinopyranose
diphosphate + UDP-beta-L-arabinopyranose
-
-
-
r
UTP + D-galacturonic acid 1-phosphate
diphosphate + UDP-galacturonic acid
-
equilibrium constant is 0.24
-
-
r
UTP + D-glucuronic acid 1-phosphate
diphosphate + UDP-D-glucuronic acid
71.3% of enzyme activity with glucose 1-phosphate
-
-
r
UTP + D-xylopyranose 1-phosphate
diphosphate + UDP-D-xylopyranose
-
-
-
r
UTP + D-xylose 1-phosphate
diphosphate + UDP-xylose
35.9% of enzyme activity with glucose 1-phosphate
-
-
r
UTP + L-arabinose 1-phosphate
diphosphate + UDP-beta-L-arabinopyranose
-
-
-
?
UTP + monosaccharide 1-phosphate
diphosphate + UDP-monosaccharide
-
the enzyme has a critical role in pollen development. The products of the AtUSP reaction can act as precursors for the synthesis of glycolipids, glycoproteins, and cell wall components including pectin and hemicellulose
-
-
?
UTP + N-acetyl-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetylglucosamine
4.3% of enzyme activity with glucose 1-phosphate
-
-
r
D-galactose 1-phosphate + UTP
UDP-D-galactose + diphosphate
-
-
95% conversion rate
-
?
D-galactose 1-phosphate + UTP
UDP-D-galactose + diphosphate
-
-
-
?
D-galactose 1-phosphate + UTP
UDP-D-galactose + diphosphate
-
-
-
?
D-galactose 1-phosphate + UTP
UDP-D-galactose + diphosphate
-
30% of the activity with D-glucose 1-phosphate
-
-
?
D-galactose 1-phosphate + UTP
UDP-galactose + diphosphate
-
-
-
?
D-glucose 1-phosphate + UTP
UDP-D-glucose + diphosphate
-
-
28% conversion rate
-
?
D-glucose 1-phosphate + UTP
UDP-D-glucose + diphosphate
preferred substrates
-
-
?
D-glucose 1-phosphate + UTP
UDP-D-glucose + diphosphate
preferred substrates
-
-
?
D-glucose 1-phosphate + UTP
UDP-D-glucose + diphosphate
-
-
-
?
D-glucose 1-phosphate + UTP
UDP-glucose + diphosphate
pH 7, 35°C, 2 mM Mg2+
reaction stop by boiling, analysis of products by HPLC (monitoring at 262 nm)
-
r
UDP + alpha-D-glucose 1-phosphate
UDP-alpha-D-glucose + diphosphate
-
-
-
-
r
UDP + alpha-D-glucose 1-phosphate
UDP-alpha-D-glucose + diphosphate
-
-
-
-
r
UTP + alpha-D-galactose 1-phosphate
diphosphate + UDP-D-galactose
-
-
-
?
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-D-glucose
-
-
-
r
UTP + D-galactose 1-phosphate
diphosphate + UDP-galactose
116% of the activity with glucuronic acid 1-phosphate
-
-
?
UTP + D-galactose 1-phosphate
diphosphate + UDP-galactose
-
-
-
r
UTP + D-galactose 1-phosphate
diphosphate + UDP-galactose
116.2% of enzyme activity with glucose 1-phosphate
-
-
r
UTP + D-galactose 1-phosphate
diphosphate + UDP-galactose
-
3% of the activity with N-acetylglucosamine 1-phosphate
-
-
?
UTP + D-galactose 1-phosphate
diphosphate + UDP-galactose
-
3% of the activity with N-acetylglucosamine 1-phosphate
-
-
?
UTP + D-glucose 1-phosphate
diphosphate + UDP-glucose
114% of the activity with glucuronic acid 1-phosphate
-
-
r
UTP + D-glucose 1-phosphate
diphosphate + UDP-glucose
UTP specific
-
-
r
UTP + D-glucose 1-phosphate
diphosphate + UDP-glucose
-
159% of the activity with N-acetylglucosamine 1-phosphate
-
-
?
UTP + D-glucose 1-phosphate
diphosphate + UDP-glucose
-
159% of the activity with N-acetylglucosamine 1-phosphate
-
-
?
UTP + D-glucuronic acid 1-phosphate
diphosphate + UDP-glucuronic acid
-
-
-
r
UTP + D-glucuronic acid 1-phosphate
diphosphate + UDP-glucuronic acid
-
-
-
?
UTP + D-mannose 1-phosphate
diphosphate + UDP-mannose
-
5% of the activity with N-acetylglucosamine 1-phosphate
-
-
?
UTP + D-mannose 1-phosphate
diphosphate + UDP-mannose
-
5% of the activity with N-acetylglucosamine 1-phosphate
-
-
?
UTP + D-xylose 1-phosphate
diphosphate + UDP-alpha-D-xylopyranose
-
-
-
?
UTP + D-xylose 1-phosphate
diphosphate + UDP-alpha-D-xylopyranose
-
44% of the activity with N-acetylglucosamine 1-phosphate
-
-
?
UTP + D-xylose 1-phosphate
diphosphate + UDP-alpha-D-xylopyranose
-
44% of the activity with N-acetylglucosamine 1-phosphate
-
-
?
UTP + N-acetylglucosamine 1-phosphate
diphosphate + UDP-N-acetylglucosamine
-
-
-
-
?
UTP + N-acetylglucosamine 1-phosphate
diphosphate + UDP-N-acetylglucosamine
-
-
-
-
?
additional information
?
-
no activity detectable for substrates L-fucose 1-phosphate and mannose 1-phosphate
-
-
-
additional information
?
-
-
the enzyme preferentially generates UDP-glucose and UDP-galactose, but it may also activate other hexose- or pentose-1-phosphates such as galacturonic acid-1-phosphate or arabinose-1-phosphate
-
-
-
additional information
?
-
-
the Leishmania major UDP-sugar pyrophosphorylase exhibits a broad substrate specificity in vitro
-
-
-
additional information
?
-
the UDP-sugar pyrophosphorylase of Trypanosoma cruzi shows a broader substrate specificity, the nucleotidyltransferase is capable of transforming different types of sugar 1-phosphates and NTP into NDP-sugars
-
-
-
additional information
?
-
-
the UDP-sugar pyrophosphorylase of Trypanosoma cruzi shows a broader substrate specificity, the nucleotidyltransferase is capable of transforming different types of sugar 1-phosphates and NTP into NDP-sugars
-
-
-
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
TTP + alpha-D-glucose 1-phosphate
diphosphate + TDP-D-glucose
-
-
-
?
UDP-galacturonic acid + diphosphate
galacturonic acid 1-phosphate + UTP
-
reduced activity in floret extracts depleted for AtUSP by immunprecipitation: only endogenous UDP-galacturonic acid-utilizing pyrophosphorylase activity and final step in myo-inositol oxidation pathway
-
-
?
UDP-monosaccharide + diphosphate
monosaccharide 1-phosphate + UTP
salvage pathway
-
-
r
UTP + a monosaccharide 1-phosphate
diphosphate + UDP-monosaccharide
the enzyme catalyzes the formation of various UDP-sugars at the end of salvage pathways
-
-
?
UTP + alpha-D-galactose 1-phosphate
diphosphate + UDP-D-galactose
-
-
-
?
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-D-glucose
-
-
-
r
UTP + alpha-D-glucuronate 1-phosphate
diphosphate + UDP-D-glucuronate
-
-
-
?
UTP + D-galactose 1-phosphate
diphosphate + UDP-galactose
-
-
-
r
UTP + monosaccharide 1-phosphate
diphosphate + UDP-monosaccharide
-
the enzyme has a critical role in pollen development. The products of the AtUSP reaction can act as precursors for the synthesis of glycolipids, glycoproteins, and cell wall components including pectin and hemicellulose
-
-
?
additional information
?
-
-
the enzyme preferentially generates UDP-glucose and UDP-galactose, but it may also activate other hexose- or pentose-1-phosphates such as galacturonic acid-1-phosphate or arabinose-1-phosphate
-
-
-
additional information
?
-
the UDP-sugar pyrophosphorylase of Trypanosoma cruzi shows a broader substrate specificity, the nucleotidyltransferase is capable of transforming different types of sugar 1-phosphates and NTP into NDP-sugars
-
-
-
additional information
?
-
-
the UDP-sugar pyrophosphorylase of Trypanosoma cruzi shows a broader substrate specificity, the nucleotidyltransferase is capable of transforming different types of sugar 1-phosphates and NTP into NDP-sugars
-
-
-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Co2+
-
divalent metal required. Mn2+ (3 mM) is 63% as effective as Mg2+ (3 mM)
Mg2+
Mn2+
Mg2+
; absolute requirement for divalent cation, maximal activity in presence of Mg2+ or Mn2+. Maximal activity in presence of 2 mM Mg2+
Mg2+
-
divalent metal required. Order of decreasing effectiveness: Mg2+ > Mn2+ > Co2+. Optimal concentration of Mg2+ is 5 mM
Mg2+
Mg2+ or Mn2+ required; the enzyme requires bivalent ions, Mg2+ or Mn2+, for its activity
Mn2+
-
divalent metal required. Mn2+ (3 mM) is 87% as effective as Mg2+ (3 mM)
Mn2+
Mg2+ or Mn2+ required; the enzyme requires bivalent ions, Mg2+ or Mn2+, for its activity
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
hydrogen peroxide
inactivation, reactivation by reduction using cysteine or thioredoxin
nitric oxide
inactivation, reactivation by reduction using cysteine or thioredoxin
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
8.14
dTTP
-
pH not specified in the publication, temperature not specified in the publication
3.74
dUTP
-
pH not specified in the publication, temperature not specified in the publication
0.09
D-galactose 1-phosphate
cosubstrate UTP, S0.5 value, pH 8.0, 37°C
0.86
D-galactose 1-phosphate
forward reaction, pH 7.8, 25°C; forward reaction, pH 7.8, 25°C
0.13
D-glucose 1-phosphate
cosubstrate UTP, S0.5 value, pH 8.0, 37°C
0.177
D-glucose 1-phosphate
co-substrate: UTP, pH 7.6, 37°C; forward reaction, pH 7.6, 37°C
0.36
D-glucose 1-phosphate
cosubstrate TTP, S0.5 value, pH 8.0, 37°C
0.307
diphosphate
reverse reaction, co-substrate: UDP-D-galactose, pH 7.8, 25°C; reverse reaction, UDP-galactose, pH 7.8, 25°C
0.383
diphosphate
reverse reaction, co-substrate: UDP-D-glucose, pH 7.8, 25°C; reverse reaction, UDP-glucose, pH 7.8, 25°C
0.728
diphosphate
reverse reaction, co-substrate: UDP-D-galacturonate, pH 7.8, 25°C; reverse reaction, UDP-alpha-D-galacturonate, pH 7.8, 25°C
1.01
diphosphate
reverse reaction, co-substrate: UDP-L-arabinopyranose, pH 7.8, 25°C
1.018
diphosphate
reverse reaction, UDP-beta-L-arabinopyranose, pH 7.8, 25°C
0.9
TTP
cosubstrate D-glucose 1-phosphate, S0.5 value, pH 8.0, 37°C
0.0284
UTP
forward reaction, pH 7.6, 37°C; pH 7.6, 37°C, recombinant enzyme
0.08
UTP
cosubstrate D-galactose 1-phosphate, S0.5 value, pH 8.0, 37°C
0.098
UTP
forward reaction, co-substrate: D-galactose 1-phosphate, pH 7.8, 25°C; forward reaction, D-galactose 1-phosphate, pH 7.8, 25°C
0.116
UTP
forward reaction, co-substrate: D-glucose 1-phosphate, pH 7.8, 25°C; forward reaction, D-glucose 1-phosphate, pH 7.8, 25°C
0.14
UTP
cosubstrate D-glucose 1-phosphate, S0.5 value, pH 8.0, 37°C
2.88
UTP
-
pH not specified in the publication, temperature not specified in the publication
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
27
dTTP
-
pH not specified in the publication, temperature not specified in the publication
219
dUTP
-
pH not specified in the publication, temperature not specified in the publication
219
D-galactose 1-phosphate
forward reaction, pH 7.8, 25°C; forward reaction, pH 7.8, 25°C
191
D-glucose 1-phosphate
forward reaction, pH 7.8, 25°C; forward reaction, pH 7.8, 25°C
15
diphosphate
reverse reaction, co-substrate: UDP-D-galacturonate, pH 7.8, 25°C; reverse reaction, UDP-alpha-D-galacturonate, pH 7.8, 25°C
81
diphosphate
reverse reaction, co-substrate: UDP-L-arabinopyranose, pH 7.8, 25°C; reverse reaction, UDP-beta-L-arabinopyranose, pH 7.8, 25°C
174
diphosphate
reverse reaction, co-substrate: UDP-D-galactose, pH 7.8, 25°C; reverse reaction, UDP-galactose, pH 7.8, 25°C
185
diphosphate
reverse reaction, co-substrate: UDP-D-glucose, pH 7.8, 25°C; reverse reaction, UDP-glucose, pH 7.8, 25°C
201
UTP
forward reaction, co-substrate: D-galactose 1-phosphate, pH 7.8, 25°C; forward reaction, D-galactose 1-phosphate, pH 7.8, 25°C
209
UTP
forward reaction, co-substrate: D-glucose 1-phosphate, pH 7.8, 25°C; forward reaction, D-glucose 1-phosphate, pH 7.8, 25°C
348
UTP
-
pH not specified in the publication, temperature not specified in the publication
additional information
D-galactose 1-phosphate
-
Kcat/KM: 490000 1/M/sec, pH 7, 35°C
additional information
D-glucose 1-phosphate
-
Kcat/KM: 530000 1/M/sec, pH 7, 35°C
additional information
D-glucuronic acid 1-phosphate
-
Kcat/KM: 710000 1/M/sec, pH 7, 35°C
additional information
D-xylose 1-phosphate
-
Kcat/KM: 51000 1/M/sec, pH 7, 35°C
additional information
diphosphate
-
Kcat/KM: 860000 1/M/sec, pH 7, 35°C
additional information
L-arabinose 1-phosphate
-
Kcat/KM: 92000 1/M/sec, pH 7, 35°C
additional information
UDP-glucose
-
Kcat/KM: 480000 1/M/sec, pH 7, 35°C
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3.3
dTTP
-
pH not specified in the publication, temperature not specified in the publication
59
dUTP
-
pH not specified in the publication, temperature not specified in the publication
150
D-glucose 1-phosphate
co-substrate: UTP, pH 7.6, 37°C; forward reaction, pH 7.6, 37°C
20.8
diphosphate
reverse reaction, co-substrate: UDP-D-galacturonate, pH 7.8, 25°C
81.2
diphosphate
reverse reaction, co-substrate: UDP-L-arabinopyranose, pH 7.8, 25°C
492
diphosphate
reverse reaction, co-substrate: UDP-D-glucose, pH 7.8, 25°C
580
diphosphate
reverse reaction, co-substrate: UDP-D-galactose, pH 7.8, 25°C
121
UTP
-
pH not specified in the publication, temperature not specified in the publication
1830
UTP
forward reaction, co-substrate: D-glucose 1-phosphate, pH 7.8, 25°C
2090
UTP
forward reaction, co-substrate: D-galactose 1-phosphate, pH 7.8, 25°C
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
143-255% UDP-L-arabinose synthesising activity in extracts from transgenic plants (aerial parts) compared to wild-type plant; 25% of wild-type UDP-L-arabinose synthesising activity in plant extracts (aerial parts) upon repression of AtUSP gene expression; no activity detectable for substrates L-fucose 1-phosphate and mannose 1-phosphate
additional information
relative activity, alpha-D-galacturonate 1-phosphate, 1.6%, forward reaction, + UTP, pH 7.8, 25°C; relative activity, D-galactose 1-phosphate, 100%, forward reaction, + UTP, pH 7.8, 25°C; relative activity, D-glucose 1-phosphate, 88%, forward reaction, + UTP, pH 7.8, 25°C; relative activity, D-xylopyranose 1-phosphate, 12%, forward reaction, + UTP, pH 7.8, 25°C; relative activity, UDP-alpha-D-galacturonate, 7.1%, reverse reaction, + diphosphate, pH 7.8, 25°C; relative activity, UDP-beta-L-arabinopyranose, 33%, reverse reaction, + diphosphate, pH 7.8, 25°C; relative activity, UDP-galactose, 83%, reverse reaction, + diphosphate, pH 7.8, 25°C; relative activity, UDP-glucose, 100%, reverse reaction, + diphosphate, pH 7.8, 25°C
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 9
-
pH 5.0: about 75% of maximal activity, pH 9.0: about 50% of maximal activity
5.5 - 8
-
pH 5.5: about 90% of maximal activity, pH 8.0: about 75% of maximal activity
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
45
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
65 - 95
-
65°C: about 60% of maximal activity, 95°C: 90% of maximal activity
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
ecotype Columbia, Landsberg erecta, Wassilewskija
UniProt
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
AtUSP mRNA-specific qRT-PCR, strong expression in vascular tissue (promoter: beta-glucuronidase assay)
brenda
-
relatively high levels in most cell types (AtUSP mRNA-specific qRT-PCR)
brenda
-
young leaves (AtUSP mRNA-specific qRT-PCR), strong expression in vascular tissue (promoter: beta-glucuronidase assay)
brenda
-
the enzyme is essential for development of viable pollen
brenda
-
AtUSP mRNA-specific qRT-PCR, strong expression in vascular tissue (promoter: beta-glucuronidase assay), essential for pollen development since loss-of-function mutation in enzyme causes male infertility
brenda
-
strong expression in growing region (promoter: beta-glucuronidase assay), young roots (AtUSP mRNA-specific qRT-PCR)
brenda
-
young seedlings, expression in most cell types (AtUSP mRNA-specific qRT-PCR)
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
USP1 and USP2, differential centrifugation and Western blot
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
-
A knock-out of the USP gene results in non-fertile pollen. Mutant plants show an arabinose reduction in the cell wall, and accumulate mainly two sugars, arabinose and xylose, in the cytoplasm
metabolism
-
the enzyme, likely involved in monosaccharide salvage, preferentially generates UDP-glucose and UDP-galactose, but it may also activate other hexose- or pentose-1-phosphates such as galacturonic acid-1-phosphate or arabinose-1-phosphate
physiological function
additional information
-
active site conformations of apoenzyme and ligand-bound enzyme, substrate binding structures, structure-function analysis, modeling, overview
physiological function
USP is able to complement the growth defect of Escherichia coli galU mutant strain DEV6. This specific bacterial strain is unable to grow on agar-containing galactose as the only carbohydrate source due to a mutation in UDP-glucose pyrophosphorylase
physiological function
the parasite enzyme with such broad substrate specificities suggests an alternative pathway that might play an essential role for nucleotide-sugar biosynthesis and for the regulation of the NDP-sugar pool in the parasite
physiological function
-
enzyme is able to complement an Escherichia coli GalU mutant
physiological function
gene silencing of USP by miRNA causes a concomitant reduction of USP and of glucuronokinase activity presumably to prevent the accumulation of sugar-1-phosphates interfering with normal metabolism and depleting the phosphate pool of the cell
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
Sequence
A0A086KSR3_TOXGO
623
0
67895
TrEMBL
S8FZQ5_TOXGM
Toxoplasma gondii (strain ATCC 50611 / Me49)
623
0
67852
TrEMBL
S7WA78_TOXGG
Toxoplasma gondii (strain ATCC 50853 / GT1)
623
0
67895
TrEMBL
A0A125YJQ9_TOXGV
Toxoplasma gondii (strain ATCC 50861 / VEG)
623
0
67852
TrEMBL
A8BJJ7_GIAIC
Giardia intestinalis (strain ATCC 50803 / WB clone C6)
450
0
49294
TrEMBL
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
66000
67000
69700
USP-His6, apparent molecular mass determind by gel filtration and standard kurve
70000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
additional information
?
x * 66040, calculated from sequence; x * 67000, SDS-PAGE; x * 67000, SDS-PAGE
additional information
-
overall structure of the enzyme, structure-function analysis, overview
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structures of a USP in the APO-, UTP-, and UDP-sugar-bound forms is presented. The overall structure of the enzyme exhibits a significant structural homology to other nucleotidyldiphosphate-glucose pyrophosphorylases. The broad substrate specificity is strongly correlated with the flexibility of the SB-loop and, in contrast to UDP-glucose pyrophosphorylase of Leishmania major, the spacious sugar binding cavity as well as the multiple conformations observed for the residues involved in sugar moiety binding
-
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate fractionation, ion exchange chromatography (DEAE), hydrophobic interaction chromatography, gel filtration and ion exchange chromatography (DEAE), recombinant protein: immobilized metal ion affinity chromatography, splitting off the fused thioredoxin and His-tag, ion exchange chromatography (DEAE); recombinant
chelating chromatography (elution: 250 mM imidazole) followed by cleavage of N-terminal thioredoxin- and His-tag with thrombin and DEAE Sepharose FF chromatography
-
on a 1-ml HisTrap HP Ni2+-chelating, a HiPrep 26/10 desalting, and a 1-ml Q-Sepharose FF anion exchange column; using Ni-NTA chromatography, ion-exchange and gel filtration
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3)pLysS by nickel affinity chromatography and gel filtration; using Ni-NTA chromatography
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
; His-tagged thioredoxin fusion protein expressed in Escherichia coli BL21gold strain
expressed in Escherichia coli as a His-tagged fusion protein; gene TcSloppy, DNA and amino acid sequence determination and analysis, phylogenetic analysis and sequence comparisons, expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)pLysS
expressed in Escherichia coli as a His-tagged fusion protein; into the vector pET22b for expression in Escherichia coli BL21DE3 cells
expression in Escherichia coli
from cDNA generated from total RNA from 2-week-old seedlings in pGEM T-Easy for amplification and in pET32a for inducible expression with N-terminal thioredoxin- and His-tag in Escherichia coli BL21(DE3) and in pBI121 for generation of transgenic plants via Agrobacterium tumefaciens
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
molecular biology
-
polyclonal rabbit anti-AtUSP antibody recognizes USP1 and USP2
synthesis
synthesis
-
the enzyme is useful for the highly efficient production of UDP-galacturonic acid for studies on pectin biosynthesis
synthesis
-
use of UDP-sugar pyrophosphorylase (USP) from Arabidopsis thaliana with a galactokinase from Streptococcus pneumoniae TIGR4 (SpGalK) and an inorganic diphosphatase (PPase) to effectively synthesize UDP-sugars
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Ohashi, T.; Cramer, N.; Ishimizu, T.; Hase, S.
Preparation of UDP-galacturonic acid using UDP-sugar pyrophosphorylase
Anal. Biochem.
352
182-187
2006
Pisum sativum
brenda
Kim, J.S.; Koh, S.; Shin, H.J.; Lee, D.S.; Lee, S.Y.
Biochemical characterization of a UDP-sugar pyrophosphorylase from Thermus caldophilus GK24
Biotechnol. Appl. Biochem.
29
11-17
1999
Thermus caldophilus, Thermus caldophilus GK24
brenda
Kotake, T.; Yamaguchi, D.; Ohzono, H.; Hojo, S.; Kaneko, S.; Ishida, H.K.; Tsumuraya, Y.
UDP-sugar pyrophosphorylase with broad substrate specificity toward various monosaccharide 1-phosphates from pea sprouts
J. Biol. Chem.
279
45728-45736
2004
Pisum sativum, Pisum sativum (Q5W915)
brenda
Litterer, L.A.; Plaisance, K.L.; Schnurr, J.A.; Storey, K.K.; Jung, H.J.G.; Gronwald, J.W.; Somers, D.A.
Biosynthesis of UDP-glucuronic acid in developing soybean embryos: Possible role of UDP-sugar pyrophosphorylase
Physiol. Plant.
128
200-211
2006
Glycine max (Q09WE7)
-
brenda
Schnurr, J.A.; Storey, K.K.; Jung, H.J.; Somers, D.A.; Gronwald, J.W.
UDP-sugar pyrophosphorylase is essential for pollen development in Arabidopsis
Planta
224
520-532
2006
Arabidopsis thaliana
brenda
Dai, N.; Petreikov, M.; Portnoy, V.; Katzir, N.; Pharr, D.M.; Schaffer, A.A.
Cloning and expression analysis of a UDP-galactose/glucose pyrophosphorylase from melon fruit provides evidence for the major metabolic pathway of galactose metabolism in raffinose oligosaccharide metabolizing plants
Plant Physiol.
142
294-304
2006
Cucumis melo (Q0GZS3)
brenda
Kotake, T.; Hojo, S.; Yamaguchi, D.; Aohara, T.; Konishi, T.; Tsumuraya, Y.
Properties and physiological functions of UDP-sugar pyrophosphorylase in Arabidopsis
Biosci. Biotechnol. Biochem.
71
761-771
2007
Arabidopsis thaliana (Q9C5I1)
brenda
Gronwald, J.W.; Miller, S.S.; Vance, C.P.
Arabidopsis UDP-sugar pyrophosphorylase: Evidence for two isoforms
Plant Physiol. Biochem.
46
1101-1105
2008
Arabidopsis thaliana (Q9C5I1)
brenda
Siddique, S.; Endres, S.; Atkins, J.M.; Szakasits, D.; Wieczorek, K.; Hofmann, J.; Blaukopf, C.; Urwin, P.E.; Tenhaken, R.; Grundler, F.M.; Kreil, D.P.; Bohlmann, H.
Myo-inositol oxygenase genes are involved in the development of syncytia induced by Heterodera schachtii in Arabidopsis roots
New Phytol.
184
457-472
2009
Arabidopsis thaliana (Q9C5I1)
brenda
Damerow, S.; Lamerz, A.C.; Haselhorst, T.; Fuehring, J.; Zarnovican, P.; von Itzstein, M.; Routier, F.H.
Leishmania UDP-sugar pyrophosphorylase: the missing link in galactose salvage?
J. Biol. Chem.
285
878-887
2010
Leishmania major (D3G6S4), Leishmania major, Leishmania major (Q4QE75)
brenda
Muthana, M.M.; Qu, J.; Li, Y.; Zhang, L.; Yu, H.; Ding, L.; Malekan, H.; Chen, X.
Efficient one-pot multienzyme synthesis of UDP-sugars using a promiscuous UDP-sugar pyrophosphorylase from Bifidobacterium longum (BLUSP)
Chem. Commun. (Camb. )
48
2728-2730
2012
Bifidobacterium longum, Bifidobacterium longum ATCC 55813
brenda
Yang, T.; Bar-Peled, M.
Identification of a novel UDP-sugar pyrophosphorylase with a broad substrate specificity in Trypanosoma cruzi
Biochem. J.
429
533-543
2010
Trypanosoma cruzi (D3YBH2), Trypanosoma cruzi
brenda
Dickmanns, A.; Damerow, S.; Neumann, P.; Schulz, E.C.; Lamerz, A.C.; Routier, F.H.; Ficner, R.
Structural basis for the broad substrate range of the UDP-sugar pyrophosphorylase from Leishmania major
J. Mol. Biol.
405
461-478
2011
Leishmania major (D3G6S4), Leishmania major, no activity in Homo sapiens
brenda
Geserick, C.; Tenhaken, R.
UDP-sugar pyrophosphorylase is essential for arabinose and xylose recycling, and is required during vegetative and reproductive growth in Arabidopsis
Plant J.
74
239-247
2013
Arabidopsis thaliana
brenda
Ebrecht, A.C.; Asencion Diez, M.D.; Piattoni, C.V.; Guerrero, S.A.; Iglesias, A.A.
The UDP-glucose pyrophosphorylase from Giardia lamblia is redox regulated and exhibits promiscuity to use galactose-1-phosphate
Biochim. Biophys. Acta
1850
88-96
2015
Giardia intestinalis (A8BJJ7), Giardia intestinalis ATCC 50803 (A8BJJ7)
brenda
Liu, J.; Zou, Y.; Guan, W.; Zhai, Y.; Xue, M.; Jin, L.; Zhao, X.; Dong, J.; Wang, W.; Shen, J.; Wang, P.G.; Chen, M.
Biosynthesis of nucleotide sugars by a promiscuous UDP-sugar pyrophosphorylase from Arabidopsis thaliana (AtUSP)
Bioorg. Med. Chem. Lett.
23
3764-3768
2013
Arabidopsis thaliana
brenda
Kim, B.; Ahn, J.
Characterization of uridine diphosphate-sugar pyrophosphorylase from Populus deltoids
J. Korean Soc. Appl. Biol. Chem.
56
525-531
2013
Populus deltoides
-
brenda
Geserick, C.; Tenhaken, R.
UDP-sugar pyrophosphorylase controls the activity of proceeding sugar-1-kinases enzymes
Plant Signal. Behav.
8
e25478
2013
Arabidopsis thaliana (Q9C5I1)
brenda
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