BRENDA home
History
Information on EC 2.7.7.64 - UTP-monosaccharide-1-phosphate uridylyltransferase
for references in articles please use BRENDA:EC2.7.7.64Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
2.7.7.64 UTP-monosaccharide-1-phosphate uridylyltransferaseSpecify your search results
Word Map
- 2.7.7.64
- udp-sugars
-
gal-1-p
- udp-glucose
- udp-glca
- synthesis
-
phytohormones
-
pisum
- sativum
-
co-substrate
- 1-phosphates
- l-arabinose
-
three-enzyme
- glycolipids
- molecular biology
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
AtUSP, GL50803_29307, HvUSP, PsUSP, TcSloppy, UDP-Gal/Glc PPase, UDP-galactose/glucose pyrophosphorylase, UDP-sugar pyrophosphorylase, UDP-sugar-producing pyrophosphorylase, UGGPase, 
more
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
AtUSP
GL50803_29307
UDP-sugar pyrophosphorylase
USP
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
UTP + a monosaccharide 1-phosphate = diphosphate + UDP-monosaccharide
-
-
-
-
UTP + a monosaccharide 1-phosphate = diphosphate + UDP-monosaccharide
UDP-sugar-producing pyrophosphorylases catalyze reversible reactions, require magnesium for catalysis, and act through an ordered sequential Bi-Bi reaction mechanism. In the forward reaction, UTP binds before the sugar 1-phosphate, and after catalysis, inorganic diphosphate is released before the UDP-sugar
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PATHWAY SOURCE
PATHWAYS
KEGG
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CAS REGISTRY NUMBER
COMMENTARY
223918-15-8
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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 + alpha-L-arabinose 1-phosphate
diphosphate + UDP-L-arabinose
-
-
-
?
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-D-xylose
-
-
-
ir
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, 35ĆĀ°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-alpha-D-galactose
-
-
-
r
UTP + alpha-D-galactose 1-phosphate
diphosphate + UDP-alpha-D-galactose
preferred substrates
-
-
r
UTP + alpha-D-galactose 1-phosphate
diphosphate + UDP-alpha-D-galactose
-
-
-
r
UTP + alpha-D-galactose 1-phosphate
diphosphate + UDP-D-galactose
-
-
-
?
UTP + alpha-D-galactose 1-phosphate
diphosphate + UDP-D-galactose
-
-
-
?
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-alpha-D-glucose
-
-
-
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-alpha-D-glucose
-
-
-
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-alpha-D-glucose
-
-
-
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-D-glucose
-
-
-
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-D-glucose
-
-
-
r
UTP + alpha-D-glucuronate 1-phosphate
diphosphate + UDP-alpha-D-glucuronate
-
-
-
r
UTP + alpha-D-glucuronate 1-phosphate
diphosphate + UDP-alpha-D-glucuronate
-
-
-
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
?
-
enzyme HvUSP has a promiscuous substrate spectrum. It is not active with ATP, CTP, GTP or dTTP, and in combination with UTP HvUSP shows conversion in decreasing order of Gal-1-P, Glc-1-P, GlcA-1-P and Xyl-1-P. No activity with mannose-1phosphate, N-acetyl-glucosamine-1-phosphate, glucosamine-1-phosphate, or fucose-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
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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 + D-xylose 1-phosphate
diphosphate + UDP-D-xylose
-
-
-
ir
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 + alpha-D-galactose 1-phosphate
diphosphate + UDP-alpha-D-galactose
-
-
-
r
UTP + alpha-D-galactose 1-phosphate
diphosphate + UDP-alpha-D-galactose
-
-
-
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-alpha-D-glucose
-
-
-
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-alpha-D-glucose
-
-
-
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-alpha-D-glucose
-
-
-
r
UTP + alpha-D-glucuronate 1-phosphate
diphosphate + UDP-alpha-D-glucuronate
-
-
-
r
UTP + alpha-D-glucuronate 1-phosphate
diphosphate + UDP-alpha-D-glucuronate
-
-
-
r
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
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Co2+
Mg2+
Mn2+
Zn2+
additional information
Co2+
-
divalent metal required. Mn2+ (3 mM) is 63% as effective as Mg2+ (3 mM)
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+
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+
the enzyme requires bivalent ions, Mg2+ or Mn2+, for its activity
additional information
the enzyme requires bivalent cations for activity. HvUSP accepts other bivalent cation such as Ca2+, Mn2+, and Zn2+, but prefers Mg2+
additional information
the enzyme requires bivalent cations for activity. HvUSP accepts other bivalent cation such as Co2+, Ni2+, Mn2+ and Zn2+, but prefers Mg2+
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(3R)-1-(4-chlorobenzoyl)-N-(3,4-dihydro-2H-1,5-benzodioxepin-7-yl)piperidine-3-carboxamide
compound (3R)-1-(4-chlorobenzoyl)-N-(3,4-dihydro-2H-1,5-benzodioxepin-7-yl)piperidine-3-carboxamide preferentially binds to one site located in the proximity of the active center of the enzyme
2-(furan-2-yl)-N'-(indol-3-ylidenemethyl)quinoline-4-carbohydrazide
-
2-[(3As,7aR)-1,3-dioxo-3a,4,7,7a-tetrahydroisoindol-2-yl]-N-[4-(propan-2-ylsulfamoyl)phenyl]acetamide
-
2-[3-(trifluoromethyl)anilino]-1,3-thiazol-4-one
compound 2-[3-(trifluoromethyl)anilino]-1,3-thiazol-4-on preferentially binds to one site located in the proximity of the active center of the enzyme
ethyl 2,4-dimethyl-5-[(2R)-2-[4-(2-phenoxyethyl)piperazin-1-yl]propanoyl]-1H-pyrrole-3-carboxylate
-
hydrogen peroxide
inactivation, reactivation by reduction using cysteine or thioredoxin
methyl (2R)-2-[[2-(4-fluorophenyl)sulfanylacetyl]amino]-3-hydroxypropanoate
-
nitric oxide
inactivation, reactivation by reduction using cysteine or thioredoxin
additional information
identification of structurally diverse scaffolds for the development of USP inhibitors by fragment library screening, selection of small molecule inhibitors with allosteric regulation sites, that inhibit both Leishmania major USP and UGP. Inhibitor binding kinetics, computational docking study, overview
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Dehydration
The Promoter of AtUSP Is Co-regulated by Phytohormones and Abiotic Stresses in Arabidopsis thaliana.
Infections
Functional characterization of the Arabidopsis universal stress protein AtUSP with an antifungal activity.
utp-monosaccharide-1-phosphate uridylyltransferase deficiency
UDP-sugar pyrophosphorylase - a new old mechanism for sugar activation.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
0.79
UDP-alpha-D-galacturonate
reverse reaction, pH 7.8, 25ĆĀ°C
0.373
UDP-beta-L-arabinopyranose
reverse reaction, pH 7.8, 25ĆĀ°C
0.2765
alpha-D-galactose 1-phosphate
mutant V330W/F383R, pH and temperature not specified in the publication
0.3
alpha-D-galactose 1-phosphate
pH 7.5, 37ĆĀ°C, recombinant enzyme
0.364
alpha-D-galactose 1-phosphate
mutant F383Rd-type enzyme, pH and temperature not specified in the publication
0.529
alpha-D-galactose 1-phosphate
wild-type enzyme, pH and temperature not specified in the publication
1.007
alpha-D-galactose 1-phosphate
mutant F199W, pH and temperature not specified in the publication
1.255
alpha-D-galactose 1-phosphate
mutant V330W, pH and temperature not specified in the publication
0.177
alpha-D-glucose 1-phosphate
pH 7.6, 37ĆĀ°C, recombinant enzyme
0.09
D-galactose 1-phosphate
cosubstrate UTP, S0.5 value, pH 8.0, 37ĆĀ°C
0.86
D-galactose 1-phosphate
forward reaction, pH 7.8, 25ĆĀ°C
0.13
D-glucose 1-phosphate
cosubstrate UTP, S0.5 value, pH 8.0, 37ĆĀ°C
0.36
D-glucose 1-phosphate
cosubstrate TTP, S0.5 value, pH 8.0, 37ĆĀ°C
0.307
diphosphate
reverse reaction, UDP-galactose, pH 7.8, 25ĆĀ°C
0.307
diphosphate
reverse reaction, co-substrate: UDP-D-galactose, pH 7.8, 25ĆĀ°C
0.383
diphosphate
reverse reaction, UDP-glucose, pH 7.8, 25ĆĀ°C
0.383
diphosphate
reverse reaction, co-substrate: UDP-D-glucose, pH 7.8, 25ĆĀ°C
0.728
diphosphate
reverse reaction, UDP-alpha-D-galacturonate, pH 7.8, 25ĆĀ°C
0.728
diphosphate
reverse reaction, co-substrate: UDP-D-galacturonate, pH 7.8, 25ĆĀ°C
1.01
diphosphate
reverse reaction, co-substrate: UDP-L-arabinopyranose, pH 7.8, 25ĆĀ°C
1.018
diphosphate
reverse reaction, UDP-beta-L-arabinopyranose, pH 7.8, 25ĆĀ°C
0.9
TTP
cosubstrate D-glucose 1-phosphate, S0.5 value, pH 8.0, 37ĆĀ°C
0.08
UTP
cosubstrate D-galactose 1-phosphate, S0.5 value, pH 8.0, 37ĆĀ°C
0.098
UTP
forward reaction, D-galactose 1-phosphate, pH 7.8, 25ĆĀ°C
0.098
UTP
forward reaction, co-substrate: D-galactose 1-phosphate, pH 7.8, 25ĆĀ°C
0.116
UTP
forward reaction, D-glucose 1-phosphate, pH 7.8, 25ĆĀ°C
0.116
UTP
forward reaction, co-substrate: D-glucose 1-phosphate, pH 7.8, 25ĆĀ°C
0.14
UTP
cosubstrate D-glucose 1-phosphate, S0.5 value, pH 8.0, 37ĆĀ°C
2.88
UTP
-
pH not specified in the publication, temperature not specified in the publication
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
Michaelis-Menten kinetics
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
13
UDP-alpha-D-galacturonate
reverse reaction, pH 7.8, 25ĆĀ°C
72
UDP-beta-L-arabinopyranose
reverse reaction, pH 7.8, 25ĆĀ°C
319.32
alpha-D-galactose 1-phosphate
mutant V330W, pH and temperature not specified in the publication
90.25
alpha-D-galactose 1-phosphate
mutant F199W, pH and temperature not specified in the publication
216.45
alpha-D-galactose 1-phosphate
wild-type enzyme, pH and temperature not specified in the publication
25.58
alpha-D-galactose 1-phosphate
mutant V330W/F383R, pH and temperature not specified in the publication
17.33
alpha-D-galactose 1-phosphate
mutant F383Rd-type enzyme, pH and temperature not specified in the publication
81
diphosphate
reverse reaction, UDP-beta-L-arabinopyranose, pH 7.8, 25ĆĀ°C
81
diphosphate
reverse reaction, co-substrate: UDP-L-arabinopyranose, pH 7.8, 25ĆĀ°C
185
diphosphate
reverse reaction, co-substrate: UDP-D-glucose, pH 7.8, 25ĆĀ°C
174
diphosphate
reverse reaction, UDP-galactose, pH 7.8, 25ĆĀ°C
174
diphosphate
reverse reaction, co-substrate: UDP-D-galactose, pH 7.8, 25ĆĀ°C
185
diphosphate
reverse reaction, co-substrate: UDP-D-glucose, pH 7.8, 25ĆĀ°C
15
diphosphate
reverse reaction, co-substrate: UDP-D-galacturonate, pH 7.8, 25ĆĀ°C
15
diphosphate
reverse reaction, UDP-alpha-D-galacturonate, pH 7.8, 25ĆĀ°C
348
UTP
-
pH not specified in the publication, temperature not specified in the publication
209
UTP
forward reaction, co-substrate: D-glucose 1-phosphate, pH 7.8, 25ĆĀ°C
209
UTP
forward reaction, D-glucose 1-phosphate, pH 7.8, 25ĆĀ°C
201
UTP
forward reaction, co-substrate: D-galactose 1-phosphate, pH 7.8, 25ĆĀ°C
201
UTP
forward reaction, D-galactose 1-phosphate, pH 7.8, 25ĆĀ°C
additional information
D-galactose 1-phosphate
Kcat/KM: 490000 1/M/sec, pH 7, 35ĆĀ°C
additional information
D-glucose 1-phosphate
Kcat/KM: 530000 1/M/sec, pH 7, 35ĆĀ°C
additional information
D-glucuronic acid 1-phosphate
Kcat/KM: 710000 1/M/sec, pH 7, 35ĆĀ°C
additional information
D-xylose 1-phosphate
Kcat/KM: 51000 1/M/sec, pH 7, 35ĆĀ°C
additional information
diphosphate
Kcat/KM: 860000 1/M/sec, pH 7, 35ĆĀ°C
additional information
L-arabinose 1-phosphate
Kcat/KM: 92000 1/M/sec, pH 7, 35ĆĀ°C
additional information
UDP-glucose
Kcat/KM: 480000 1/M/sec, pH 7, 35ĆĀ°C
additional information
UTP
Kcat/KM: 1400000 1/M/sec, pH 7, 35ĆĀ°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
409.17
alpha-D-galactose 1-phosphate
wild-type enzyme, pH and temperature not specified in the publication
254.44
alpha-D-galactose 1-phosphate
mutant V330W, pH and temperature not specified in the publication
92.51
alpha-D-galactose 1-phosphate
mutant V330W/F383R, pH and temperature not specified in the publication
89.62
alpha-D-galactose 1-phosphate
mutant F199W, pH and temperature not specified in the publication
47.61
alpha-D-galactose 1-phosphate
mutant F383Rd-type enzyme, pH and temperature not specified in the publication
580
diphosphate
reverse reaction, co-substrate: UDP-D-galactose, pH 7.8, 25ĆĀ°C
492
diphosphate
reverse reaction, co-substrate: UDP-D-glucose, pH 7.8, 25ĆĀ°C
580
diphosphate
reverse reaction, co-substrate: UDP-D-galactose, pH 7.8, 25ĆĀ°C
20.8
diphosphate
reverse reaction, co-substrate: UDP-D-galacturonate, pH 7.8, 25ĆĀ°C
81.2
diphosphate
reverse reaction, co-substrate: UDP-L-arabinopyranose, pH 7.8, 25ĆĀ°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, 25ĆĀ°C
2090
UTP
forward reaction, co-substrate: D-galactose 1-phosphate, pH 7.8, 25ĆĀ°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0781 - 0.1066
(3R)-1-(4-chlorobenzoyl)-N-(3,4-dihydro-2H-1,5-benzodioxepin-7-yl)piperidine-3-carboxamide
Leishmania major
wild-type enzyme, pH 8.0, 25ĆĀ°C
0.1698 - 0.1948
2-(5,6-dimethylthieno[2,3-d]pyrimidin-4-yl)oxybenzamide
Leishmania major
wild-type enzyme, pH 8.0 25ĆĀ°C
0.25
2-(furan-2-yl)-N'-(indol-3-ylidenemethyl)quinoline-4-carbohydrazide
Leishmania major
above, wild-type enzyme, pH 8.0, 25ĆĀ°C
0.25
2-[(3As,7aR)-1,3-dioxo-3a,4,7,7a-tetrahydroisoindol-2-yl]-N-[4-(propan-2-ylsulfamoyl)phenyl]acetamide
Leishmania major
above, wild-type enzyme, pH 8.0, 25ĆĀ°C
0.135 - 0.175
2-[3-(trifluoromethyl)anilino]-1,3-thiazol-4-one
Leishmania major
wild-type enzyme, pH 8.0, 25ĆĀ°C
0.0404 - 0.0463
ethyl 2,4-dimethyl-5-[(2R)-2-[4-(2-phenoxyethyl)piperazin-1-yl]propanoyl]-1H-pyrrole-3-carboxylate
Leishmania major
wild-type enzyme, pH 8.0, 25ĆĀ°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
63.9
additional information
additional information
25% of wild-type UDP-L-arabinose synthesising activity in plant extracts (aerial parts) upon repression of AtUSP gene expression
additional information
no activity detectable for substrates L-fucose 1-phosphate and mannose 1-phosphate
additional information
143-255% UDP-L-arabinose synthesising activity in extracts from transgenic plants (aerial parts) compared to wild-type plant
additional information
relative activity, UDP-glucose, 100%, reverse reaction, + diphosphate, pH 7.8, 25ĆĀ°C
additional information
relative activity, UDP-glucose, 100%, reverse reaction, + diphosphate, pH 7.8, 25ĆĀ°C
additional information
relative activity, UDP-galactose, 83%, reverse reaction, + diphosphate, pH 7.8, 25ĆĀ°C
additional information
relative activity, UDP-galactose, 83%, reverse reaction, + diphosphate, pH 7.8, 25ĆĀ°C
additional information
relative activity, UDP-beta-L-arabinopyranose, 33%, reverse reaction, + diphosphate, pH 7.8, 25ĆĀ°C
additional information
relative activity, UDP-beta-L-arabinopyranose, 33%, reverse reaction, + diphosphate, pH 7.8, 25ĆĀ°C
additional information
relative activity, UDP-alpha-D-galacturonate, 7.1%, reverse reaction, + diphosphate, pH 7.8, 25ĆĀ°C
additional information
relative activity, UDP-alpha-D-galacturonate, 7.1%, reverse reaction, + diphosphate, pH 7.8, 25ĆĀ°C
additional information
relative activity, D-xylopyranose 1-phosphate, 12%, forward reaction, + UTP, pH 7.8, 25ĆĀ°C
additional information
relative activity, D-glucose 1-phosphate, 88%, forward reaction, + UTP, pH 7.8, 25ĆĀ°C
additional information
relative activity, D-glucose 1-phosphate, 88%, forward reaction, + UTP, pH 7.8, 25ĆĀ°C
additional information
relative activity, D-galactose 1-phosphate, 100%, forward reaction, + UTP, pH 7.8, 25ĆĀ°C
additional information
relative activity, D-galactose 1-phosphate, 100%, forward reaction, + UTP, pH 7.8, 25ĆĀ°C
additional information
relative activity, alpha-D-galacturonate 1-phosphate, 1.6%, forward reaction, + UTP, pH 7.8, 25ĆĀ°C
additional information
relative activity, alpha-D-galacturonate 1-phosphate, 1.6%, forward reaction, + UTP, pH 7.8, 25ĆĀ°C
additional information
relative activity, D-xylopyranose 1-phosphate, 12%, forward reaction, + UTP, pH 7.8, 25ĆĀ°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.8
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
45
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
65 - 95
-
65ĆĀ°C: about 60% of maximal activity, 95ĆĀ°C: 90% of maximal activity
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
ecotype Columbia, Landsberg erecta, Wassilewskija
UniProt
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
enzyme assay on homogenate of transgenic plants
brenda
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
USP1 and USP2, differential centrifugation and Western blot
brenda
USP1, differential centrifugation and Western blot
-
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
physiological function
additional information
active site conformations of apoenzyme and ligand-bound enzyme, substrate binding structures, structure-function analysis, modeling, overview
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
malfunction
inactivation of the two parasite diphosphorylases UGP and USP, results in parasite death
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
metabolism
Leishmania parasites possess a UDP-sugar pyrophosphorylase (USP), which has broad substrate specificity and is involved in monosaccharide salvage
metabolism
UDP-sugar pyrophosphorylases are involved in the plant salvage pathways
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
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
-
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
physiological function
Leishmania parasites express a UDP-sugar pyrophosphorylase (USP) responsible for monosaccharides salvage that is able to generate both UDP-Gal and UDP-Glc. In vitro, Leishmania USP preferentially uses UTP as a nucleotide donor, and can activate a variety of sugar-1-phosphates. The enzyme is most active with galactose 1-phosphate and glucose 1-phosphate, with a slight preference for the former, but it cannot activate N-acetylated sugars. UDP-sugar-producing diphosphorylases catalyze reversible reactions, require magnesium for catalysis, and act through an ordered sequential Bi-Bi reaction mechanism. In the forward reaction, UTP binds before the sugar 1-phosphate, and after catalysis, inorganic diphosphate is released before the UDP-sugar
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). USP_ARATH
614
0
67852
Swiss-Prot
Secretory Pathway (Reliability: 5)
USP_CUCME
614
0
67788
Swiss-Prot
Chloroplast (Reliability: 5)
USP_ORYSI
616
0
67462
Swiss-Prot
other Location (Reliability: 3)
USP_ORYSJ
616
0
67509
Swiss-Prot
other Location (Reliability: 2)
USP_PEA
600
0
66177
Swiss-Prot
other Location (Reliability: 3)
USP1_SOYBN
600
0
66126
Swiss-Prot
other Location (Reliability: 2)
A0A086M7A5_TOXGO
428
0
46688
TrEMBL
other Location (Reliability: 1)
A0A086L242_TOXGO
195
0
21225
TrEMBL
other Location (Reliability: 1)
A0A086L235_TOXGO
397
0
42978
TrEMBL
Mitochondrion (Reliability: 3)
S7WA78_TOXGG
Toxoplasma gondii (strain ATCC 50853 / GT1)
623
0
67895
TrEMBL
other Location (Reliability: 1)
A0A5B7CIF2_DAVIN
151
0
17458
TrEMBL
Secretory Pathway (Reliability: 3)
A0A5B6YVD8_DAVIN
333
0
37383
TrEMBL
Mitochondrion (Reliability: 4)
A0A3S7WUL7_LEIDO
630
0
68576
TrEMBL
other Location (Reliability: 2)
A0A2G8YCG0_TOXGO
195
0
21182
TrEMBL
other Location (Reliability: 1)
A0A5B6YUV0_DAVIN
394
0
43544
TrEMBL
other Location (Reliability: 5)
A0A086PXZ0_TOXGO
238
0
25986
TrEMBL
Mitochondrion (Reliability: 2)
A0A5B7C043_DAVIN
115
0
13319
TrEMBL
other Location (Reliability: 3)
A4H971_LEIBR
630
0
68701
TrEMBL
other Location (Reliability: 2)
A0A023AZ38_GRENI
978
0
109407
TrEMBL
other Location (Reliability: 1)
A0A1Z5JBW2_FISSO
588
0
65351
TrEMBL
other Location (Reliability: 2)
A0A086M7A9_TOXGO
195
0
21225
TrEMBL
other Location (Reliability: 1)
A0A0D2NCC2_9CHLO
183
0
18624
TrEMBL
other Location (Reliability: 2)
A0A1Z5KLZ9_FISSO
657
0
72153
TrEMBL
Secretory Pathway (Reliability: 4)
A0A425HZJ1_TOXGO
195
0
21225
TrEMBL
other Location (Reliability: 1)
A0A086K0F6_TOXGO
448
0
49224
TrEMBL
other Location (Reliability: 1)
A0A2G8YD59_TOXGO
428
0
46644
TrEMBL
other Location (Reliability: 1)
A0A125YJQ9_TOXGV
Toxoplasma gondii (strain ATCC 50861 / VEG)
623
0
67852
TrEMBL
other Location (Reliability: 1)
A0A139Y9D5_TOXGO
428
0
46672
TrEMBL
other Location (Reliability: 1)
Q4QE75_LEIMA
630
0
68980
TrEMBL
other Location (Reliability: 2)
A0A086L231_TOXGO
30
0
3613
TrEMBL
other Location (Reliability: 1)
A0A0B2SC43_GLYSO
633
0
69768
TrEMBL
Chloroplast (Reliability: 5)
A0A086K0H6_TOXGO
101
0
11225
TrEMBL
Mitochondrion (Reliability: 4)
A0A1Z5KMY8_FISSO
655
0
71782
TrEMBL
Secretory Pathway (Reliability: 4)
A0A5B7C7Q0_DAVIN
146
0
16285
TrEMBL
other Location (Reliability: 4)
A0A072V120_MEDTR
600
0
66135
TrEMBL
other Location (Reliability: 2)
A0A3R8BWW3_TOXGO
428
0
46688
TrEMBL
other Location (Reliability: 1)
A0A1Z5JQB3_FISSO
588
0
65170
TrEMBL
other Location (Reliability: 1)
A0A086QTA8_TOXGO
428
0
46688
TrEMBL
other Location (Reliability: 1)
A0A2I0A1U9_9ASPA
656
0
73405
TrEMBL
other Location (Reliability: 3)
A0A139Y968_TOXGO
195
0
21198
TrEMBL
other Location (Reliability: 1)
A0A086QT99_TOXGO
195
0
21198
TrEMBL
other Location (Reliability: 1)
A0A5B6YXD8_DAVIN
319
0
35487
TrEMBL
other Location (Reliability: 5)
S8FZQ5_TOXGM
Toxoplasma gondii (strain ATCC 50611 / Me49)
623
0
67852
TrEMBL
other Location (Reliability: 1)
A0A086PY20_TOXGO
433
0
47253
TrEMBL
other Location (Reliability: 1)
A4HXJ3_LEIIN
630
0
68576
TrEMBL
other Location (Reliability: 2)
A0A086KSR3_TOXGO
623
0
67895
TrEMBL
other Location (Reliability: 1)
A0A088S6K9_9TRYP
630
0
68550
TrEMBL
other Location (Reliability: 2)
A0A5B6YTK4_DAVIN
626
0
68930
TrEMBL
other Location (Reliability: 3)
B6AFL1_CRYMR
Cryptosporidium muris (strain RN66)
651
1
72025
TrEMBL
Secretory Pathway (Reliability: 1)
A8BJJ7_GIAIC
Giardia intestinalis (strain ATCC 50803 / WB clone C6)
450
0
49294
TrEMBL
other Location (Reliability: 2)
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PDB
SCOP
CATH
UNIPROT
ORGANISM
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
66000
67000
69700
USP-His6, apparent molecular mass determind by gel filtration and standard kurve
70000
66000
USP-His6, determined by SDS-PAGE and Western blot analysis
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
additional information
additional information
overall structure of the enzyme, structure-function analysis, overview
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
F383R
site-directed mutagenesis, the mutant shows 88% reduction of catalytic efficiency compared to the wild-type enzyme enzyme with substrate alpha-D-galactose 1-phosphate
V199W
site-directed mutagenesis, the mutant shows 78% reduction of catalytic efficiency compared to the wild-type enzyme with substrate alpha-D-galactose 1-phosphate
V330W
site-directed mutagenesis, the mutant shows 38% reduction of catalytic efficiency compared to the wild-type enzyme enzyme with substrate alpha-D-galactose 1-phosphate
V330W/F383R
site-directed mutagenesis, the mutant shows 77% reduction of catalytic efficiency compared to the wild-type enzyme enzyme with substrate alpha-D-galactose 1-phosphate
additional information
additional information
functional UDP-sugar diphosphorylase from Arabidopsis thaliana, constitutively expressed in Pichia pastoris and secreted into the extracellular medium, is used for synthesis of UDP-alpha-D-glucuronate, purification of the UDP-sugar from medium by anion exchange chromatography. Purification and assay methods optimization, overview. The fermentation of Pichia pastoris strain SMD1168H-C-AtUSP is performed at 30ĆĀ°C and pH 7.0 throughout the procedure, 20% glucose is supplemented at a rate of 9 ml/h, and DO is maintained at over 20%. After 60 h, the cell wet weight stabilizes (a wet weight of 276.7 g/l is obtained at 96 h). The crude enzyme activity increases up to 84 h, then it is stabilized, with activity 1601 U/ml. Thus, USP activity increases in 5-l fermenter compared with that in shaken flasks. The optimal temperature is around 35ĆĀ°C, lower than the optimal temperature of enzymatic reaction by purified AtUSP (45ĆĀ°C), while the optimal pH value and metal ion conditions are close to those of the purified enzyme system
additional information
UDP-sugar pyrophosphorylase from Hordeum vulgare, with favorable biochemical properties like broad pH and temperature tolerances as well as a broad substrate spectrum and high synthesis stability, is used for efficient synthesis of nucleotide sugars under conditions optimized by high-through-put multiplexed capillary electrophoresis analysis in combination with a galactokinase UDP-alpha-D-galactose (UDP-Gal). Assay optimization, overview
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
purified recombinant His-taged enzyme, residual activity of HvUSP after 88 h is 46%
additional information
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4ĆĀ°C, purified recombinant His-taged enzyme, HvUSP shows a high storage stability over 31 days
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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)
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
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3)pLysS by nickel affinity chromatography and gel filtration
recombinant His-tagged enzyme from Escherichia coli strain T7 Express by nickel affinity chromatography and ultrafiltration
recombinant His6-biotin-tagged enzyme from Escherichia coli strain BL21(DE3) by affinity chromatography, tag cleavage via TEV protease, and dialysis
using Ni-NTA chromatography
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli as a His-tagged fusion protein
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
gene hvusp, identified due to a BLAST search using the gene psusp from Pisum sativum as template, recombinant expression of C-terminally His-tagged enzyme best in Escherichia coli strain T7 Express, several Escherichia coli strains are tested
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
gene USP, functional UDP-sugar diphosphorylase from Arabidopsis thaliana is constitutively expressed in Pichia pastoris strain SMD1168H and secreted into the extracellular medium using the secretion signal from Saccharomyces cerevisiae alpha-factor prepro-peptide
gene USP, recombinant expression of His6-biotin-tagged enzyme in Escherichia coli strain BL21(DE3)
His-tagged thioredoxin fusion protein expressed in Escherichia coli BL21gold strain
into the vector pET22b for expression in Escherichia coli BL21DE3 cells
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
synthesis
in mammals, uridine 5'-diphosphate-glucose (UDP-Glc) and uridine 5'-diphosphate-glucuronic acid (UDP-GlcA) are common building blocks of glycans and glycoconjugates. The commercial demand for these high-energy donors is increasing. To produce valuable UDP-GlcA in a cost-effective way, UDP-sugar pyrophosphorylase from Arabidopsis thaliana is constitutively expressed in Pichia pastoris and secreted into the extracellular medium. The synthesis of 4.2 g UDP-GlcA or 5.5 g UDP-Glc per liter of culture is revealed in the culture medium, without any need for purification. An anion exchange chromatography purification method for UDP-sugars is also developed. This route opens a door to large-scale production of the cheaper UDP-GlcA
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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 (Q5W915), Pisum sativum
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 (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, Trypanosoma cruzi (D3YBH2)
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), 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
Zang, L.; Du, R.; Zang, H.; Wang, F.; Sheng, J.
Production of Arabidopsis thaliana UDP-sugar pyrophosphorylase by Pichia pastoris and its application in efficient UDP-Glucose and UDP-glucuronic acid synthesis
Appl. Biochem. Microbiol.
55
631-638
2019
Arabidopsis thaliana (Q9C5I1)
-
brenda
Wahl, C.; Spiertz, M.; Elling, L.
Characterization of a new UDP-sugar pyrophosphorylase from Hordeum vulgare (barley)
J. Biotechnol.
258
51-55
2017
Hordeum vulgare subsp. vulgare (F2DQG9)
brenda
Prakash, O.; Fuehring, J.; Post, J.; Shepherd, S.M.; Eadsforth, T.C.; Gray, D.; Fedorov, R.; Routier, F.H.
Identification of Leishmania major UDP-sugar pyrophosphorylase inhibitors using biosensor-based small molecule fragment library screening
Molecules
24
996
2019
Leishmania major (Q4QE75)
brenda
Select items on the left to see more content.
EXTERNAL LINKS (specific for EC-Number 2.7.7.64)
html completed
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
About BRENDA
Help
Download
Contribution
member of
curated at
curated at
Server: brenda5 Ver: 9edf756-main (2022-05-17 10:30:03 +0200)