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
3.6.1.45
-
RECOMMENDED NAME
GeneOntology No.
UDP-sugar diphosphatase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
UDP-sugar + H2O = UMP + alpha-D-aldose 1-phosphate
show the reaction diagram
-
-
-
-
UDP-sugar + H2O = UMP + alpha-D-aldose 1-phosphate
show the reaction diagram
UDP-sugar is the best substrate, although other nucleoside-sugar diphosphates are used as substrates with similar Km values but much lower maximum velocities
-, Q9RQT7
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
hydrolysis of diphosphate bonds
-
-
-
-
hydrolysis of phosphoric ester
-, Q9RQT7
-
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.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5'-nucleotidase/UDP-sugar hydrolase
-
-
5'-nucleotidase/UDP-sugar hydrolase
A4URQ8
-
5'-nucleotidase/UDP-sugar hydrolase
Yersinia intermedia CECT 7230
A4URQ8
-
-
hydrolase, uridine diphosphoglucose (Escherichia coli precursor reduced)
-
-
-
-
hydrolase, uridine diphosphoglucose (Escherichia coli reduced)
-
-
-
-
hydrolase, uridine diphosphoglucose (Salmonella typhimurium clone pAGS5 gene ushB isoenzyme reduced)
-
-
-
-
hydrolase, uridine diphosphoglucose (Salmonella typhimurium gene ushA0 isoenzyme precursor reduced)
-
-
-
-
hydrolase, uridine diphosphoglucose (Salmonella typhimurium gene ushA0 isoenzyme reduced)
-
-
-
-
nucleosidediphosphate-sugar diphosphatase
-
-
-
-
nucleosidediphosphate-sugar pyrophosphatase
-
-
-
-
Nudix hydrolase-like nucleotide hydrolase
-
-
toxin A
Clostridium difficile
-
-
toxin B
Clostridium difficile
-
-
UDP-glucose pyrophosphatase
-
-
UDP-glucose pyrophosphatase
Q9D142
-
UDP-glucose pyrophosphatase
-
-
UDP-sugar diphosphatase
-
-
-
-
UDP-sugar hydrolase
-
-
-
-
UDP-sugar hydrolase
Q9RQT7
-
UDP-sugar pyrophosphatase
-
-
-
-
UDPG pyrophosphatase
-
-
UGPPase
-
-
UGPPase
Q9D142
-
UGPPase
-
-
UshA
-
secreted enzyme with UDP-sugar hydrolase and 5' nucleotidase activities
UshA
-
bifunctional enzyme with UDP-sugar hydrolase and 5' nucleotidase activity
UshA
A4URQ8
-
UshA
Yersinia intermedia CECT 7230
A4URQ8
-
-
UshB protein
-
-
CAS REGISTRY NUMBER
COMMENTARY
103716-25-2
-, hydrolase, uridine diphosphoglucose (Escherichia coli precursor reduced)
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
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
Clostridium difficile
2 different enzyme forms: toxin A and toxin B
-
-
Manually annotated by BRENDA team
strain ATCC 13032, expression is phosphate starvation inducible
-
-
Manually annotated by BRENDA team
strain IFO 12010, gene ushA
UniProt
Manually annotated by BRENDA team
ATCC 12793
-
-
Manually annotated by BRENDA team
encoded by the gene ushA, that is nonhomologous to the gene ushB, that encodes the enzyme from Salmonella typhimurium. Escherichia coli also contains a silent allel of the ushB gene, i.e. ushB0
-
-
Manually annotated by BRENDA team
gene ushA
-
-
Manually annotated by BRENDA team
K12 TG1 and K12 5A-1 strains
-
-
Manually annotated by BRENDA team
gene UGPP
Uniprot
Manually annotated by BRENDA team
encoded by the gene ushB, that is nonhomologous to the gene ushA, that encodes the enzyme from Escherichia coli. Salmonella typhimurium also contains a silent allel of the gene ushA, i.e. ushA0; Salmonella enterica serotype typhimurium
-
-
Manually annotated by BRENDA team
strain CECT 7230, gene ushA
UniProt
Manually annotated by BRENDA team
Yersinia intermedia CECT 7230
strain CECT 7230, gene ushA
UniProt
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ADP-D-ribose + H2O
AMP + alpha-D-ribose 1-phosphate
show the reaction diagram
-, Q9D142
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
-, O95848
15% of the activity with UDP-glucose
-
-
?
ADP-glucose + H2O
AMP + alpha-D-glucose 1-phosphate
show the reaction diagram
-
20% of the activity with UDP-glucose
-
-
?
ADP-ribose + H2O
AMP + alpha-D-ribose 1-phosphate
show the reaction diagram
-
95% of the activity with UDP-glucose
-
-
?
ADP-ribose + H2O
AMP + alpha-D-ribose 1-phosphate
show the reaction diagram
-, O95848
best substrate, 130% of the activity with UDP-glucose
-
-
?
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
-
2% of the activity with UDP-glucose
-
-
?
CDP-glucose + H2O
CMP + alpha-D-glucose 1-phosphate
show the reaction diagram
-, O95848
3% of the activity with UDP-glucose
-
-
?
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
-, O95848
10% of the activity with UDP-glucose
-
-
?
NDP + H2O
NMP + 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
UMP + glucose 1-phosphate
show the reaction diagram
Clostridium difficile
-
-
-
-
-
UDP-D-glucose + H2O
UMP + alpha-D-glucose 1-phosphate
show the reaction diagram
-, Q9D142
-
-
-
?
UDP-galactose
UMP + galactose 1-phosphate
show the reaction diagram
-
-
-
-
UDP-glucose + H2O
UMP + alpha-D-glucose 1-phosphate
show the reaction diagram
-
-
-
-
?
UDP-glucose + H2O
UMP + alpha-D-glucose 1-phosphate
show the reaction diagram
-, O95848
-
-
-
?
UDP-glucose + H2O
UMP + alpha-D-glucose 1-phosphate
show the reaction diagram
A4URQ8, -
-
-
-
?
UDP-glucose + H2O
UMP + alpha-D-glucose 1-phosphate
show the reaction diagram
A4URQ8, -
-
products are uridine, phosphate and D-glucose 1-phosphate. The phosphoanhydride and the nucleoside 5'-ester linkages are hydrolyzed without detectable signs of nucleoside monophosphate as an intermediate, possibly because it is hydrolyzed as soon as it is formed without leaving the active center
-
?
UDP-glucose + H2O
UMP + alpha-D-glucose 1-phosphate
show the reaction diagram
-
best substrate
-
-
?
UDP-glucose + H2O
UMP + alpha-D-glucose 1-phosphate
show the reaction diagram
-, O95848
hydrolysis of the precursor molecule of numerous glycosylation reactions in animals, to produce glucose 1-phosphate and UMP
-
-
?
UDP-glucose + H2O
UMP + alpha-D-glucose 1-phosphate
show the reaction diagram
-
hydrolysis of the precursor molecule of numerous glycosylation reactions in animals, to produce glucose 1-phosphate and UMP
-
-
?
UDP-glucose + H2O
UMP + alpha-D-glucose 1-phosphate
show the reaction diagram
-
UshA protein, with 5'-nucleotidase and UDP-sugar hydrolase activities, is required for growth on AMP or UDP-glucose as sole sources of phosphorus
-
-
?
UDP-glucose + H2O
UMP + alpha-D-glucose 1-phosphate
show the reaction diagram
Yersinia intermedia CECT 7230
A4URQ8
-
-, products are uridine, phosphate and D-glucose 1-phosphate. The phosphoanhydride and the nucleoside 5'-ester linkages are hydrolyzed without detectable signs of nucleoside monophosphate as an intermediate, possibly because it is hydrolyzed as soon as it is formed without leaving the active center
-
?
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
-
-
-
-
GDP-glucose + H2O
GMP + alpha-D-glucose 1-phosphate
show the reaction diagram
-
10% of the activity with UDP-glucose
-
-
?
additional information
?
-
-
the enzyme has 5'-nucleotidase activity
-
-
-
additional information
?
-
-
the enzyme shows UDP-sugar hydrolase EC 3.6.1.45, dinucleoside-polyphosphate hydrolase, CDP-alcohol hydrolase EC 3.6.1.53, and 5'-nucleosidase activities EC 3.1.3.5, it has a variety of activities and structure-function relationships, substrate specificity, overview
-
-
-
additional information
?
-
A4URQ8, -
the enzyme shows UDP-sugar hydrolase EC 3.6.1.45, dinucleoside-polyphosphate hydrolase, CDP-alcohol hydrolase EC 3.6.1.53, and 5'-nucleosidase activities EC 3.1.3.5, it has a variety of activities and structure-function relationships, substrate specificity, overview
-
-
-
additional information
?
-
Yersinia intermedia CECT 7230
A4URQ8
the enzyme shows UDP-sugar hydrolase EC 3.6.1.45, dinucleoside-polyphosphate hydrolase, CDP-alcohol hydrolase EC 3.6.1.53, and 5'-nucleosidase activities EC 3.1.3.5, it has a variety of activities and structure-function relationships, substrate specificity, overview
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
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
A4URQ8, -
-
-
-
?
UDP-glucose + H2O
UMP + alpha-D-glucose 1-phosphate
show the reaction diagram
-, O95848
hydrolysis of the precursor molecule of numerous glycosylation reactions in animals, to produce glucose 1-phosphate and UMP
-
-
?
UDP-glucose + H2O
UMP + alpha-D-glucose 1-phosphate
show the reaction diagram
-
hydrolysis of the precursor molecule of numerous glycosylation reactions in animals, to produce glucose 1-phosphate and UMP
-
-
?
UDP-glucose + H2O
UMP + alpha-D-glucose 1-phosphate
show the reaction diagram
-
UshA protein, with 5'-nucleotidase and UDP-sugar hydrolase activities, is required for growth on AMP or UDP-glucose as sole sources of phosphorus
-
-
?
UDP-glucose + H2O
UMP + alpha-D-glucose 1-phosphate
show the reaction diagram
Yersinia intermedia CECT 7230
A4URQ8
-
-
-
?
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
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+
Clostridium difficile
-
absolute requirement for K+
Mg2+
-
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
Mg2+
Clostridium difficile
-
divalent metal ion required, significantly lower Km in presence of Mn2+ as compared with Mg2+
Mg2+
-, O95848
-
Mg2+
-
absolutely required for optimal activity, not replacable by Mn2+
Mg2+
A4URQ8, -
-
Mg2+
-, Q9D142
activity is dependent on the presence of Mg2+
Mn2+
-
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
Mn2+
Clostridium difficile
-
divalent metal ion required, significantly lower Km in presence of Mn2+ as compared with Mg2+
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
ADP-D-glucose
-
competitive
CDP-D-glucose
-
competitive
EDTA
Clostridium difficile
-
-
EDTA
-
complete inhibition at 1 mM
GDP-D-glucose
-
competitive
Inhibitor from E. coli
-
-
-
Inhibitor from Salmonella typhimurium cytoplasm
-
-
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.3
-
ADP-D-ribose
-, Q9D142
in 50 mM Tris-HCl, pH 8.0, 10 mM Mg2+, at 37C
0.33
-
CDP-D-glucose
-
-
0.11
-
GDP-D-glucose
-
-
0.002
-
UDP-D-glucose
-
with 5 mM CoSO4, pH 8.0, 37 C
0.02
-
UDP-D-glucose
-
with 5 mM CoSO4, pH 8.0, 37 C
0.2
-
UDP-D-glucose
-
with 5 mM MgCl2, pH 8.0, 25 C
4.1
-
UDP-D-glucose
-, Q9D142
in 50 mM Tris-HCl, pH 8.0, 10 mM MgCl2, at 37C
0.0096
-
UDP-glucose
A4URQ8, -
pH 7.5, 37C
0.0104
-
UDP-glucose
-
pH 7.5, 37C
0.0894
-
UDP-glucose
Clostridium difficile
-
with MnCl2
0.1215
-
UDP-glucose
Clostridium difficile
-
isozyme toxin A, with MnCl2
0.1423
-
UDP-glucose
Clostridium difficile
-
isozyme toxin A, with MgCl2 and 150 mM KCl
0.1435
-
UDP-glucose
Clostridium difficile
-
isozyme toxin A, with 50 mM KCl
0.1574
-
UDP-glucose
Clostridium difficile
-
isozyme toxin B, with 50 mM KCl
0.1638
-
UDP-glucose
Clostridium difficile
-
isozyme toxin A, with 500 mM KCl
0.1735
-
UDP-glucose
Clostridium difficile
-
isozyme toxin B, with 500 mM KCl
0.1755
-
UDP-glucose
Clostridium difficile
-
isozyme toxin B, with MgCl2 and 150 mM KCl
additional information
-
additional information
-
-
-
additional information
-
additional information
-
kinetics of all the enzyme activites, overview
-
additional information
-
additional information
A4URQ8, -
kinetics of all the enzyme activites, overview
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
71
-
UDP-glucose
-
pH 7.5, 37C
97
-
UDP-glucose
A4URQ8, -
pH 7.5, 37C
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
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
12.58
-
-
-
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
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
7.5
-
-
assay at
7.5
-
A4URQ8, -
assay at
7.8
8
Clostridium difficile
-
-
8
9.5
-
with substrate UDP-glucose
9
-
-, O95848
assay at
9
-
-, Q9D142
-
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
8
9.5
-, Q9D142
-
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
37
40
Clostridium difficile
-
-
37
-
-
assay at
37
-
A4URQ8, -
assay at
pI VALUE
pI VALUE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4.7
-
-
isoelectric focusing
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
A4URQ8, -
the CDP-hydrolase activity is released on Triton X-100-containing medium. Growth at 25C is deemed optimum in terms of the enzyme-activity yield
Manually annotated by BRENDA team
Yersinia intermedia CECT 7230
-
the CDP-hydrolase activity is released on Triton X-100-containing medium. Growth at 25C is deemed optimum in terms of the enzyme-activity yield
-
Manually annotated by BRENDA team
-, Q9D142
-
Manually annotated by BRENDA team
-, Q9D142
-
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
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
-
inner and outer. 90% of the activity is located in the inner membrane
-
Manually annotated by BRENDA team
-
inner membrane associated enzyme contains an N-terminal signal peptide that serves to anchor the UshB protein in the inner membrane. The enzyme has an 'N-terminus inside/C-terminus outside' membrane orientation consistent with a role in the degradation of external substrates
-
Manually annotated by BRENDA team
-
wild-type expressed in Escherichia coli TG1 and 5A-1
-
Manually annotated by BRENDA team
-
100000 x g supernatant from kidney
-
Manually annotated by BRENDA team
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
50000
60000
-
gel filtration
52000
-
A4URQ8, -
gel filtration
54000
-
-, Q9D142
SDS-PAGE
70000
-
-
SDS-PAGE of supernatant of phosphate-starved cells
70460
-
-
MALDI-TOF mass spectrometry
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 60767, calculation from nucleotide sequence
?
-
x * 28349, calculation from nucleotide sequence
?
-
x * 60750, calculation from nucleotide sequence
?
-
x * 61000, SDS-PAGE
?
A4URQ8, -
x * 63000, band 1, SDS-PAGE, x * 23000, band 2, SDS-PAGE
?
Yersinia intermedia CECT 7230
-
x * 63000, band 1, SDS-PAGE, x * 23000, band 2, SDS-PAGE
-
homodimer
-
2 * 28000, SDS-PAGE
homodimer
-, Q9D142
2 * 26700, calculated from amino acid sequence; 2 * 30000, SDS-PAGE
additional information
-, O95848
amino acid sequence comparisons, overview
additional information
A4URQ8, -
UshA peptide mass fingerprint, overview
additional information
Yersinia intermedia CECT 7230
-
UshA peptide mass fingerprint, overview
-
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
additional information
-
-
Co2+, Mn2+ or Mg2+ protect against heat inactivation
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
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
-, O95848
Ni-NTA resin column chromatography
-, Q9D142
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
-
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
A4URQ8, -
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
overexpressed in Corynebacterium glutamicum
-
DNA and amino acid sequence determination and analysis, functional overexpression in Escherichia coli
-, Q9RQT7
from the gene ushA
-
gene ushA, overexpression of the enzyme
-
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
-
gene UGPP, overexpression in Escherichia coli strain AD494(DE3), subcloning in strain JM109
-, O95848
expressed in Escherichia coli BL21 (DE3) cells
-, Q9D142
gene ushA, DNA and amino acid sequence determination and analysis, expression analysis by RT-PCR
A4URQ8, -
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
F463L
-
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
-
carboxyterminal deletion which abolishes the 5' nucleotidase activity and deletion of the signal peptide; deletion of the signal peptide, identical to the mature periplasmic enzyme, except for the presence of an N-terminal methionine residue, expressed in Escherichia coli 5A-1
additional information
-
ushA knockouts are unable to grow on AMP as the only carbon source and are significantly delayed or impaired in their growth on other purine nucleotides. Growth on nonadenine purine nucleotides is made possible by an acid phosphatase encoded by the aphA gene, which at neutral pH acts as an efficient 5'-nucleotidase of purine nucleotides, except AMP. Double knockouts in ushA and aphA do not grow on nucleotides AMP