Information on EC 3.6.1.45 - UDP-sugar diphosphatase

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

EC NUMBER
COMMENTARY hide
3.6.1.45
-
RECOMMENDED NAME
GeneOntology No.
UDP-sugar diphosphatase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
UDP-sugar + H2O = UMP + alpha-D-aldose 1-phosphate
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of diphosphate bonds
-
-
-
-
hydrolysis of phosphoric ester
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SYSTEMATIC NAME
IUBMB Comments
UDP-sugar sugarphosphohydrolase
A divalent cation is required for activity. UDP-sugar is the best substrate, although other nucleoside-sugar diphosphates are used as substrates with similar Km values but much lower maximum velocities. Thus, this enzyme has a specificity distinct from that of ADP-sugar diphosphatase (EC 3.6.1.21). Some but not all enzymes of this class also appear to have 5'-nucleotidase (see EC 3.1.3.5) activity.
CAS REGISTRY NUMBER
COMMENTARY hide
103716-25-2
-
103716-25-2
hydrolase, uridine diphosphoglucose (Escherichia coli precursor reduced)
103716-26-3
-
103716-26-3
hydrolase, uridine diphosphoglucose (Escherichia coli reduced)
106528-92-1
hydrolase, uridine diphosphoglucose (Salmonella typhimurium gene ushA0 isoenzyme precursor reduced)
106528-93-2
hydrolase, uridine diphosphoglucose (Salmonella typhimurium gene ushA0 isoenzyme reduced)
127497-57-8
hydrolase, uridine diphosphoglucose (Salmonella typhimurium clone pAGS5 gene ushB isoenzyme reduced)
57127-20-5
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain ATCC 13032, expression is phosphate starvation inducible
-
-
Manually annotated by BRENDA team
strain IFO 12010, gene ushA
UniProt
Manually annotated by BRENDA team
-
Uniprot
Manually annotated by BRENDA team
gene UGPP
Uniprot
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
2 different enzyme forms: toxin A and toxin B
-
-
Manually annotated by BRENDA team
yeast
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
strain CECT 7230, gene ushA
UniProt
Manually annotated by BRENDA team
strain CECT 7230, gene ushA
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
ADP-D-ribose + H2O
AMP + alpha-D-ribose 1-phosphate
show the reaction diagram
based on Vmax/Km values, the enzyme is about 20fold more active toward ADP-D-ribose as compared to UDP-D-glucose
-
-
?
ADP-glucose + H2O
AMP + alpha-D-glucose 1-phosphate
show the reaction diagram
ADP-ribose + H2O
AMP + alpha-D-ribose 1-phosphate
show the reaction diagram
AMP + H2O
adenosine + phosphate
show the reaction diagram
CDP-D-glucose
CMP + glucose 1-phosphate
show the reaction diagram
-
at 5% of the activity with UDP-glucose
-
-
-
CDP-glucose + H2O
CMP + alpha-D-glucose 1-phosphate
show the reaction diagram
GDP-glucose
GMP + glucose 1-phosphate
show the reaction diagram
-
at 5% of the activity with UDP-glucose
-
-
-
GDP-glucose + H2O
GMP + alpha-D-glucose 1-phosphate
show the reaction diagram
NAD+ + H2O
AMP + NMN
show the reaction diagram
NADH + H2O
NMNH + AMP
show the reaction diagram
NDP + H2O
NMP + phosphate
show the reaction diagram
-
-
-
-
?
NMN + H2O
nicotinamide riboside + phosphate
show the reaction diagram
NTP + H2O
NDP + phosphate
show the reaction diagram
-
-
-
-
?
UDP-D-glucose
UMP + glucose 1-phosphate
show the reaction diagram
UDP-D-glucose + H2O
UMP + alpha-D-glucose 1-phosphate
show the reaction diagram
-
-
-
?
UDP-galactose
UMP + galactose 1-phosphate
show the reaction diagram
-
-
-
-
UDP-glucose + H2O
UMP + alpha-D-glucose 1-phosphate
show the reaction diagram
UDP-N-acetyl-D-galactosamine
UMP + N-acetyl-D-galactosamine 1-phosphate
show the reaction diagram
-
-
-
-
UDP-N-acetyl-D-glucosamine
UMP + N-acetyl-D-glucosamine 1-phosphate
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
NTP + H2O
NDP + phosphate
show the reaction diagram
-
-
-
-
?
UDP-glucose + H2O
UMP + alpha-D-glucose 1-phosphate
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Co2+
-
absolute requirement for a divalent cation, at pH 8.0 in Tris-HCl buffer the requirement can be satisfied in order of decreasing affinity by Co2+, Mn2+, Mg2+. At pH 5.1 in acetate buffer only Co2+ and Mn2+ are effective
K+
-
absolute requirement for K+
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ADP-D-glucose
-
competitive
CDP-D-glucose
-
competitive
erythrosine B
-
-
GDP-D-glucose
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competitive
Inhibitor from E. coli
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-
-
Inhibitor from Salmonella typhimurium cytoplasm
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.3
ADP-D-ribose
in 50 mM Tris-HCl, pH 8.0, 10 mM Mg2+, at 37C
0.0012
AMP
pH 7.5, 30C
0.33
CDP-D-glucose
-
-
0.11
GDP-D-glucose
-
-
0.25
MgATP2-
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-
0.0053
NAD+
pH 7.5, 30C
0.007
NADH
pH 7.5, 30C
0.0111
NMN
pH 7.5, 30C
0.002 - 4.1
UDP-D-glucose
0.0096 - 0.1755
UDP-glucose
additional information
additional information
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
405
AMP
Escherichia coli
P07024
pH 7.5, 30C
19.3
NAD+
Escherichia coli
P07024
pH 7.5, 30C
10
NADH
Escherichia coli
P07024
pH 7.5, 30C
1492
NMN
Escherichia coli
P07024
pH 7.5, 30C
71 - 97
UDP-glucose
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
334000
AMP
Escherichia coli
P07024
pH 7.5, 30C
30
3700
NAD+
Escherichia coli
P07024
pH 7.5, 30C
7
1400
NADH
Escherichia coli
P07024
pH 7.5, 30C
8
135000
NMN
Escherichia coli
P07024
pH 7.5, 30C
775
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.076
-
endogenous UDP-sugar hydrolase activity 24 hours after the onset of phosphate starvation
0.55
-
UDP-sugar hydrolase activity of overexpressed UshA enzyme
additional information
-
endogenous UDP-sugar hydrolase activity not detectable before the shift to phosphate-free medium; UDP-sugar hydrolase activity detectable in cell extracts of phosphate-starved wild-type delta-ushA cells
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8 - 9.5
-
with substrate UDP-glucose
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
-
assay at
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.7
-
isoelectric focusing
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
enzyme lacking signal sequence except for that encoding the initiating methionine residue, expressed in Escherichia coli 5A-1
Manually annotated by BRENDA team
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100000 x g supernatant from kidney
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Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
UNIPROT
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50000 - 60000
-
gel filtration
52000
gel filtration
54000
SDS-PAGE
70000
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SDS-PAGE of supernatant of phosphate-starved cells
70460
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MALDI-TOF mass spectrometry
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
additional information
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
Co2+, Mn2+ or Mg2+ protect against heat inactivation
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
native enzyme from kineys by anion exchange chromatography, hydroxyapatite and again anion exchange chromatography, gel filtration, another different step of anion exchange and finally cation exchange chromatography followed by native PAGE
native enzyme over 20000fold from kidneys by anion exchange chromatography, hydroxyapatite and again anion exchange chromatography, gel filtration, another different step of anion exchange and finally cation exchange chromatography followed by native PAGE
-
Ni-NTA resin column chromatography
partial
UshA from suspension cell culture by gel filtration, dialysis, and anion exchange chromatography for enzyme characterization, and also by another adsorption chromatography step for peptide mass fingerprinting
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination and analysis, functional overexpression in Escherichia coli
expressed in Escherichia coli BL21 (DE3) cells
from the gene ushA
-
gene UGPP, overexpression in Escherichia coli strain AD494(DE3), subcloning in strain JM109
gene ushA, DNA and amino acid sequence determination and analysis, expression analysis by RT-PCR
gene ushA, overexpression of the enzyme
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overexpressed in Corynebacterium glutamicum
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overexpression of wild-type and mutant UshA enzyme lacking signal peptide in Escherichia coli 5A-1, UshA lacking the signal peptide is an active cytoplasmic 5' nucleotidase which causes conditional lethality
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
F463L
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enhanced 5' nucleotidase activity, UDP-sugar hydrolase activity not determined
S139Y
-
occurs naturally, loss of 5' nucleotidase activity, UDP-sugar hydrolase activity not determined
S139Y/F463Y
-
loss of 5' nucleotidase activity, UDP-sugar hydrolase activity not determined
additional information
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